human fgf23 Search Results


fgf23  (R&D Systems)
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R&D Systems fgf23
Figure 1. A novel kidney-specific protein regulates Pi homeostasis. siRNA library screening identified that the TMEM174 gene regulates Pi uptake in cells expressing NPT2A. (A) siRNA knockdown efficiency, (B) total Pi uptake, and (C) levels of NPT2A protein. Human renal tubular cells expressing NPT2A were treated with 20 nM siRNA and then with <t>FGF23</t> (10 nM) in the presence of 100 ng/ml secretory KL and 2 mg/ml heparin for 1 hour. (D) TMEM174 and NPT2A protein expression in human proximal tubular cells treated with 20 nM TMEM174 siRNA and then treated with FGF23 (10 nM) for 1–4 hours in the presence of 100 ng/ml secretory KL, 2 mg/ml heparin, and 0.1% BSA. Flarebio and Novus TMEM174 antibodies were used for human proximal tubular cells. The asterisk (*) represents nonspecific protein signal. (E) TMEM174 and NPT2A protein expression in OK-P cells treated with 20 nM TMEM174 siRNA and then with PTH (10 nM) for 1–4 hours in the presence of 0.1% BSA. Biomatik TMEM174 antibody was used for OK-P cells. Statistical analysis was performed using a one-way ANOVA. The experiments were repeated three times. ***P,0.001, **P,0.01 (ver- sus Scr1FGF23), #P,0.05 (versus Scr-FGF23).
Fgf23, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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rhfgf23  (R&D Systems)
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R&D Systems rhfgf23
Figure 1. A novel kidney-specific protein regulates Pi homeostasis. siRNA library screening identified that the TMEM174 gene regulates Pi uptake in cells expressing NPT2A. (A) siRNA knockdown efficiency, (B) total Pi uptake, and (C) levels of NPT2A protein. Human renal tubular cells expressing NPT2A were treated with 20 nM siRNA and then with <t>FGF23</t> (10 nM) in the presence of 100 ng/ml secretory KL and 2 mg/ml heparin for 1 hour. (D) TMEM174 and NPT2A protein expression in human proximal tubular cells treated with 20 nM TMEM174 siRNA and then treated with FGF23 (10 nM) for 1–4 hours in the presence of 100 ng/ml secretory KL, 2 mg/ml heparin, and 0.1% BSA. Flarebio and Novus TMEM174 antibodies were used for human proximal tubular cells. The asterisk (*) represents nonspecific protein signal. (E) TMEM174 and NPT2A protein expression in OK-P cells treated with 20 nM TMEM174 siRNA and then with PTH (10 nM) for 1–4 hours in the presence of 0.1% BSA. Biomatik TMEM174 antibody was used for OK-P cells. Statistical analysis was performed using a one-way ANOVA. The experiments were repeated three times. ***P,0.001, **P,0.01 (ver- sus Scr1FGF23), #P,0.05 (versus Scr-FGF23).
Rhfgf23, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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intact fgf 23  (R&D Systems)
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R&D Systems intact fgf 23
Figure 1. A novel kidney-specific protein regulates Pi homeostasis. siRNA library screening identified that the TMEM174 gene regulates Pi uptake in cells expressing NPT2A. (A) siRNA knockdown efficiency, (B) total Pi uptake, and (C) levels of NPT2A protein. Human renal tubular cells expressing NPT2A were treated with 20 nM siRNA and then with <t>FGF23</t> (10 nM) in the presence of 100 ng/ml secretory KL and 2 mg/ml heparin for 1 hour. (D) TMEM174 and NPT2A protein expression in human proximal tubular cells treated with 20 nM TMEM174 siRNA and then treated with FGF23 (10 nM) for 1–4 hours in the presence of 100 ng/ml secretory KL, 2 mg/ml heparin, and 0.1% BSA. Flarebio and Novus TMEM174 antibodies were used for human proximal tubular cells. The asterisk (*) represents nonspecific protein signal. (E) TMEM174 and NPT2A protein expression in OK-P cells treated with 20 nM TMEM174 siRNA and then with PTH (10 nM) for 1–4 hours in the presence of 0.1% BSA. Biomatik TMEM174 antibody was used for OK-P cells. Statistical analysis was performed using a one-way ANOVA. The experiments were repeated three times. ***P,0.001, **P,0.01 (ver- sus Scr1FGF23), #P,0.05 (versus Scr-FGF23).
Intact Fgf 23, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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human fgf23  (R&D Systems)
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R&D Systems human fgf23
Figure 1. A novel kidney-specific protein regulates Pi homeostasis. siRNA library screening identified that the TMEM174 gene regulates Pi uptake in cells expressing NPT2A. (A) siRNA knockdown efficiency, (B) total Pi uptake, and (C) levels of NPT2A protein. Human renal tubular cells expressing NPT2A were treated with 20 nM siRNA and then with <t>FGF23</t> (10 nM) in the presence of 100 ng/ml secretory KL and 2 mg/ml heparin for 1 hour. (D) TMEM174 and NPT2A protein expression in human proximal tubular cells treated with 20 nM TMEM174 siRNA and then treated with FGF23 (10 nM) for 1–4 hours in the presence of 100 ng/ml secretory KL, 2 mg/ml heparin, and 0.1% BSA. Flarebio and Novus TMEM174 antibodies were used for human proximal tubular cells. The asterisk (*) represents nonspecific protein signal. (E) TMEM174 and NPT2A protein expression in OK-P cells treated with 20 nM TMEM174 siRNA and then with PTH (10 nM) for 1–4 hours in the presence of 0.1% BSA. Biomatik TMEM174 antibody was used for OK-P cells. Statistical analysis was performed using a one-way ANOVA. The experiments were repeated three times. ***P,0.001, **P,0.01 (ver- sus Scr1FGF23), #P,0.05 (versus Scr-FGF23).
Human Fgf23, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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283511 r d systems goat polyclonal antihuman mouse fgf23 b n  (R&D Systems)
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R&D Systems 283511 r d systems goat polyclonal antihuman mouse fgf23 b n
Figure 1. A novel kidney-specific protein regulates Pi homeostasis. siRNA library screening identified that the TMEM174 gene regulates Pi uptake in cells expressing NPT2A. (A) siRNA knockdown efficiency, (B) total Pi uptake, and (C) levels of NPT2A protein. Human renal tubular cells expressing NPT2A were treated with 20 nM siRNA and then with <t>FGF23</t> (10 nM) in the presence of 100 ng/ml secretory KL and 2 mg/ml heparin for 1 hour. (D) TMEM174 and NPT2A protein expression in human proximal tubular cells treated with 20 nM TMEM174 siRNA and then treated with FGF23 (10 nM) for 1–4 hours in the presence of 100 ng/ml secretory KL, 2 mg/ml heparin, and 0.1% BSA. Flarebio and Novus TMEM174 antibodies were used for human proximal tubular cells. The asterisk (*) represents nonspecific protein signal. (E) TMEM174 and NPT2A protein expression in OK-P cells treated with 20 nM TMEM174 siRNA and then with PTH (10 nM) for 1–4 hours in the presence of 0.1% BSA. Biomatik TMEM174 antibody was used for OK-P cells. Statistical analysis was performed using a one-way ANOVA. The experiments were repeated three times. ***P,0.001, **P,0.01 (ver- sus Scr1FGF23), #P,0.05 (versus Scr-FGF23).
283511 R D Systems Goat Polyclonal Antihuman Mouse Fgf23 B N, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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human fgf 23 elisa kit  (Elabscience Biotechnology)
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Elabscience Biotechnology human fgf 23 elisa kit
Figure 1. A novel kidney-specific protein regulates Pi homeostasis. siRNA library screening identified that the TMEM174 gene regulates Pi uptake in cells expressing NPT2A. (A) siRNA knockdown efficiency, (B) total Pi uptake, and (C) levels of NPT2A protein. Human renal tubular cells expressing NPT2A were treated with 20 nM siRNA and then with <t>FGF23</t> (10 nM) in the presence of 100 ng/ml secretory KL and 2 mg/ml heparin for 1 hour. (D) TMEM174 and NPT2A protein expression in human proximal tubular cells treated with 20 nM TMEM174 siRNA and then treated with FGF23 (10 nM) for 1–4 hours in the presence of 100 ng/ml secretory KL, 2 mg/ml heparin, and 0.1% BSA. Flarebio and Novus TMEM174 antibodies were used for human proximal tubular cells. The asterisk (*) represents nonspecific protein signal. (E) TMEM174 and NPT2A protein expression in OK-P cells treated with 20 nM TMEM174 siRNA and then with PTH (10 nM) for 1–4 hours in the presence of 0.1% BSA. Biomatik TMEM174 antibody was used for OK-P cells. Statistical analysis was performed using a one-way ANOVA. The experiments were repeated three times. ***P,0.001, **P,0.01 (ver- sus Scr1FGF23), #P,0.05 (versus Scr-FGF23).
Human Fgf 23 Elisa Kit, supplied by Elabscience Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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recombinant human rh fgf23  (R&D Systems)
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R&D Systems recombinant human rh fgf23
Figure 1. A novel kidney-specific protein regulates Pi homeostasis. siRNA library screening identified that the TMEM174 gene regulates Pi uptake in cells expressing NPT2A. (A) siRNA knockdown efficiency, (B) total Pi uptake, and (C) levels of NPT2A protein. Human renal tubular cells expressing NPT2A were treated with 20 nM siRNA and then with <t>FGF23</t> (10 nM) in the presence of 100 ng/ml secretory KL and 2 mg/ml heparin for 1 hour. (D) TMEM174 and NPT2A protein expression in human proximal tubular cells treated with 20 nM TMEM174 siRNA and then treated with FGF23 (10 nM) for 1–4 hours in the presence of 100 ng/ml secretory KL, 2 mg/ml heparin, and 0.1% BSA. Flarebio and Novus TMEM174 antibodies were used for human proximal tubular cells. The asterisk (*) represents nonspecific protein signal. (E) TMEM174 and NPT2A protein expression in OK-P cells treated with 20 nM TMEM174 siRNA and then with PTH (10 nM) for 1–4 hours in the presence of 0.1% BSA. Biomatik TMEM174 antibody was used for OK-P cells. Statistical analysis was performed using a one-way ANOVA. The experiments were repeated three times. ***P,0.001, **P,0.01 (ver- sus Scr1FGF23), #P,0.05 (versus Scr-FGF23).
Recombinant Human Rh Fgf23, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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monoclonal anti rat fgf23 antibody  (R&D Systems)
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Fibroblast growth factor 23 increases mRNA levels of markers of hypertrophy and fibrosis. Rat cardiac myoblast cells (H9c2) were cultured with 0, 50, or 100 ng/mL fibroblast growth factor 3 <t>(FGF23)</t> for 24 h, and mRNA expression levels were analyzed by real-time PCR. (A) Atrial natriuretic factor (ANF) ( n = 6). ** P < 0.05 versus 0 ng/mL. (B) Brain natriuretic peptide (BNP) ( n = 6). * P < 0.01 versus 0 ng/mL. (C) β-myosin heavy chain ( beta MHC ) ( n = 6). ** P < 0.05 versus 0 ng/mL. (D) Alpha smooth muscle actin ( alpha SMA ) ( n = 6). * P < 0.01 versus 0 ng/mL. (E) Collagen I ( n = 6). * P < 0.01 versus 0 ng/mL. (F) FGF23 ( n = 6). * P < 0.01 versus 0 ng/mL. Data were analyzed by one-way analysis of variance.
Monoclonal Anti Rat Fgf23 Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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human fgf23 protein  (R&D Systems)
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Interaction of Klotho-EGFP N614Q with the proteasome and ER-chaperones. ( A ) Scheme of the GFP-TRAP immunoprecipitation followed by mass spectroscopy (MS). HEK239T cells expressing GFP or Klotho-EGFP variants were used. Created with BioRender.com. ( B ) Bar graph illustrating KEGG pathway analysis of proteins exhibiting increased interaction with Klotho-EGFP N614Q compared to Klotho-EGFP WT . ( C ) Heatmap plot of proteins that exhibit enhanced interaction with Klotho-EGFP N614Q associated with protein processing in the ER . The color code indicates a log2-fold change. ( D ) Western blot analysis of proteins co-IPed with Klotho-EGFP variants from lysates of HEK293T cells stably expressing Klotho-EGFP WT or N614Q after GFP-TRAP IP. Samples were probed with antibodies against Klotho, HSPA5, and ERGIC53. Where indicated, cells were treated with 2.5 nM <t>FGF23</t> for 5 min. ( E ) Quantification of the interaction of Klotho-EGFP variants with HSPA5 and ERGIC53; displayed is the relative intensity of HSPA5 or ERGIC53 to KL in %. (n = 4 experiments, mean ± SD, two-sided Student’s t -test. For full-size blots, see .
Human Fgf23 Protein, supplied by R&D Systems, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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systems catalog dy2604 05  (R&D Systems)
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R&D Systems systems catalog dy2604 05
Interaction of Klotho-EGFP N614Q with the proteasome and ER-chaperones. ( A ) Scheme of the GFP-TRAP immunoprecipitation followed by mass spectroscopy (MS). HEK239T cells expressing GFP or Klotho-EGFP variants were used. Created with BioRender.com. ( B ) Bar graph illustrating KEGG pathway analysis of proteins exhibiting increased interaction with Klotho-EGFP N614Q compared to Klotho-EGFP WT . ( C ) Heatmap plot of proteins that exhibit enhanced interaction with Klotho-EGFP N614Q associated with protein processing in the ER . The color code indicates a log2-fold change. ( D ) Western blot analysis of proteins co-IPed with Klotho-EGFP variants from lysates of HEK293T cells stably expressing Klotho-EGFP WT or N614Q after GFP-TRAP IP. Samples were probed with antibodies against Klotho, HSPA5, and ERGIC53. Where indicated, cells were treated with 2.5 nM <t>FGF23</t> for 5 min. ( E ) Quantification of the interaction of Klotho-EGFP variants with HSPA5 and ERGIC53; displayed is the relative intensity of HSPA5 or ERGIC53 to KL in %. (n = 4 experiments, mean ± SD, two-sided Student’s t -test. For full-size blots, see .
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human fgf23 monoclonal antibody  (R&D Systems)
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(A) displays the distribution of post-KT <t>FGF23</t> levels based on the hypertension status. (B) shows that the patients with larger LA volumes had the worst NHYA class.
Human Fgf23 Monoclonal Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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monoclonal mouse anti human fgf23 antibody  (R&D Systems)
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Dependence of the SPRi signal on <t>FGF23</t> antibody concentration. The used concentration of the FGF23-αKlotho complex was 40:169.2 pg/mL; pH = 7.4. “Standard deviation (SD)” was calculated from 12 individual measurements.
Monoclonal Mouse Anti Human Fgf23 Antibody, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Figure 1. A novel kidney-specific protein regulates Pi homeostasis. siRNA library screening identified that the TMEM174 gene regulates Pi uptake in cells expressing NPT2A. (A) siRNA knockdown efficiency, (B) total Pi uptake, and (C) levels of NPT2A protein. Human renal tubular cells expressing NPT2A were treated with 20 nM siRNA and then with FGF23 (10 nM) in the presence of 100 ng/ml secretory KL and 2 mg/ml heparin for 1 hour. (D) TMEM174 and NPT2A protein expression in human proximal tubular cells treated with 20 nM TMEM174 siRNA and then treated with FGF23 (10 nM) for 1–4 hours in the presence of 100 ng/ml secretory KL, 2 mg/ml heparin, and 0.1% BSA. Flarebio and Novus TMEM174 antibodies were used for human proximal tubular cells. The asterisk (*) represents nonspecific protein signal. (E) TMEM174 and NPT2A protein expression in OK-P cells treated with 20 nM TMEM174 siRNA and then with PTH (10 nM) for 1–4 hours in the presence of 0.1% BSA. Biomatik TMEM174 antibody was used for OK-P cells. Statistical analysis was performed using a one-way ANOVA. The experiments were repeated three times. ***P,0.001, **P,0.01 (ver- sus Scr1FGF23), #P,0.05 (versus Scr-FGF23).

Journal: Journal of the American Society of Nephrology

Article Title: Targeted Disruption of a Proximal Tubule–Specific TMEM174 Gene in Mice Causes Hyperphosphatemia and Vascular Calcification

doi: 10.1681/asn.2021121578

Figure Lengend Snippet: Figure 1. A novel kidney-specific protein regulates Pi homeostasis. siRNA library screening identified that the TMEM174 gene regulates Pi uptake in cells expressing NPT2A. (A) siRNA knockdown efficiency, (B) total Pi uptake, and (C) levels of NPT2A protein. Human renal tubular cells expressing NPT2A were treated with 20 nM siRNA and then with FGF23 (10 nM) in the presence of 100 ng/ml secretory KL and 2 mg/ml heparin for 1 hour. (D) TMEM174 and NPT2A protein expression in human proximal tubular cells treated with 20 nM TMEM174 siRNA and then treated with FGF23 (10 nM) for 1–4 hours in the presence of 100 ng/ml secretory KL, 2 mg/ml heparin, and 0.1% BSA. Flarebio and Novus TMEM174 antibodies were used for human proximal tubular cells. The asterisk (*) represents nonspecific protein signal. (E) TMEM174 and NPT2A protein expression in OK-P cells treated with 20 nM TMEM174 siRNA and then with PTH (10 nM) for 1–4 hours in the presence of 0.1% BSA. Biomatik TMEM174 antibody was used for OK-P cells. Statistical analysis was performed using a one-way ANOVA. The experiments were repeated three times. ***P,0.001, **P,0.01 (ver- sus Scr1FGF23), #P,0.05 (versus Scr-FGF23).

Article Snippet: Primary renal proximal tubular cells (PCS400-010) were purchased from ATCC and were grown and maintained at 37 C, in an atmosphere of 5% carbon dioxide, in a growth media (PCS- 400-030) in the absence/presence of 10–100 nM FGF23 (2604-FG; R&D System) and 100 ng/ml of a secretory form of KL, which was synthesized and purified from HEK293- expressing pcDNA3.1-KL-His cells at the Cell Technologies Core Facility at the University of Colorado Denver.

Techniques: Library Screening, Expressing, Knockdown

Figure 3. Disruption of Pi homeostasis by TMEM174 deficiency. Serum (A) Pi, (B) FGF23, (C) PTH, and (D) 1,25(OH)2D in 8-week- old TMEM174 KO male mice fed a chow diet. (E) TMEM174, renal Pi cotransporters, and NHEFR1 in the renal BBM of TMEM174 KO mice. Flarebio TMEM174 antibody was used to detect mouse TMEM174. (F) Immunofluorescence analysis of NPT2A in the kidneys of TMEM174 KO mice.25–27 (G) Total Pi uptake and (H) sodium-independent Pi uptake in the renal BBM of TMEM174 KO mice. Urinary (I) Pi and (J) Ca excretion of TMEM174 KO mice. Urine was collected in metabolic cages for 24 hours. (K) Alizarin red staining, (L) calcified lesions, and (M) aortic Ca content in the aortic sinus of TMEM174 KO mice. Statistical analysis was performed using a two-tailed t test. *P,0.05, **P,0.01, ***P,0.001. WT, wild type.

Journal: Journal of the American Society of Nephrology

Article Title: Targeted Disruption of a Proximal Tubule–Specific TMEM174 Gene in Mice Causes Hyperphosphatemia and Vascular Calcification

doi: 10.1681/asn.2021121578

Figure Lengend Snippet: Figure 3. Disruption of Pi homeostasis by TMEM174 deficiency. Serum (A) Pi, (B) FGF23, (C) PTH, and (D) 1,25(OH)2D in 8-week- old TMEM174 KO male mice fed a chow diet. (E) TMEM174, renal Pi cotransporters, and NHEFR1 in the renal BBM of TMEM174 KO mice. Flarebio TMEM174 antibody was used to detect mouse TMEM174. (F) Immunofluorescence analysis of NPT2A in the kidneys of TMEM174 KO mice.25–27 (G) Total Pi uptake and (H) sodium-independent Pi uptake in the renal BBM of TMEM174 KO mice. Urinary (I) Pi and (J) Ca excretion of TMEM174 KO mice. Urine was collected in metabolic cages for 24 hours. (K) Alizarin red staining, (L) calcified lesions, and (M) aortic Ca content in the aortic sinus of TMEM174 KO mice. Statistical analysis was performed using a two-tailed t test. *P,0.05, **P,0.01, ***P,0.001. WT, wild type.

Article Snippet: Primary renal proximal tubular cells (PCS400-010) were purchased from ATCC and were grown and maintained at 37 C, in an atmosphere of 5% carbon dioxide, in a growth media (PCS- 400-030) in the absence/presence of 10–100 nM FGF23 (2604-FG; R&D System) and 100 ng/ml of a secretory form of KL, which was synthesized and purified from HEK293- expressing pcDNA3.1-KL-His cells at the Cell Technologies Core Facility at the University of Colorado Denver.

Techniques: Disruption, Staining, Two Tailed Test

Fibroblast growth factor 23 increases mRNA levels of markers of hypertrophy and fibrosis. Rat cardiac myoblast cells (H9c2) were cultured with 0, 50, or 100 ng/mL fibroblast growth factor 3 (FGF23) for 24 h, and mRNA expression levels were analyzed by real-time PCR. (A) Atrial natriuretic factor (ANF) ( n = 6). ** P < 0.05 versus 0 ng/mL. (B) Brain natriuretic peptide (BNP) ( n = 6). * P < 0.01 versus 0 ng/mL. (C) β-myosin heavy chain ( beta MHC ) ( n = 6). ** P < 0.05 versus 0 ng/mL. (D) Alpha smooth muscle actin ( alpha SMA ) ( n = 6). * P < 0.01 versus 0 ng/mL. (E) Collagen I ( n = 6). * P < 0.01 versus 0 ng/mL. (F) FGF23 ( n = 6). * P < 0.01 versus 0 ng/mL. Data were analyzed by one-way analysis of variance.

Journal: Frontiers in Cardiovascular Medicine

Article Title: Indoxyl sulfate induces left ventricular hypertrophy via the AhR-FGF23-FGFR4 signaling pathway

doi: 10.3389/fcvm.2023.990422

Figure Lengend Snippet: Fibroblast growth factor 23 increases mRNA levels of markers of hypertrophy and fibrosis. Rat cardiac myoblast cells (H9c2) were cultured with 0, 50, or 100 ng/mL fibroblast growth factor 3 (FGF23) for 24 h, and mRNA expression levels were analyzed by real-time PCR. (A) Atrial natriuretic factor (ANF) ( n = 6). ** P < 0.05 versus 0 ng/mL. (B) Brain natriuretic peptide (BNP) ( n = 6). * P < 0.01 versus 0 ng/mL. (C) β-myosin heavy chain ( beta MHC ) ( n = 6). ** P < 0.05 versus 0 ng/mL. (D) Alpha smooth muscle actin ( alpha SMA ) ( n = 6). * P < 0.01 versus 0 ng/mL. (E) Collagen I ( n = 6). * P < 0.01 versus 0 ng/mL. (F) FGF23 ( n = 6). * P < 0.01 versus 0 ng/mL. Data were analyzed by one-way analysis of variance.

Article Snippet: The following antibodies were used as primary antibodies: monoclonal anti-rat FGF23 antibody (1:500, MAB2629; R&D Systems); polyclonal anti-goat FGF23 antibody (1:1000, ab123502; Abcam, Cambridge, UK); polyclonal anti-rabbit FGFR4 antibody (1:1000, ab119378; Abcam); polyclonal anti-rabbit FGFR4 (phospho Y642; pFGFR4) antibody (1:1000, ab192589; Abcam); polyclonal anti-rabbit furin antibody (1:1000, PA1-062; Thermo Fisher Scientific); polyclonal anti-rabbit hypoxia-inducible factor 1 alpha (HIF1α) antibody (1:1000, NB100-134; Novus Biologicals, Centennial, CO); polyclonal anti-rabbit polypeptide GALNT3 antibody (1:1000, SAB2106736; Sigma-Aldrich); and anti-rabbit α/β tubulin (1:1000, CST#2148; Cell Signaling Technology, Danvers, MA).

Techniques: Cell Culture, Expressing, Real-time Polymerase Chain Reaction

Indoxyl sulfate increases mRNA levels of markers of hypertrophy and fibrosis. H9c2 cells were cultured with 0, 0.25, or 1.0 mM indoxyl sulfate (IS) for 24 h, and mRNA expression levels were analyzed by real-time PCR. (A) Atrial natriuretic factor ( ANF ) ( n = 6). * P < 0.01 versus 0 mM. (B) Brain natriuretic peptide (BNP) ( n = 6). * P < 0.01 versus 0 mM. (C) β-myosin heavy chain ( beta MHC ) ( n = 6). ** P < 0.05 versus 0 mM. (D) Alpha smooth muscle actin ( alpha SMA ) ( n = 6). ** P < 0.05 versus 0 mM. (E) Collagen I ( n = 6). ** P < 0.05 versus 0 mM. (F) FGF23 ( n = 6). ** P < 0.05 versus 0 mM. Data were analyzed by one-way analysis of variance.

Journal: Frontiers in Cardiovascular Medicine

Article Title: Indoxyl sulfate induces left ventricular hypertrophy via the AhR-FGF23-FGFR4 signaling pathway

doi: 10.3389/fcvm.2023.990422

Figure Lengend Snippet: Indoxyl sulfate increases mRNA levels of markers of hypertrophy and fibrosis. H9c2 cells were cultured with 0, 0.25, or 1.0 mM indoxyl sulfate (IS) for 24 h, and mRNA expression levels were analyzed by real-time PCR. (A) Atrial natriuretic factor ( ANF ) ( n = 6). * P < 0.01 versus 0 mM. (B) Brain natriuretic peptide (BNP) ( n = 6). * P < 0.01 versus 0 mM. (C) β-myosin heavy chain ( beta MHC ) ( n = 6). ** P < 0.05 versus 0 mM. (D) Alpha smooth muscle actin ( alpha SMA ) ( n = 6). ** P < 0.05 versus 0 mM. (E) Collagen I ( n = 6). ** P < 0.05 versus 0 mM. (F) FGF23 ( n = 6). ** P < 0.05 versus 0 mM. Data were analyzed by one-way analysis of variance.

Article Snippet: The following antibodies were used as primary antibodies: monoclonal anti-rat FGF23 antibody (1:500, MAB2629; R&D Systems); polyclonal anti-goat FGF23 antibody (1:1000, ab123502; Abcam, Cambridge, UK); polyclonal anti-rabbit FGFR4 antibody (1:1000, ab119378; Abcam); polyclonal anti-rabbit FGFR4 (phospho Y642; pFGFR4) antibody (1:1000, ab192589; Abcam); polyclonal anti-rabbit furin antibody (1:1000, PA1-062; Thermo Fisher Scientific); polyclonal anti-rabbit hypoxia-inducible factor 1 alpha (HIF1α) antibody (1:1000, NB100-134; Novus Biologicals, Centennial, CO); polyclonal anti-rabbit polypeptide GALNT3 antibody (1:1000, SAB2106736; Sigma-Aldrich); and anti-rabbit α/β tubulin (1:1000, CST#2148; Cell Signaling Technology, Danvers, MA).

Techniques: Cell Culture, Expressing, Real-time Polymerase Chain Reaction

Indoxyl sulfate increases fibroblast growth factor 23 protein expression and fibroblast growth factor receptor 4 phosphorylation. (A,B) Western blotting of fibroblast growth factor 3 (FGF23) protein expression in H9c2 cells. H9c2 cells were cultured with 0, 0.25, or 1.0 mM indoxyl sulfate (IS) for 72 h. Alpha, beta-tubulin protein expression was examined as an internal control ( n = 5). * P < 0.05 versus IS 0 mM. (C,D) Western blotting of fibroblast growth factor receptor 4 (FGFR4) protein expression and FGFR4 phosphorylation in H9c2 cells. H9c2 cells were cultured with 0, 0.25, or 1.0 mM IS for 72 h. Alpha, beta-tubulin protein expression was examined as an internal control ( n = 5). * P < 0.05 versus IS 0 mM. (E–G) Western blotting of furin protein in H9c2 cells. H9c2 cells were cultured with 0 or 1.0 mM IS for 72 h. The images are from different parts of the same gel. Beta actin protein expression was examined as an internal control ( n = 6). Furin stained as two bands, furin precursor (96 KDa) and mature (90 KDa) forms. * P < 0.05 versus IS 0 mM. Data were analyzed by one-way analysis of variance.

Journal: Frontiers in Cardiovascular Medicine

Article Title: Indoxyl sulfate induces left ventricular hypertrophy via the AhR-FGF23-FGFR4 signaling pathway

doi: 10.3389/fcvm.2023.990422

Figure Lengend Snippet: Indoxyl sulfate increases fibroblast growth factor 23 protein expression and fibroblast growth factor receptor 4 phosphorylation. (A,B) Western blotting of fibroblast growth factor 3 (FGF23) protein expression in H9c2 cells. H9c2 cells were cultured with 0, 0.25, or 1.0 mM indoxyl sulfate (IS) for 72 h. Alpha, beta-tubulin protein expression was examined as an internal control ( n = 5). * P < 0.05 versus IS 0 mM. (C,D) Western blotting of fibroblast growth factor receptor 4 (FGFR4) protein expression and FGFR4 phosphorylation in H9c2 cells. H9c2 cells were cultured with 0, 0.25, or 1.0 mM IS for 72 h. Alpha, beta-tubulin protein expression was examined as an internal control ( n = 5). * P < 0.05 versus IS 0 mM. (E–G) Western blotting of furin protein in H9c2 cells. H9c2 cells were cultured with 0 or 1.0 mM IS for 72 h. The images are from different parts of the same gel. Beta actin protein expression was examined as an internal control ( n = 6). Furin stained as two bands, furin precursor (96 KDa) and mature (90 KDa) forms. * P < 0.05 versus IS 0 mM. Data were analyzed by one-way analysis of variance.

Article Snippet: The following antibodies were used as primary antibodies: monoclonal anti-rat FGF23 antibody (1:500, MAB2629; R&D Systems); polyclonal anti-goat FGF23 antibody (1:1000, ab123502; Abcam, Cambridge, UK); polyclonal anti-rabbit FGFR4 antibody (1:1000, ab119378; Abcam); polyclonal anti-rabbit FGFR4 (phospho Y642; pFGFR4) antibody (1:1000, ab192589; Abcam); polyclonal anti-rabbit furin antibody (1:1000, PA1-062; Thermo Fisher Scientific); polyclonal anti-rabbit hypoxia-inducible factor 1 alpha (HIF1α) antibody (1:1000, NB100-134; Novus Biologicals, Centennial, CO); polyclonal anti-rabbit polypeptide GALNT3 antibody (1:1000, SAB2106736; Sigma-Aldrich); and anti-rabbit α/β tubulin (1:1000, CST#2148; Cell Signaling Technology, Danvers, MA).

Techniques: Expressing, Phospho-proteomics, Western Blot, Cell Culture, Control, Staining

Body weight, blood pressure, and laboratory data from animal experiments.

Journal: Frontiers in Cardiovascular Medicine

Article Title: Indoxyl sulfate induces left ventricular hypertrophy via the AhR-FGF23-FGFR4 signaling pathway

doi: 10.3389/fcvm.2023.990422

Figure Lengend Snippet: Body weight, blood pressure, and laboratory data from animal experiments.

Article Snippet: The following antibodies were used as primary antibodies: monoclonal anti-rat FGF23 antibody (1:500, MAB2629; R&D Systems); polyclonal anti-goat FGF23 antibody (1:1000, ab123502; Abcam, Cambridge, UK); polyclonal anti-rabbit FGFR4 antibody (1:1000, ab119378; Abcam); polyclonal anti-rabbit FGFR4 (phospho Y642; pFGFR4) antibody (1:1000, ab192589; Abcam); polyclonal anti-rabbit furin antibody (1:1000, PA1-062; Thermo Fisher Scientific); polyclonal anti-rabbit hypoxia-inducible factor 1 alpha (HIF1α) antibody (1:1000, NB100-134; Novus Biologicals, Centennial, CO); polyclonal anti-rabbit polypeptide GALNT3 antibody (1:1000, SAB2106736; Sigma-Aldrich); and anti-rabbit α/β tubulin (1:1000, CST#2148; Cell Signaling Technology, Danvers, MA).

Techniques:

(A,B) IS increases intact FGF23 expression in the heart. The expression of intact FGF23 in the heart was significantly increased after IS treatment. This effect was abrogated by FGFR4 inhibition as shown by Western blotting ( n = 3–6). Data were analyzed by one-way analysis of variance. * P < 0.05.

Journal: Frontiers in Cardiovascular Medicine

Article Title: Indoxyl sulfate induces left ventricular hypertrophy via the AhR-FGF23-FGFR4 signaling pathway

doi: 10.3389/fcvm.2023.990422

Figure Lengend Snippet: (A,B) IS increases intact FGF23 expression in the heart. The expression of intact FGF23 in the heart was significantly increased after IS treatment. This effect was abrogated by FGFR4 inhibition as shown by Western blotting ( n = 3–6). Data were analyzed by one-way analysis of variance. * P < 0.05.

Article Snippet: The following antibodies were used as primary antibodies: monoclonal anti-rat FGF23 antibody (1:500, MAB2629; R&D Systems); polyclonal anti-goat FGF23 antibody (1:1000, ab123502; Abcam, Cambridge, UK); polyclonal anti-rabbit FGFR4 antibody (1:1000, ab119378; Abcam); polyclonal anti-rabbit FGFR4 (phospho Y642; pFGFR4) antibody (1:1000, ab192589; Abcam); polyclonal anti-rabbit furin antibody (1:1000, PA1-062; Thermo Fisher Scientific); polyclonal anti-rabbit hypoxia-inducible factor 1 alpha (HIF1α) antibody (1:1000, NB100-134; Novus Biologicals, Centennial, CO); polyclonal anti-rabbit polypeptide GALNT3 antibody (1:1000, SAB2106736; Sigma-Aldrich); and anti-rabbit α/β tubulin (1:1000, CST#2148; Cell Signaling Technology, Danvers, MA).

Techniques: Expressing, Inhibition, Western Blot

IS induces FGF23 via AhR in vitro . H9c2 cells were cultured with 0 or 1 mM IS for 6 h (for mRNA) or 48 h (for protein) after pretreatment with AhR siRNA or control siRNA (ctrl). (A) FGF23 mRNA levels were significantly increased by IS and downregulated with AhR siRNA ( n = 11). * P < 0.01, ** P < 0.05. (B,C) Western blotting of FGF23 protein expression in H9c2 cells. Alpha, beta-tubulin protein expression was examined as an internal control ( n = 6). * P < 0.01, ** P < 0.05. (D,E) Western blotting of HIF1α protein expression in H9c2 cells. The images are different parts of the same gel. Alpha, beta-tubulin protein expression was used as an internal control ( n = 6). * P < 0.01, ** P < 0.05. (F) H9c2 cells were cultured with 0, 50, or 100 ng/mL FGF23 for 24 h, and mRNA expression levels were analyzed by real-time PCR. Levels of polypeptide N-acetylgalactosaminyltransferase 3 ( GALNT3 ) mRNA ( n = 6). * P < 0.01, ** P < 0.05. (G) H9c2 cells were cultured with 0, 0.25, or 1.0 mM IS for 24 h, and mRNA expression levels were analyzed by real-time PCR. Levels of GALNT3 mRNA ( n = 6). * P < 0.01, ** P < 0.05. (H) Levels of GALNT3 mRNA ( n = 9). * P < 0.01, ** P < 0.05. (I,J) Western blotting of GALNT3 protein expression in H9c2 cells. Alpha, beta-tubulin protein expression was used as an internal control ( n = 6). * P < 0.01, ** P < 0.05. Data were analyzed by one-way analysis of variance.

Journal: Frontiers in Cardiovascular Medicine

Article Title: Indoxyl sulfate induces left ventricular hypertrophy via the AhR-FGF23-FGFR4 signaling pathway

doi: 10.3389/fcvm.2023.990422

Figure Lengend Snippet: IS induces FGF23 via AhR in vitro . H9c2 cells were cultured with 0 or 1 mM IS for 6 h (for mRNA) or 48 h (for protein) after pretreatment with AhR siRNA or control siRNA (ctrl). (A) FGF23 mRNA levels were significantly increased by IS and downregulated with AhR siRNA ( n = 11). * P < 0.01, ** P < 0.05. (B,C) Western blotting of FGF23 protein expression in H9c2 cells. Alpha, beta-tubulin protein expression was examined as an internal control ( n = 6). * P < 0.01, ** P < 0.05. (D,E) Western blotting of HIF1α protein expression in H9c2 cells. The images are different parts of the same gel. Alpha, beta-tubulin protein expression was used as an internal control ( n = 6). * P < 0.01, ** P < 0.05. (F) H9c2 cells were cultured with 0, 50, or 100 ng/mL FGF23 for 24 h, and mRNA expression levels were analyzed by real-time PCR. Levels of polypeptide N-acetylgalactosaminyltransferase 3 ( GALNT3 ) mRNA ( n = 6). * P < 0.01, ** P < 0.05. (G) H9c2 cells were cultured with 0, 0.25, or 1.0 mM IS for 24 h, and mRNA expression levels were analyzed by real-time PCR. Levels of GALNT3 mRNA ( n = 6). * P < 0.01, ** P < 0.05. (H) Levels of GALNT3 mRNA ( n = 9). * P < 0.01, ** P < 0.05. (I,J) Western blotting of GALNT3 protein expression in H9c2 cells. Alpha, beta-tubulin protein expression was used as an internal control ( n = 6). * P < 0.01, ** P < 0.05. Data were analyzed by one-way analysis of variance.

Article Snippet: The following antibodies were used as primary antibodies: monoclonal anti-rat FGF23 antibody (1:500, MAB2629; R&D Systems); polyclonal anti-goat FGF23 antibody (1:1000, ab123502; Abcam, Cambridge, UK); polyclonal anti-rabbit FGFR4 antibody (1:1000, ab119378; Abcam); polyclonal anti-rabbit FGFR4 (phospho Y642; pFGFR4) antibody (1:1000, ab192589; Abcam); polyclonal anti-rabbit furin antibody (1:1000, PA1-062; Thermo Fisher Scientific); polyclonal anti-rabbit hypoxia-inducible factor 1 alpha (HIF1α) antibody (1:1000, NB100-134; Novus Biologicals, Centennial, CO); polyclonal anti-rabbit polypeptide GALNT3 antibody (1:1000, SAB2106736; Sigma-Aldrich); and anti-rabbit α/β tubulin (1:1000, CST#2148; Cell Signaling Technology, Danvers, MA).

Techniques: In Vitro, Cell Culture, Control, Western Blot, Expressing, Real-time Polymerase Chain Reaction

IS increases hypertrophic markers via FGF23 in vitro . H9c2 cells were cultured with 0 or 1 mM IS for 24 h after pretreatment with FGF23 siRNA or control siRNA (ctrl), and mRNA expression levels were analyzed by real-time PCR. (A) ANF , (B) BNP , (C) beta MHC , (D) alpha SMA , (E) collagen I, and (F) FGF23 mRNA levels were significantly increased by IS and downregulated with FGF23 siRNA ( n = 6). Data were analyzed by one-way analysis of variance. * P < 0.01, ** P < 0.05.

Journal: Frontiers in Cardiovascular Medicine

Article Title: Indoxyl sulfate induces left ventricular hypertrophy via the AhR-FGF23-FGFR4 signaling pathway

doi: 10.3389/fcvm.2023.990422

Figure Lengend Snippet: IS increases hypertrophic markers via FGF23 in vitro . H9c2 cells were cultured with 0 or 1 mM IS for 24 h after pretreatment with FGF23 siRNA or control siRNA (ctrl), and mRNA expression levels were analyzed by real-time PCR. (A) ANF , (B) BNP , (C) beta MHC , (D) alpha SMA , (E) collagen I, and (F) FGF23 mRNA levels were significantly increased by IS and downregulated with FGF23 siRNA ( n = 6). Data were analyzed by one-way analysis of variance. * P < 0.01, ** P < 0.05.

Article Snippet: The following antibodies were used as primary antibodies: monoclonal anti-rat FGF23 antibody (1:500, MAB2629; R&D Systems); polyclonal anti-goat FGF23 antibody (1:1000, ab123502; Abcam, Cambridge, UK); polyclonal anti-rabbit FGFR4 antibody (1:1000, ab119378; Abcam); polyclonal anti-rabbit FGFR4 (phospho Y642; pFGFR4) antibody (1:1000, ab192589; Abcam); polyclonal anti-rabbit furin antibody (1:1000, PA1-062; Thermo Fisher Scientific); polyclonal anti-rabbit hypoxia-inducible factor 1 alpha (HIF1α) antibody (1:1000, NB100-134; Novus Biologicals, Centennial, CO); polyclonal anti-rabbit polypeptide GALNT3 antibody (1:1000, SAB2106736; Sigma-Aldrich); and anti-rabbit α/β tubulin (1:1000, CST#2148; Cell Signaling Technology, Danvers, MA).

Techniques: In Vitro, Cell Culture, Control, Expressing, Real-time Polymerase Chain Reaction

IS increases FGFR4 via FGF23 in vitro . H9c2 cells were cultured with 0 or 1 mM IS for 48 h after pretreatment with FGF23 siRNA or control siRNA (ctrl). (A,B) Western blotting of FGF23 protein expression in H9c2 cells. (C,D) Western blotting of FGFR4 protein expression and FGFR4 phosphorylation in H9c2 cells. Alpha, beta-tubulin protein expression was examined as an internal control ( n = 6). Data were analyzed by one-way analysis of variance. * P < 0.01, ** P < 0.05.

Journal: Frontiers in Cardiovascular Medicine

Article Title: Indoxyl sulfate induces left ventricular hypertrophy via the AhR-FGF23-FGFR4 signaling pathway

doi: 10.3389/fcvm.2023.990422

Figure Lengend Snippet: IS increases FGFR4 via FGF23 in vitro . H9c2 cells were cultured with 0 or 1 mM IS for 48 h after pretreatment with FGF23 siRNA or control siRNA (ctrl). (A,B) Western blotting of FGF23 protein expression in H9c2 cells. (C,D) Western blotting of FGFR4 protein expression and FGFR4 phosphorylation in H9c2 cells. Alpha, beta-tubulin protein expression was examined as an internal control ( n = 6). Data were analyzed by one-way analysis of variance. * P < 0.01, ** P < 0.05.

Article Snippet: The following antibodies were used as primary antibodies: monoclonal anti-rat FGF23 antibody (1:500, MAB2629; R&D Systems); polyclonal anti-goat FGF23 antibody (1:1000, ab123502; Abcam, Cambridge, UK); polyclonal anti-rabbit FGFR4 antibody (1:1000, ab119378; Abcam); polyclonal anti-rabbit FGFR4 (phospho Y642; pFGFR4) antibody (1:1000, ab192589; Abcam); polyclonal anti-rabbit furin antibody (1:1000, PA1-062; Thermo Fisher Scientific); polyclonal anti-rabbit hypoxia-inducible factor 1 alpha (HIF1α) antibody (1:1000, NB100-134; Novus Biologicals, Centennial, CO); polyclonal anti-rabbit polypeptide GALNT3 antibody (1:1000, SAB2106736; Sigma-Aldrich); and anti-rabbit α/β tubulin (1:1000, CST#2148; Cell Signaling Technology, Danvers, MA).

Techniques: In Vitro, Cell Culture, Control, Western Blot, Expressing, Phospho-proteomics

Potential mechanism by which IS may induce LVH via the FGF23-FGFR4 pathway. IS upregulates FGF23 mRNA via AhR and HIF1α. IS also increases GALNT3 gene expression, preventing furin-mediated degradation of intact FGF23. Increased FGF23 induces myocardial hypertrophy by FGFR4-dependent activation.

Journal: Frontiers in Cardiovascular Medicine

Article Title: Indoxyl sulfate induces left ventricular hypertrophy via the AhR-FGF23-FGFR4 signaling pathway

doi: 10.3389/fcvm.2023.990422

Figure Lengend Snippet: Potential mechanism by which IS may induce LVH via the FGF23-FGFR4 pathway. IS upregulates FGF23 mRNA via AhR and HIF1α. IS also increases GALNT3 gene expression, preventing furin-mediated degradation of intact FGF23. Increased FGF23 induces myocardial hypertrophy by FGFR4-dependent activation.

Article Snippet: The following antibodies were used as primary antibodies: monoclonal anti-rat FGF23 antibody (1:500, MAB2629; R&D Systems); polyclonal anti-goat FGF23 antibody (1:1000, ab123502; Abcam, Cambridge, UK); polyclonal anti-rabbit FGFR4 antibody (1:1000, ab119378; Abcam); polyclonal anti-rabbit FGFR4 (phospho Y642; pFGFR4) antibody (1:1000, ab192589; Abcam); polyclonal anti-rabbit furin antibody (1:1000, PA1-062; Thermo Fisher Scientific); polyclonal anti-rabbit hypoxia-inducible factor 1 alpha (HIF1α) antibody (1:1000, NB100-134; Novus Biologicals, Centennial, CO); polyclonal anti-rabbit polypeptide GALNT3 antibody (1:1000, SAB2106736; Sigma-Aldrich); and anti-rabbit α/β tubulin (1:1000, CST#2148; Cell Signaling Technology, Danvers, MA).

Techniques: Gene Expression, Activation Assay

Interaction of Klotho-EGFP N614Q with the proteasome and ER-chaperones. ( A ) Scheme of the GFP-TRAP immunoprecipitation followed by mass spectroscopy (MS). HEK239T cells expressing GFP or Klotho-EGFP variants were used. Created with BioRender.com. ( B ) Bar graph illustrating KEGG pathway analysis of proteins exhibiting increased interaction with Klotho-EGFP N614Q compared to Klotho-EGFP WT . ( C ) Heatmap plot of proteins that exhibit enhanced interaction with Klotho-EGFP N614Q associated with protein processing in the ER . The color code indicates a log2-fold change. ( D ) Western blot analysis of proteins co-IPed with Klotho-EGFP variants from lysates of HEK293T cells stably expressing Klotho-EGFP WT or N614Q after GFP-TRAP IP. Samples were probed with antibodies against Klotho, HSPA5, and ERGIC53. Where indicated, cells were treated with 2.5 nM FGF23 for 5 min. ( E ) Quantification of the interaction of Klotho-EGFP variants with HSPA5 and ERGIC53; displayed is the relative intensity of HSPA5 or ERGIC53 to KL in %. (n = 4 experiments, mean ± SD, two-sided Student’s t -test. For full-size blots, see .

Journal: Cells

Article Title: Asparagine614 Determines the Transport and Function of the Murine Anti-Aging Protein Klotho

doi: 10.3390/cells13201743

Figure Lengend Snippet: Interaction of Klotho-EGFP N614Q with the proteasome and ER-chaperones. ( A ) Scheme of the GFP-TRAP immunoprecipitation followed by mass spectroscopy (MS). HEK239T cells expressing GFP or Klotho-EGFP variants were used. Created with BioRender.com. ( B ) Bar graph illustrating KEGG pathway analysis of proteins exhibiting increased interaction with Klotho-EGFP N614Q compared to Klotho-EGFP WT . ( C ) Heatmap plot of proteins that exhibit enhanced interaction with Klotho-EGFP N614Q associated with protein processing in the ER . The color code indicates a log2-fold change. ( D ) Western blot analysis of proteins co-IPed with Klotho-EGFP variants from lysates of HEK293T cells stably expressing Klotho-EGFP WT or N614Q after GFP-TRAP IP. Samples were probed with antibodies against Klotho, HSPA5, and ERGIC53. Where indicated, cells were treated with 2.5 nM FGF23 for 5 min. ( E ) Quantification of the interaction of Klotho-EGFP variants with HSPA5 and ERGIC53; displayed is the relative intensity of HSPA5 or ERGIC53 to KL in %. (n = 4 experiments, mean ± SD, two-sided Student’s t -test. For full-size blots, see .

Article Snippet: Dulbecco’s modified Eagle Medium + GlutaMax (Gibco, Waltham, MS, USA, 61965-026), Hygromycin B (50 mg/mL) (Thermo Fischer Scientific, 10687010, Waltham, MS, USA), penicillin/streptomycin (Merck, P0781, Rahway, NJ, USA), Fetal Bovine Serum (F7524 Sigma-Aldrich, Burlington, MA), ROTI ® Histofix 4% paraformaldehyde (Carl Roth, No. P087.1, Karlsruhe, Germany), Hoechst 33342 (Invitrogen, H1399, Waltham, MS, USA), Human FGF23 protein (R&D Systems, 2604, Minneapolis, MN, USA), LipofectamineTM 2000 Transfection Reagent (Thermo Fischer Scientific, 11668019), Protease Inhibitor Cocktail (Sigma P8340, Burlington, MA, USA), phosphatase inhibitors (PhosSTOP, Roche, #4906837001, Basel, Switzerland), CHAPSO (Carl Roth), I-BlockTM powder (T2015, Applied Biosystems, Thermo Fisher Scientific).

Techniques: Immunoprecipitation, Mass Spectrometry, Expressing, Western Blot, Stable Transfection

N-glycosylation is not essential for Klotho-FGFR interaction. HEK293T cells stably expressing Klotho-EGFP variants were serum-starved for 16 h and incubated for 5 min with FGF23, followed by lysis and processing for Western blotting with the indicated antibodies. ( B ) Quantification of n = 4 independent experiments, as shown in ( A ). The ratio of the phospho (p)-ERK to total (t)-ERK in the presence and absence of FGF23 is displayed as mean ± SD, with statistical analysis performed using a two-sided Student’s t -test (ns: non-significant) Vertical black lines indicate splicing; for full-size blots, see .

Journal: Cells

Article Title: Asparagine614 Determines the Transport and Function of the Murine Anti-Aging Protein Klotho

doi: 10.3390/cells13201743

Figure Lengend Snippet: N-glycosylation is not essential for Klotho-FGFR interaction. HEK293T cells stably expressing Klotho-EGFP variants were serum-starved for 16 h and incubated for 5 min with FGF23, followed by lysis and processing for Western blotting with the indicated antibodies. ( B ) Quantification of n = 4 independent experiments, as shown in ( A ). The ratio of the phospho (p)-ERK to total (t)-ERK in the presence and absence of FGF23 is displayed as mean ± SD, with statistical analysis performed using a two-sided Student’s t -test (ns: non-significant) Vertical black lines indicate splicing; for full-size blots, see .

Article Snippet: Dulbecco’s modified Eagle Medium + GlutaMax (Gibco, Waltham, MS, USA, 61965-026), Hygromycin B (50 mg/mL) (Thermo Fischer Scientific, 10687010, Waltham, MS, USA), penicillin/streptomycin (Merck, P0781, Rahway, NJ, USA), Fetal Bovine Serum (F7524 Sigma-Aldrich, Burlington, MA), ROTI ® Histofix 4% paraformaldehyde (Carl Roth, No. P087.1, Karlsruhe, Germany), Hoechst 33342 (Invitrogen, H1399, Waltham, MS, USA), Human FGF23 protein (R&D Systems, 2604, Minneapolis, MN, USA), LipofectamineTM 2000 Transfection Reagent (Thermo Fischer Scientific, 11668019), Protease Inhibitor Cocktail (Sigma P8340, Burlington, MA, USA), phosphatase inhibitors (PhosSTOP, Roche, #4906837001, Basel, Switzerland), CHAPSO (Carl Roth), I-BlockTM powder (T2015, Applied Biosystems, Thermo Fisher Scientific).

Techniques: Glycoproteomics, Stable Transfection, Expressing, Incubation, Lysis, Western Blot

FGF23 does not activate ER-resident Klotho-EGFP-EGFR3 complexes. ( A , C ) Western blot of HEK293T cell lysates stably expressing Klotho-EGFP WT or N614Q after treatment with different FGF23 concentrations for 5 min ( A ) or with 2.5 nM FGF23 for the indicated times ( B ), probed with the indicated antibodies. p, phospho;t, total. ( B ) Quantification of n = 4 independent experiments from ( A ). Displayed is the ratio of phospho(p)-ERK normalized to total (t)-ERK. ( C ) A representative blot from n = 2 independent experiments. ( D ) HEK293T cells stably expressing EGFP, Klotho-EGFP WT, or N614Q-treated with 2.5 nM FGF23 for 5 min were subjected to IP with GFP-TRAP. IP lysates (Inp., input) after IP were separated by SDS-PAGE, blotted, and probed with antibodies against FGFR3 or Klotho. ( E ) Quantification of n = 3 independent experiments from ( D ). Displayed is the ratio of FGFR3 to Klotho-EGFP variant. A two-sided Student’s t -test was used to assess statistical significance * p < 0.05. Error bars indicate SD. Vertical black lines indicate splicing; for full-size blots, see .

Journal: Cells

Article Title: Asparagine614 Determines the Transport and Function of the Murine Anti-Aging Protein Klotho

doi: 10.3390/cells13201743

Figure Lengend Snippet: FGF23 does not activate ER-resident Klotho-EGFP-EGFR3 complexes. ( A , C ) Western blot of HEK293T cell lysates stably expressing Klotho-EGFP WT or N614Q after treatment with different FGF23 concentrations for 5 min ( A ) or with 2.5 nM FGF23 for the indicated times ( B ), probed with the indicated antibodies. p, phospho;t, total. ( B ) Quantification of n = 4 independent experiments from ( A ). Displayed is the ratio of phospho(p)-ERK normalized to total (t)-ERK. ( C ) A representative blot from n = 2 independent experiments. ( D ) HEK293T cells stably expressing EGFP, Klotho-EGFP WT, or N614Q-treated with 2.5 nM FGF23 for 5 min were subjected to IP with GFP-TRAP. IP lysates (Inp., input) after IP were separated by SDS-PAGE, blotted, and probed with antibodies against FGFR3 or Klotho. ( E ) Quantification of n = 3 independent experiments from ( D ). Displayed is the ratio of FGFR3 to Klotho-EGFP variant. A two-sided Student’s t -test was used to assess statistical significance * p < 0.05. Error bars indicate SD. Vertical black lines indicate splicing; for full-size blots, see .

Article Snippet: Dulbecco’s modified Eagle Medium + GlutaMax (Gibco, Waltham, MS, USA, 61965-026), Hygromycin B (50 mg/mL) (Thermo Fischer Scientific, 10687010, Waltham, MS, USA), penicillin/streptomycin (Merck, P0781, Rahway, NJ, USA), Fetal Bovine Serum (F7524 Sigma-Aldrich, Burlington, MA), ROTI ® Histofix 4% paraformaldehyde (Carl Roth, No. P087.1, Karlsruhe, Germany), Hoechst 33342 (Invitrogen, H1399, Waltham, MS, USA), Human FGF23 protein (R&D Systems, 2604, Minneapolis, MN, USA), LipofectamineTM 2000 Transfection Reagent (Thermo Fischer Scientific, 11668019), Protease Inhibitor Cocktail (Sigma P8340, Burlington, MA, USA), phosphatase inhibitors (PhosSTOP, Roche, #4906837001, Basel, Switzerland), CHAPSO (Carl Roth), I-BlockTM powder (T2015, Applied Biosystems, Thermo Fisher Scientific).

Techniques: Western Blot, Stable Transfection, Expressing, SDS Page, Variant Assay

Low amounts of Klotho-EGFP at the plasma membrane are sufficient for ERK activation. ( A ) HEK293T cells stably expressing Klotho-EGFP at low (l), median (m), and high (h) levels were incubated with 2.5 nM FGF23 for 5 min, lysed, separated on SDS-PAGE, and subjected to Western Blotting with the indicated antibodies. ( B ) Quantification of n = 4 independent experiments from A. The displayed ratio is p-ERK/t-ERK. A Two-sided Student’s t -test was used to assess statistical significance, (ns: non-significant). Error bars indicate SD. For full-size blots, see .

Journal: Cells

Article Title: Asparagine614 Determines the Transport and Function of the Murine Anti-Aging Protein Klotho

doi: 10.3390/cells13201743

Figure Lengend Snippet: Low amounts of Klotho-EGFP at the plasma membrane are sufficient for ERK activation. ( A ) HEK293T cells stably expressing Klotho-EGFP at low (l), median (m), and high (h) levels were incubated with 2.5 nM FGF23 for 5 min, lysed, separated on SDS-PAGE, and subjected to Western Blotting with the indicated antibodies. ( B ) Quantification of n = 4 independent experiments from A. The displayed ratio is p-ERK/t-ERK. A Two-sided Student’s t -test was used to assess statistical significance, (ns: non-significant). Error bars indicate SD. For full-size blots, see .

Article Snippet: Dulbecco’s modified Eagle Medium + GlutaMax (Gibco, Waltham, MS, USA, 61965-026), Hygromycin B (50 mg/mL) (Thermo Fischer Scientific, 10687010, Waltham, MS, USA), penicillin/streptomycin (Merck, P0781, Rahway, NJ, USA), Fetal Bovine Serum (F7524 Sigma-Aldrich, Burlington, MA), ROTI ® Histofix 4% paraformaldehyde (Carl Roth, No. P087.1, Karlsruhe, Germany), Hoechst 33342 (Invitrogen, H1399, Waltham, MS, USA), Human FGF23 protein (R&D Systems, 2604, Minneapolis, MN, USA), LipofectamineTM 2000 Transfection Reagent (Thermo Fischer Scientific, 11668019), Protease Inhibitor Cocktail (Sigma P8340, Burlington, MA, USA), phosphatase inhibitors (PhosSTOP, Roche, #4906837001, Basel, Switzerland), CHAPSO (Carl Roth), I-BlockTM powder (T2015, Applied Biosystems, Thermo Fisher Scientific).

Techniques: Clinical Proteomics, Membrane, Activation Assay, Stable Transfection, Expressing, Incubation, SDS Page, Western Blot

( A ) Venn diagram illustrating the overlap and distinctions between differentially up-regulated phosphorylated proteins in Klotho-EGFP WT and N614Q mutant after FGF23 treatment. ( B ) Pathway enrichment analysis depicting the differentially up-regulated phosphorylated proteins between Klotho-EGFP WT and N614Q after FGF23 treatment, highlighting the activation of key signaling pathways. ( C , D ) Heatmap illustrating the differentially expressed phosphosites and the predicted kinases responsible for their phosphorylation (the rows) in cells expressing Klotho-EGFP WT ( C ) or Klotho-EGFP N614Q ( D ). The red arrows on the right side of each heatmap indicate the presence of the ERK downstream target ELK1 and MAPK1 itself. The arrows at the bottom of the heatmap denote the predicted MAPKs responsible for phosphorylating the phosphosites depicted in the heatmap.

Journal: Cells

Article Title: Asparagine614 Determines the Transport and Function of the Murine Anti-Aging Protein Klotho

doi: 10.3390/cells13201743

Figure Lengend Snippet: ( A ) Venn diagram illustrating the overlap and distinctions between differentially up-regulated phosphorylated proteins in Klotho-EGFP WT and N614Q mutant after FGF23 treatment. ( B ) Pathway enrichment analysis depicting the differentially up-regulated phosphorylated proteins between Klotho-EGFP WT and N614Q after FGF23 treatment, highlighting the activation of key signaling pathways. ( C , D ) Heatmap illustrating the differentially expressed phosphosites and the predicted kinases responsible for their phosphorylation (the rows) in cells expressing Klotho-EGFP WT ( C ) or Klotho-EGFP N614Q ( D ). The red arrows on the right side of each heatmap indicate the presence of the ERK downstream target ELK1 and MAPK1 itself. The arrows at the bottom of the heatmap denote the predicted MAPKs responsible for phosphorylating the phosphosites depicted in the heatmap.

Article Snippet: Dulbecco’s modified Eagle Medium + GlutaMax (Gibco, Waltham, MS, USA, 61965-026), Hygromycin B (50 mg/mL) (Thermo Fischer Scientific, 10687010, Waltham, MS, USA), penicillin/streptomycin (Merck, P0781, Rahway, NJ, USA), Fetal Bovine Serum (F7524 Sigma-Aldrich, Burlington, MA), ROTI ® Histofix 4% paraformaldehyde (Carl Roth, No. P087.1, Karlsruhe, Germany), Hoechst 33342 (Invitrogen, H1399, Waltham, MS, USA), Human FGF23 protein (R&D Systems, 2604, Minneapolis, MN, USA), LipofectamineTM 2000 Transfection Reagent (Thermo Fischer Scientific, 11668019), Protease Inhibitor Cocktail (Sigma P8340, Burlington, MA, USA), phosphatase inhibitors (PhosSTOP, Roche, #4906837001, Basel, Switzerland), CHAPSO (Carl Roth), I-BlockTM powder (T2015, Applied Biosystems, Thermo Fisher Scientific).

Techniques: Mutagenesis, Activation Assay, Protein-Protein interactions, Phospho-proteomics, Expressing

(A) displays the distribution of post-KT FGF23 levels based on the hypertension status. (B) shows that the patients with larger LA volumes had the worst NHYA class.

Journal: Frontiers in Nephrology

Article Title: Role of kidney transplantation in long-term cardiac reverse remodeling and interconnecting mechanisms in type 4 cardiorenal syndrome

doi: 10.3389/fneph.2024.1455036

Figure Lengend Snippet: (A) displays the distribution of post-KT FGF23 levels based on the hypertension status. (B) shows that the patients with larger LA volumes had the worst NHYA class.

Article Snippet: FGF23 levels were quantified using the Human FGF23 monoclonal antibody and R&D Systems reagent (Minneapolis, MN, USA).

Techniques:

Biochemical and echocardiographic characteristics grouped according the basal LVEF and after KT.

Journal: Frontiers in Nephrology

Article Title: Role of kidney transplantation in long-term cardiac reverse remodeling and interconnecting mechanisms in type 4 cardiorenal syndrome

doi: 10.3389/fneph.2024.1455036

Figure Lengend Snippet: Biochemical and echocardiographic characteristics grouped according the basal LVEF and after KT.

Article Snippet: FGF23 levels were quantified using the Human FGF23 monoclonal antibody and R&D Systems reagent (Minneapolis, MN, USA).

Techniques:

Dependence of the SPRi signal on FGF23 antibody concentration. The used concentration of the FGF23-αKlotho complex was 40:169.2 pg/mL; pH = 7.4. “Standard deviation (SD)” was calculated from 12 individual measurements.

Journal: International Journal of Molecular Sciences

Article Title: A New Approach to the Quantification of Fibroblast Growth Factor 23—An Array Surface Plasmon Resonance Imaging Biosensor

doi: 10.3390/ijms242015327

Figure Lengend Snippet: Dependence of the SPRi signal on FGF23 antibody concentration. The used concentration of the FGF23-αKlotho complex was 40:169.2 pg/mL; pH = 7.4. “Standard deviation (SD)” was calculated from 12 individual measurements.

Article Snippet: The monoclonal mouse anti-human FGF23 antibody (R&D Systems) was a receptor that bound the FGF23 protein from samples to the chip’s surface.

Techniques: Concentration Assay, Standard Deviation

Dependence of the SPRi signal on the FGF23 concentration. The used FGF23 antibody concentration is 25 ng/mL; pH = 7.4. SD was calculated from 12 individual measurements.

Journal: International Journal of Molecular Sciences

Article Title: A New Approach to the Quantification of Fibroblast Growth Factor 23—An Array Surface Plasmon Resonance Imaging Biosensor

doi: 10.3390/ijms242015327

Figure Lengend Snippet: Dependence of the SPRi signal on the FGF23 concentration. The used FGF23 antibody concentration is 25 ng/mL; pH = 7.4. SD was calculated from 12 individual measurements.

Article Snippet: The monoclonal mouse anti-human FGF23 antibody (R&D Systems) was a receptor that bound the FGF23 protein from samples to the chip’s surface.

Techniques: Concentration Assay

Dependence of the SPRi signal on the FGF23 concentration with the addition of αKlotho protein. The used FGF23 antibody concentration is 25 ng/mL; pH = 7.4. SD was calculated from 12 individual measurements.

Journal: International Journal of Molecular Sciences

Article Title: A New Approach to the Quantification of Fibroblast Growth Factor 23—An Array Surface Plasmon Resonance Imaging Biosensor

doi: 10.3390/ijms242015327

Figure Lengend Snippet: Dependence of the SPRi signal on the FGF23 concentration with the addition of αKlotho protein. The used FGF23 antibody concentration is 25 ng/mL; pH = 7.4. SD was calculated from 12 individual measurements.

Article Snippet: The monoclonal mouse anti-human FGF23 antibody (R&D Systems) was a receptor that bound the FGF23 protein from samples to the chip’s surface.

Techniques: Concentration Assay

Influence of the αKlotho protein on the detected FGF23 concentration. SD was calculated from 12 individual measurements.

Journal: International Journal of Molecular Sciences

Article Title: A New Approach to the Quantification of Fibroblast Growth Factor 23—An Array Surface Plasmon Resonance Imaging Biosensor

doi: 10.3390/ijms242015327

Figure Lengend Snippet: Influence of the αKlotho protein on the detected FGF23 concentration. SD was calculated from 12 individual measurements.

Article Snippet: The monoclonal mouse anti-human FGF23 antibody (R&D Systems) was a receptor that bound the FGF23 protein from samples to the chip’s surface.

Techniques: Concentration Assay

Influence of the time on the formation of the FGF23-αKlotho complex. SD was calculated from 12 individual measurements.

Journal: International Journal of Molecular Sciences

Article Title: A New Approach to the Quantification of Fibroblast Growth Factor 23—An Array Surface Plasmon Resonance Imaging Biosensor

doi: 10.3390/ijms242015327

Figure Lengend Snippet: Influence of the time on the formation of the FGF23-αKlotho complex. SD was calculated from 12 individual measurements.

Article Snippet: The monoclonal mouse anti-human FGF23 antibody (R&D Systems) was a receptor that bound the FGF23 protein from samples to the chip’s surface.

Techniques: Concentration Assay

The influence of the potential interferents on the determination of the FGF23 with array SPRi biosensor. SD was calculated from 12 individual measurements.

Journal: International Journal of Molecular Sciences

Article Title: A New Approach to the Quantification of Fibroblast Growth Factor 23—An Array Surface Plasmon Resonance Imaging Biosensor

doi: 10.3390/ijms242015327

Figure Lengend Snippet: The influence of the potential interferents on the determination of the FGF23 with array SPRi biosensor. SD was calculated from 12 individual measurements.

Article Snippet: The monoclonal mouse anti-human FGF23 antibody (R&D Systems) was a receptor that bound the FGF23 protein from samples to the chip’s surface.

Techniques: Concentration Assay

Precision and accuracy of the FGF23 SPRi biosensor. SD and RSD were calculated from 36 individual measurements.

Journal: International Journal of Molecular Sciences

Article Title: A New Approach to the Quantification of Fibroblast Growth Factor 23—An Array Surface Plasmon Resonance Imaging Biosensor

doi: 10.3390/ijms242015327

Figure Lengend Snippet: Precision and accuracy of the FGF23 SPRi biosensor. SD and RSD were calculated from 36 individual measurements.

Article Snippet: The monoclonal mouse anti-human FGF23 antibody (R&D Systems) was a receptor that bound the FGF23 protein from samples to the chip’s surface.

Techniques: Concentration Assay

Precision and recovery of the FGF23 SPRi biosensor tested in a plasma sample after the addition of a 25 pg/mL spike. SD and RSD were calculated from 12 individual measurements.

Journal: International Journal of Molecular Sciences

Article Title: A New Approach to the Quantification of Fibroblast Growth Factor 23—An Array Surface Plasmon Resonance Imaging Biosensor

doi: 10.3390/ijms242015327

Figure Lengend Snippet: Precision and recovery of the FGF23 SPRi biosensor tested in a plasma sample after the addition of a 25 pg/mL spike. SD and RSD were calculated from 12 individual measurements.

Article Snippet: The monoclonal mouse anti-human FGF23 antibody (R&D Systems) was a receptor that bound the FGF23 protein from samples to the chip’s surface.

Techniques: Clinical Proteomics

Formation of the FGF23 SPRi biosensor layers, i.e., bare gold, cysteamine, FGF23 antibody, and FGF23-αKlotho complex, captured via SEM. Used parameters: 12.5 or 15 kV, and 100,000× magnification.

Journal: International Journal of Molecular Sciences

Article Title: A New Approach to the Quantification of Fibroblast Growth Factor 23—An Array Surface Plasmon Resonance Imaging Biosensor

doi: 10.3390/ijms242015327

Figure Lengend Snippet: Formation of the FGF23 SPRi biosensor layers, i.e., bare gold, cysteamine, FGF23 antibody, and FGF23-αKlotho complex, captured via SEM. Used parameters: 12.5 or 15 kV, and 100,000× magnification.

Article Snippet: The monoclonal mouse anti-human FGF23 antibody (R&D Systems) was a receptor that bound the FGF23 protein from samples to the chip’s surface.

Techniques:

The comparison of the results of FGF23 concentration measurements performed with the SPRi biosensor and ELISA in blood plasma samples. SD was calculated based on 12 measurements for the SPRi biosensor and 2 for the ELISA.

Journal: International Journal of Molecular Sciences

Article Title: A New Approach to the Quantification of Fibroblast Growth Factor 23—An Array Surface Plasmon Resonance Imaging Biosensor

doi: 10.3390/ijms242015327

Figure Lengend Snippet: The comparison of the results of FGF23 concentration measurements performed with the SPRi biosensor and ELISA in blood plasma samples. SD was calculated based on 12 measurements for the SPRi biosensor and 2 for the ELISA.

Article Snippet: The monoclonal mouse anti-human FGF23 antibody (R&D Systems) was a receptor that bound the FGF23 protein from samples to the chip’s surface.

Techniques: Comparison, Concentration Assay, Enzyme-linked Immunosorbent Assay, Clinical Proteomics

Scheme of the measuring system of the SPRi apparatus and an overview diagram of the FGF23 biosensor.

Journal: International Journal of Molecular Sciences

Article Title: A New Approach to the Quantification of Fibroblast Growth Factor 23—An Array Surface Plasmon Resonance Imaging Biosensor

doi: 10.3390/ijms242015327

Figure Lengend Snippet: Scheme of the measuring system of the SPRi apparatus and an overview diagram of the FGF23 biosensor.

Article Snippet: The monoclonal mouse anti-human FGF23 antibody (R&D Systems) was a receptor that bound the FGF23 protein from samples to the chip’s surface.

Techniques: