Journal: eLife

Article Title: High-phytate/low-calcium diet is a risk factor for crystal nephropathies, renal phosphate wasting, and bone loss

doi: 10.7554/eLife.52709

Figure Lengend Snippet: Time-course analysis of serum levels of intact FGF23 for three consecutive phytate doses. Statistical significance was tested by repeated measure ANOVA between subjects and groups. All data are presented as the mean ± SD for each dose (n = 6 per dose).

Article Snippet: Rat intact PTH (Immutopics, San Clemente, CA, USA), human intact PTH (Abcam), soluble RANKL (Immundiagnostik, Bensheim, Germany), osteoprotegerin (Alpco Immunoassay, Salem, NH, USA), rat intact and C-terminal FGF23 (Elabscience, Houston, TX, USA), and human intact FGF23 (Elabscience) were measured using enzyme-linked immunosorbent assay.

Techniques:

Journal: eLife

Article Title: High-phytate/low-calcium diet is a risk factor for crystal nephropathies, renal phosphate wasting, and bone loss

doi: 10.7554/eLife.52709

Figure Lengend Snippet: ( A–C ) Time-course analysis of serum levels of intact PTH ( A ), 25(OH)D ( B ), and 1,25(OH) 2 D ( C ) in rats fed control, HP-LCa 2+ , and HP-HCa 2+ diets. For the early measurement of 25(OH)D ( B ) and 1,25(OH) 2 D, we pooled the sera from 2 to 3 rats. ( D–F ) Time-course analysis of renal CYP27B1 ( D ), CYP24A1 ( E ), and VDR ( F ) in rats fed control, HP-LCa 2+ , and HP-HCa 2+ diets. ( G ) Immunoblot analysis of renal αKlotho, NHERF1, NaPi-2a in rats fed control, HP-LCa 2+ , and HP-HCa 2+ diets. ( H ) The levels of renal proteins were quantified using ImageJ software (NIH, Bethesda, MD, USA). ( I ) Immunoblot analysis of calvarial FGF23 in rats fed control, HP-LCa 2+ , and HP-HCa 2+ diets. ( J ) The levels of total calvarial FGF23 were quantified using ImageJ software. All comparisons were conducted using two-way ANOVA with Tukey’s post hoc multiple comparison testing or the Kruskal–Wallis test ( A–C ) for non-parametric statistical analysis of data that did not have a normal distribution. Panels ( A–C ) failed the normality test, but no outliers were identified. All data are presented as the mean ± SD of each group (n = 4–6 per group). *, p<0.05; **, p<0.01; ***, p<0.001, compared with controls.

Article Snippet: Rat intact PTH (Immutopics, San Clemente, CA, USA), human intact PTH (Abcam), soluble RANKL (Immundiagnostik, Bensheim, Germany), osteoprotegerin (Alpco Immunoassay, Salem, NH, USA), rat intact and C-terminal FGF23 (Elabscience, Houston, TX, USA), and human intact FGF23 (Elabscience) were measured using enzyme-linked immunosorbent assay.

Techniques: Control, Western Blot, Software, Comparison

Journal: eLife

Article Title: High-phytate/low-calcium diet is a risk factor for crystal nephropathies, renal phosphate wasting, and bone loss

doi: 10.7554/eLife.52709

Figure Lengend Snippet: ( A ) The renal expression of downregulated genes associated with Ca 2+ and phosphate homeostasis in rats fed control or phytate-supplemented diets (n = 8 per group). ( B ) Results of immunoblot analyses and protein levels of renal aKlotho, NHERF1, and NaPi-2a after 2 weeks for rats fed control, HP- LCa 2+ , and HP-HCa 2+ diets. ( C ) The levels of renal proteins were quantified using ImageJ software (n = 6 per group). ( D, E ) Time course analysis of serum levels of intact FGF23 ( D ) and C-terminal FGF23 ( E ) in rats fed control, HP-LCa 2+ , and HP-HCa 2+ diets. ( F ) Representative immunohistochemical staining of EDTA-decalcified femur sections for FGF23 from rats fed control, HP-LCa 2+ , and HP-HCa 2+ diets. All data are presented as the mean ± SD of each group (n = 3–8 per group). *, p<0.05; **, p<0.01; ***, p<0.001, compared with controls.

Article Snippet: Rat intact PTH (Immutopics, San Clemente, CA, USA), human intact PTH (Abcam), soluble RANKL (Immundiagnostik, Bensheim, Germany), osteoprotegerin (Alpco Immunoassay, Salem, NH, USA), rat intact and C-terminal FGF23 (Elabscience, Houston, TX, USA), and human intact FGF23 (Elabscience) were measured using enzyme-linked immunosorbent assay.

Techniques: Expressing, Control, Western Blot, Software, Immunohistochemical staining, Staining

Journal: eLife

Article Title: High-phytate/low-calcium diet is a risk factor for crystal nephropathies, renal phosphate wasting, and bone loss

doi: 10.7554/eLife.52709

Figure Lengend Snippet:

Article Snippet: Rat intact PTH (Immutopics, San Clemente, CA, USA), human intact PTH (Abcam), soluble RANKL (Immundiagnostik, Bensheim, Germany), osteoprotegerin (Alpco Immunoassay, Salem, NH, USA), rat intact and C-terminal FGF23 (Elabscience, Houston, TX, USA), and human intact FGF23 (Elabscience) were measured using enzyme-linked immunosorbent assay.

Techniques: Control, Enzyme-linked Immunosorbent Assay, RIA Assay, Staining, Colorimetric Assay, Blocking Assay, Recombinant, In Vitro, Software

Journal: BMJ Open

Article Title: Association between serum vitamin B 6 concentration and risk of osteoporosis in the middle-aged and older people in China: a cross-sectional study

doi: 10.1136/bmjopen-2018-028129

Figure Lengend Snippet: Comparison of serum Vit B 6 and serological metabolism parameters among control, osteopenia and osteoporosis groups

Article Snippet: The concentration of fibroblast growth factor 23 (FGF23) was measured through an ELISA performed using a human FGF23 ELISA kit (CSB-E10113h, Cusabio Biotech, Wuhan, China) and a micro plate reader (MK3, Thermo, Waltham, Massachusetts, USA).

Techniques: Comparison, Control

Journal: BMJ Open

Article Title: Association between serum vitamin B 6 concentration and risk of osteoporosis in the middle-aged and older people in China: a cross-sectional study

doi: 10.1136/bmjopen-2018-028129

Figure Lengend Snippet: Relationship between serum Vit B 6 concentrations and bone metabolism parameter concentrations in control, osteopenia and osteoporosis groups

Article Snippet: The concentration of fibroblast growth factor 23 (FGF23) was measured through an ELISA performed using a human FGF23 ELISA kit (CSB-E10113h, Cusabio Biotech, Wuhan, China) and a micro plate reader (MK3, Thermo, Waltham, Massachusetts, USA).

Techniques: Control

Journal: Frontiers in endocrinology

Article Title: In Vivo Analysis of the Contribution of Proprotein Convertases to the Processing of FGF23.

doi: 10.3389/fendo.2021.690681

Figure Lengend Snippet: FIGURE 1 | Increased FGF23 level and reduced phosphate excretion in Furinosb-/- mice. FGF23 and phosphate levels in in 4-month-old Furinflox/flox (n=6) and Furinosb-/- (n=6) mice fed on standard chow diet (see Material and Methods) (A–D). Intact FGF23 levels in plasma (A). FGF23 target genes expression in kidney (B). Serum phosphate level (C). Von Kossa/van Gieson staining on vertebrae sections (D). FGF23 and phosphate parameters in 6-months-old Furinflox/flox (n=6) and Furinosb-/- (n=6-7) mice fed a normal phosphate diet (0.6%; see Material and Methods) or a low phosphate diet (0.02%; see Material and Methods) for one week (E–N). Body weight (E). Kidney weight normalize to body weight (F). Serum phosphate levels (G). Plasma level of C-terminal FGF23 (H), intact FGF23 (I), percentage (%) of intact over C-terminal FGF23 (J) and cleaved FGF23 levels (K) calculated as (C-terminal FGF23) - (intact FGF23). Expression level in kidney of the sodium phosphate cotransporter Slc34a1 (L) and Slc34a3 (M). (N) Urine phosphate measurements normalized to creatinine. Results represent the mean ± SEM. *P < 0.05, **P < 0.01, and ***P < 0.001, by 2-way ANOVA with Bonferroni’s multiple comparisons test or by Student’s t-test (A–C, G, H, K, M) #: P<0.05; ##: P<0.01; &: 0.05

Article Snippet: Intact and C-terminal FGF23 measurements were performed on EDTA plasma collected from mice under fed conditions using ELISA assays specific for mouse intact or C-terminal FGF23 (Quidel, cat#: 60-6800 and cat#: 60-6300).

Techniques: Clinical Proteomics, Expressing, Staining

Journal: Frontiers in endocrinology

Article Title: In Vivo Analysis of the Contribution of Proprotein Convertases to the Processing of FGF23.

doi: 10.3389/fendo.2021.690681

Figure Lengend Snippet: FIGURE 2 | Impaired FGF23 processing in Furinosb-/- mice following iron restriction. Furinflox/flox (n=3-5) and Furinosb-/- (n=7-8) 21-day-old mice were fed normal chow diet (ND) or a low iron diet (LI) for 14 weeks. (A) Body weight growth curve presented as percentage of initial body weight. (B, C) Expression of iron-regulated genes in liver. Hepcidin (Hamp) expression (B). Transferrin receptor (Tfrc) expression (C). (D) Fgf23 expression in long bone. (E–H) Plasma level of C-terminal FGF23 (E), intact FGF23 (F), percentage (%) of intact over C-terminal FGF23 (G) and cleaved FGF23 levels (H), calculated as (C-terminal FGF23) - (intact FGF23). (I) Serum phosphate levels. Results represent the mean ± SEM. *P < 0.05, **P < 0.01, and ***P < 0.001, by 2-way ANOVA with Bonferroni’s multiple comparisons test or by Student’s t-test (D–F) #: P<0.05; ##: P<0.01; &: 0.05

Article Snippet: Intact and C-terminal FGF23 measurements were performed on EDTA plasma collected from mice under fed conditions using ELISA assays specific for mouse intact or C-terminal FGF23 (Quidel, cat#: 60-6800 and cat#: 60-6300).

Techniques: Expressing, Clinical Proteomics

Journal: Frontiers in endocrinology

Article Title: In Vivo Analysis of the Contribution of Proprotein Convertases to the Processing of FGF23.

doi: 10.3389/fendo.2021.690681

Figure Lengend Snippet: FIGURE 3 | FGF23 is normally processed following erythropoietin and IL-1b injection in Furinosb-/- mice. Genes expression in long bone (A, B, E) and bone marrow (C, D, F) of 2-month-old C57BL/6J mice 6 hours following the injection of vehicle (n=4), 300 U/kg (n=4) or 3000 U/kg (n=4) of recombinant human erythropoietin (rhEPO). Erythropoietin receptor (Epor) (A, C), erythroferrone (Erfe) (B, D) and FGF23 (Fgf23) (C, F). (G–J) Plasma FGF23 measurements in 4-month- old Furinflox/flox (n=3) and Furinosb-/- (n=3) mice 6 hours following the injection of vehicle, 300 U/kg or 3000 U/kg of rhEPO. C-terminal FGF23 (G), intact FGF23 (H), percentage (%) of intact over C-terminal FGF23 (I) and cleaved FGF23 levels (J), calculated as (C-terminal FGF23) - (intact FGF23). (K–N) Plasma FGF23 measurements in 4-month-old Furinflox/flox (n=4) and Furinosb-/- (n=4) mice before (T0) and 6 hours following the injection of 50 ng/g IL-1b (T=6hrs). C-terminal FGF23 (K), intact FGF23 (L), percentage (%) of intact over C-terminal FGF23 (M) and cleaved FGF23 levels (N). Results represent the mean ± SEM. *P < 0.05, **P < 0.01, and ***P < 0.001, by 1-way ANOVA (A–F) or 2-way ANOVA (G–N) with Bonferroni’s multiple comparisons test, or by Student’s t-test (A, E, F) #: P<0.05; ##: P<0.01, ###: P<0.001.

Article Snippet: Intact and C-terminal FGF23 measurements were performed on EDTA plasma collected from mice under fed conditions using ELISA assays specific for mouse intact or C-terminal FGF23 (Quidel, cat#: 60-6800 and cat#: 60-6300).

Techniques: Injection, Expressing, Recombinant, Clinical Proteomics

Journal: Frontiers in endocrinology

Article Title: In Vivo Analysis of the Contribution of Proprotein Convertases to the Processing of FGF23.

doi: 10.3389/fendo.2021.690681

Figure Lengend Snippet: FIGURE 4 | Furin inactivation in osteoblasts, osteocytes and hematopoietic cells did not impair FGF23 processing following erythropoietin injection. Plasma FGF23 measurements in 8-week-old Furinflox/flox (n=7), Furinosb-/- (n=5), Furinosb-/- (n=5) and Furinosb;BM-/- (n=6) male and female mice 6 hours following injection of vehicle or 3000 U/kg of recombinant human erythropoietin (rhEPO): C-terminal FGF23 (A), intact FGF23 (B), percentage (%) of intact over C-terminal FGF23 (C) and cleaved FGF23 levels (D), calculated as (C-terminal FGF23) - (intact FGF23). Results represent the mean ± SEM. *P < 0.05 and ***P < 0.001, by 2-way ANOVA with Bonferroni’s multiple comparisons test.

Article Snippet: Intact and C-terminal FGF23 measurements were performed on EDTA plasma collected from mice under fed conditions using ELISA assays specific for mouse intact or C-terminal FGF23 (Quidel, cat#: 60-6800 and cat#: 60-6300).

Techniques: Injection, Clinical Proteomics, Recombinant

Journal: Frontiers in endocrinology

Article Title: In Vivo Analysis of the Contribution of Proprotein Convertases to the Processing of FGF23.

doi: 10.3389/fendo.2021.690681

Figure Lengend Snippet: FIGURE 5 | Multiple proprotein convertases can process FGF23 in mammalian cells. (A) Western blot analysis of the secretion media (SM) from CHO-K1 cells transfected with V5 tagged human FGF23 (hFGF23-V5) and cultured in the absence (–) or presence (+) of PC inhibitors, decanoyl-RVKR-CMK (RVKR) (50 mM) or hexa- D-arginine (D6R) (20 mM). (B) Western blot analysis of the secretion media (SM) from CHO furin-deficient FD11 cells co-transfected with V5 tagged human FGF23 (hFGF23-V5) and proprotein convertase Furin, PC5A, PC5B, PACE4 or PC7. Intact and processed C-terminal (CT) FGF23 forms are detected with V5 antibody.

Article Snippet: Intact and C-terminal FGF23 measurements were performed on EDTA plasma collected from mice under fed conditions using ELISA assays specific for mouse intact or C-terminal FGF23 (Quidel, cat#: 60-6800 and cat#: 60-6300).

Techniques: Western Blot, Transfection, Cell Culture

Journal: Frontiers in endocrinology

Article Title: In Vivo Analysis of the Contribution of Proprotein Convertases to the Processing of FGF23.

doi: 10.3389/fendo.2021.690681

Figure Lengend Snippet: FIGURE 6 | Genetic ablation of PC5 alone or in combination with Furin does not impair FGF23 processing in vivo. Plasma intact FGF23 (A) and serum phosphate levels (B) in 4-month-old Pcsk5flox/flox (n=6) and Pcsk5osb-/- (n=7) mice fed a normal chow diet. (C) Von Kossa/van Gieson staining of vertebrae sections of Pcsk5flox/flox and Pcsk5osb-/-. (D) Plasma intact FGF23 in 6-month-old Furin;Pcsk5flox/flox (n=7-8) and Furin;Pcsk5osb-/- (n=8) fed a normal phosphate diet (0.6%) or a low phosphate diet (0.02%) for one week. (E, H) Plasma FGF23 measurements in 4-month-old Furin;Pcsk5flox/flox (n=4) and Furin;Pcsk5osb-/- (n=4) 6 hours following an injection of vehicle and 300 U/kg of recombinant human erythropoietin (rhEPO): C-terminal FGF23 (E), intact FGF23 (F), percentage (%) of intact over C-terminal FGF23 (G) and cleaved FGF23 levels (H), calculated as (C-terminal FGF23) - (intact FGF23). Results represent the mean ± SEM. *P < 0.01, **P < 0.01 and ***P < 0.001, by 2-way ANOVA with Bonferroni’s multiple comparisons test, or by Student’s t-test (A, B).

Article Snippet: Intact and C-terminal FGF23 measurements were performed on EDTA plasma collected from mice under fed conditions using ELISA assays specific for mouse intact or C-terminal FGF23 (Quidel, cat#: 60-6800 and cat#: 60-6300).

Techniques: In Vivo, Clinical Proteomics, Staining, Injection, Recombinant

Journal: Frontiers in endocrinology

Article Title: In Vivo Analysis of the Contribution of Proprotein Convertases to the Processing of FGF23.

doi: 10.3389/fendo.2021.690681

Figure Lengend Snippet: FIGURE 7 | PACE4 inactivation in mice does not impair FGF23 processing. Plasma FGF23 measurements in 4-month-old Pcsk6 +/+ (n=4) and Pcsk6 -/- (n=4) male mice before (T0) and 6 hours following the injection of 50 ng/g of IL-1b: C-terminal FGF23 (A), intact FGF23 (B), percentage (%) of intact over C-terminal FGF23 (C), and cleaved FGF23 levels (D), calculated as (C-terminal FGF23) - (intact FGF23). Results represent the mean ± SEM. *P < 0.01, **P < 0.01 and ***P < 0.001, by 2-way ANOVA with Bonferroni’s multiple comparisons test.

Article Snippet: Intact and C-terminal FGF23 measurements were performed on EDTA plasma collected from mice under fed conditions using ELISA assays specific for mouse intact or C-terminal FGF23 (Quidel, cat#: 60-6800 and cat#: 60-6300).

Techniques: Clinical Proteomics, Injection

Journal: Scientific Reports

Article Title: FGF23, a novel muscle biomarker detected in the early stages of ALS

doi: 10.1038/s41598-021-91496-6

Figure Lengend Snippet: FGF23 mRNA levels are increased in ALS muscle tissue. FGF23 mRNA levels were assessed in human muscle samples by qPCR using GAPDH as an internal housekeeping control. Disease samples were expressed as a fold-change (mean ± SEM) compared to normal control tissue (set at 1). *** P = 0.0001. BI, biceps brachii; DL, deltoid; GC, gastrocnemius; Myo, myopathy disease control; neuro, neuropathy disease control, TA, tibialis anterior; VL, vastus lateralis.

Article Snippet: Human plasma FGF-23 was analyzed using U-PLEX Human FGF-23 Assay (K1516EK, MSD), and mouse plasma FGF23 was measure using mouse/rat FGF23 (intact) ELISA kit (60-6800, Quidel) according to the manufacturer’s instruction.

Techniques: Control

Journal: Scientific Reports

Article Title: FGF23, a novel muscle biomarker detected in the early stages of ALS

doi: 10.1038/s41598-021-91496-6

Figure Lengend Snippet: FGF23 protein is increased in ALS muscle tissue. Sections from 6 ALS and 4 normal muscle biopsy samples were immunostained with an anti-FGF23 antibody and counterstained with Hoechst and wheat germ agglutin (WGA). All 6 ALS patient samples but no control samples showed positive staining. Three of the ALS and two of the normal control sections are shown here. ALSp1 (deltoid), ALSp2 (vastus lateralis), ALSp3 (vastus lateralis), Ctrl1 (deltoid), Ctrl 2 (vastus lateralis). Asterisks highlight areas of grouped atrophy and arrowheads highlight several of the loci where FGF23 and WGA immunostaining colocalizes. Scale bars, 100 μm.

Article Snippet: Human plasma FGF-23 was analyzed using U-PLEX Human FGF-23 Assay (K1516EK, MSD), and mouse plasma FGF23 was measure using mouse/rat FGF23 (intact) ELISA kit (60-6800, Quidel) according to the manufacturer’s instruction.

Techniques: Control, Staining, Immunostaining

Journal: Scientific Reports

Article Title: FGF23, a novel muscle biomarker detected in the early stages of ALS

doi: 10.1038/s41598-021-91496-6

Figure Lengend Snippet: FGF23 immunoreactivity is higher in areas of grouped atrophy in human ALS muscle tissue. Using ImageJ Fluorescence Intensity (FI) Analysis function, we compared the FGF23 FI (per μM 2 ) of 37 atrophic fibers (< 25 μM minimal feret’s diameter) sampled from areas of grouped atrophy seen in 5 human ALS muscle samples with 37 non-atrophic fibers (> 25 μM minimal feret’s diameter) from the same sections. Representative photomicrographs of patient ALSp1 are shown with regions of interest highlighted for 6 grouped atrophic fibers (AF) and 6 non-atrophic fibers (NAF). An FGF23 intensity ratio was calculated by dividing the FI in atrophic fibers by the FI in non-atrophic factors for each patient. A ratio was also calculated between a similar number of non-atrophic fibers in the same section to the NAF region of interest as a control. The FI ratio was nearly sixfold higher in areas of grouped atrophy versus non-atrophic fibers. ** P = 0.006. Scale bar, 100 μm.

Article Snippet: Human plasma FGF-23 was analyzed using U-PLEX Human FGF-23 Assay (K1516EK, MSD), and mouse plasma FGF23 was measure using mouse/rat FGF23 (intact) ELISA kit (60-6800, Quidel) according to the manufacturer’s instruction.

Techniques: Fluorescence, Control

Journal: Scientific Reports

Article Title: FGF23, a novel muscle biomarker detected in the early stages of ALS

doi: 10.1038/s41598-021-91496-6

Figure Lengend Snippet: FGF23 is increased in SOD1 G93A muscle. ( A ) The clinical timeline of disease progression in the SOD1 G93A mouse is shown above . Below is a qPCR analysis of gastrocnemius muscle samples from littermate controls (WT) and SOD1 G93A mice at different ages as indicated. Data points are the mean ± SEM of 6–8 mice. * P < 0.05, *** P < 0.0005. ( B ) Photomicrographs of gastrocnemius muscle sections from a WT and SOD1 G93A mouse (60 d) immunostained with an anti-FGF23 antibody and counterstained with Hoechst and WGA. Scale bar, 100 μm. Arrowheads highlight several areas of merged FGF23 and WGA staining. ( C ) ELISA analysis of FGF23 in plasma samples obtained at the ages indicated. Data points are the mean ± SEM of 3 mice per group. ** P < 0.01.

Article Snippet: Human plasma FGF-23 was analyzed using U-PLEX Human FGF-23 Assay (K1516EK, MSD), and mouse plasma FGF23 was measure using mouse/rat FGF23 (intact) ELISA kit (60-6800, Quidel) according to the manufacturer’s instruction.

Techniques: Biomarker Discovery, Staining, Enzyme-linked Immunosorbent Assay, Clinical Proteomics

Journal: Scientific Reports

Article Title: FGF23, a novel muscle biomarker detected in the early stages of ALS

doi: 10.1038/s41598-021-91496-6

Figure Lengend Snippet: Plasma FGF23 concentration.

Article Snippet: Human plasma FGF-23 was analyzed using U-PLEX Human FGF-23 Assay (K1516EK, MSD), and mouse plasma FGF23 was measure using mouse/rat FGF23 (intact) ELISA kit (60-6800, Quidel) according to the manufacturer’s instruction.

Techniques: Clinical Proteomics, Concentration Assay, Control

Journal: Scientific Reports

Article Title: FGF23, a novel muscle biomarker detected in the early stages of ALS

doi: 10.1038/s41598-021-91496-6

Figure Lengend Snippet: FGF23 in human plasma samples from ALS patients and healthy controls. ( A ) Baseline levels of log-transformed plasma FGF23 concentration (pg/ml) among controls, and faster and slower progressing ALS patients. Boxes show median (middle line), and 25th and 75th percentiles (lower and upper border, respectively); whiskers extend to a maximum of 1.5 × interquartile range (IQR), or to the most extreme value if it is less than 1.5 × IQR from the 25th or 75th percentile. ( B ) Longitudinal changes in log-transformed plasma FGF23 among controls. ( C ) Longitudinal changes in log-transformed plasma FGF23 among ALS slower progressors (ALSFRS-R decline < 0.8 point/month). ( D ) Longitudinal changes in log-transformed plasma FGF23 among ALS faster progressors (ALSFRS-R decline > 1.2 points/month).

Article Snippet: Human plasma FGF-23 was analyzed using U-PLEX Human FGF-23 Assay (K1516EK, MSD), and mouse plasma FGF23 was measure using mouse/rat FGF23 (intact) ELISA kit (60-6800, Quidel) according to the manufacturer’s instruction.

Techniques: Clinical Proteomics, Transformation Assay, Concentration Assay

Journal: Journal of orthopaedic research : official publication of the Orthopaedic Research Society

Article Title: FGF23 is a putative marker for bone healing and regeneration.

doi: 10.1002/jor.20857

Figure Lengend Snippet: Figure 1. Serum FGF23 levels in pa- tients undergoing hip replacement therapy. Pilot study. (A) FGF23 (C-Term) serum levels of 55 patients before and 3 days after hip replacement after aseptic loosening. Prospective study. (B) FGF23 (C-Term, black bars) and intact (grey bars) levels from stored serum samples of 40 patients before and 1, 4, and 10 days after primary hip arthroplasty. Comparison of FGF23 C- Term intact ELISA. (C) FGF23 (C-Term) (black bars) and intact (grey bars) levels from freshly collected serum levels of 10 patients before and 1 day after surgery (**p < 0.001; *p < 0.05, Mann-Whitney test).

Article Snippet: Deparaffinized and rehydrated sections were pretreated with trypsin, blocked with 1% normal rabbit serum, and incubated with a monoclonal antimouse antibody to FGF23 from rat (1:200; R&D Systems).

Techniques: Comparison, Enzyme-linked Immunosorbent Assay, MANN-WHITNEY

Journal: Journal of orthopaedic research : official publication of the Orthopaedic Research Society

Article Title: FGF23 is a putative marker for bone healing and regeneration.

doi: 10.1002/jor.20857

Figure Lengend Snippet: Figure 3. Immunohistochemical characterization of FGF23-producing cells in ovine healthy bone (A) and fracture callus at day 9 (B,C) and day 21 (D) postoperatively. Arrowheads indicate FGF23 immu- noreactivity in periosteal cells (A), cells of the granulation tissue (B), and osteoblasts actively involved in deposition of new bone (C,D). Arrows mark FGF23 immunopositive mature (A) and newly formed osteocytes (C,D). Specific regions are labeled as follows: CtB, cortical bone; GT, granulation tissue; Ps, periosteum; WoB, woven bone. Scale bars: 25 mm (A,D), 50 mm (B,C).

Article Snippet: Deparaffinized and rehydrated sections were pretreated with trypsin, blocked with 1% normal rabbit serum, and incubated with a monoclonal antimouse antibody to FGF23 from rat (1:200; R&D Systems).

Techniques: Immunohistochemical staining, Labeling