Journal: American journal of physiology. Endocrinology and metabolism

Article Title: Myostatin propeptide mutation of the hypermuscular Compact mice decreases the formation of myostatin and improves insulin sensitivity.

doi: 10.1152/ajpendo.00216.2016

Figure Lengend Snippet: Fig. 3. Myostatin level in skeletal muscle of Compact, congenic wild-type, and BALB/c mice. M. gastrocnemius protein extracts were subjected to SDS-PAGE and blotted with anti-myostatin or anti-propeptide antibody. Represen- tative images are shown. Note the presence of mature myostatin dimer and myostatin propeptide in Compact sam- ples. Mouse recombinant myostatin was used as a positive control, and muscle homogenates of myostatin knockout (KO) mice served as a negative control. Differences in glycosylation may cause altered electrophoretic mobility. Bar diagrams show the quantification of the results. Data are reported as means SE; n 5 Compact, 5 congenic wild-type, and 6 BALB/c mice. *P 0.05; **P 0.01; ***P 0.001.

Article Snippet: Mouse recombinant myostatin (788-G8; R&D Systems) was used as a positive control.

Techniques: SDS Page, Recombinant, Positive Control, Knock-Out, Negative Control, Glycoproteomics

Journal: American journal of physiology. Endocrinology and metabolism

Article Title: Myostatin propeptide mutation of the hypermuscular Compact mice decreases the formation of myostatin and improves insulin sensitivity.

doi: 10.1152/ajpendo.00216.2016

Figure Lengend Snippet: Fig. 5. Glucose tolerance and insulin sensitivity are improved by Compact myostatin mutation and reduced in congenic wild-type mice. Intraperitoneal (ip) glucose tolerance (A and B) and insulin sensitivity tests (C and D) of 3- to 4-mo-old (A and C) and 10-mo-old animals (B and D). Area under the curve (AUC) values are presented in bar diagrams. Data are reported as means SE. *P 0.05 and **P 0.01; n 3 Compact, 7 congenic wild-type, and 3 BALB/c mice (A), n 7 Compact, 3 congenic wild-type, and 6 BALB/c mice (B), n 3 Compact, 3 congenic wild-type, and 4 BALB/c mice (C), and n 6 Compact, 4 congenic wild-type, and 4 BALB/c mice (D).

Article Snippet: Mouse recombinant myostatin (788-G8; R&D Systems) was used as a positive control.

Techniques: Mutagenesis

Journal: Biology

Article Title: Transdifferentiation of Human Fibroblasts into Skeletal Muscle Cells: Optimization and Assembly into Engineered Tissue Constructs through Biological Ligands

doi: 10.3390/biology10060539

Figure Lengend Snippet: Determination of efficacy of C2C12 differentiation in conjunction with the exposure to ligand combinations. C2C12s were differentiated for 7 days and treated with combination ligands of GDF11 (G), TMSB4X (T), IL6 (I), and TNF-α (F) at 10 ng/mL for seven additional days. ( A ) Fusion index was calculated from total myotube nuclei vs. total nuclei ( n = 16, mean + SD). ( B ) Multinucleation of C2C12 myotubes were quantified ( n = 11, mean + SD). ( C ) Nuclear density was evaluated from nuclear count per field of 5x microscopy ( n = 4, mean + SD). ( D ) C2C12 exposed to ligand combinations were stained to express nuclear MYOD1 ( n = 6, mean + SD). ( E ) Cells were stained with Ki67, and where similarly quantified based on average total nuclear count ( n = 6, mean + SD). ( F ) ACTN2 and Ki67 immunostaining of control cells. ( G ) Cells exposed to GTF showed decreases in fusion index and myonucleation levels, although no change in nuclear density and Ki67+ expression was detected. ( H ) GTIF supplementation significantly reduced skeletal muscle differentiation parameters fusion index and multinucleation, in addition to decreasing average nuclear density. ( I ) Control C2C12s expressing nuclear MYOD1. ( J ) GTF treatment greatly reduced nuclear fusion and showed limited differentiation capacity while expressing comparable levels of nuclear MYOD1. ( K ) Exposure of C2C12s to GTIF combination significantly inhibited skeletal muscle differentiation. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

Article Snippet: Proteins utilized included recombinant human Follistatin (Fs, 669-FO-025), recombinant human Myostatin (GDF8, 788-G8-010) or Growth Differentiation factor (GDF8), recombinant human basic Fibroblast Growth Factor 2 (FGF2, 233-FB-025), recombinant human GDF11 (1958-GD-010), recombinant human GDF15 (957-GD-025/CF), recombinant human Bone Morphogenetic Protein 4 (BMP4, 314-BP-010/CF), recombinant human BMP7 (354-BP-010), recombinant human Growth Hormone (hGH, 1067-GH-025), recombinant human Interleukin 6 (IL6, 206-IL-010), recombinant human Tumor Necrosis Factor Alpha (TNF-α, 210-TA-005) (All R&D Systems), and Thymosin β (TOCRIS, 3390).

Techniques: Microscopy, Staining, Immunostaining, Control, Expressing

Journal: Biology

Article Title: Transdifferentiation of Human Fibroblasts into Skeletal Muscle Cells: Optimization and Assembly into Engineered Tissue Constructs through Biological Ligands

doi: 10.3390/biology10060539

Figure Lengend Snippet: Effect of ligand combination exposure on differentiation of skeletal muscle cells derived from tHFs. Cells were transduced with MYOD1 fragments and induced to express the skeletal muscle phenotype via the induction of doxycycline and SB431542 over a 7-day period. Ligand combinations of GDF11 (G), TMSB4X (T), IL6 (I), and TNF-α (F) at 10 ng/mL were introduced for an additional week, and SB and Dox administration was discontinued. Skeletal muscle cells were fixed and stained on day 14 and characterized by various differentiation and proliferation parameters from 5× microscopy. ( A ) Fusion index of tHFs was evaluated by determining the ratio of myotube nuclei vs total nuclear count ( n = 16, mean + SD). ( B ) Cellular multinucleation was quantified to assess tHF development of differentiation ( n = 22, mean + SD). ( C ) Nuclear density was similarly assessed by quantifying nuclear count per field ( n = 4, mean + SD). ( D ) Nuclear MYOD1 was quantified ( n = 6, mean + SD). ( E ) Ki67 nuclei were also assessed with a nuclear count ( n = 6, mean + SD). ( F ) Control tHF myotubes were immunostained with ACTN2 and Ki67. ( G ) IL6 and TNF-α combination demonstrated significant decrease in differentiation parameters fusion index, multinucleation, myotube length, and diameter , although Ki67+ expression had increased. ( H ) Exposure of tHFs to combined GDF11, TMSB4X, IL6, and TNF-α showed similar results, however nuclear Ki67 expression was unchanged. ( I ) Untreated tHFs with ACTN2 and MYOD1 nuclear stains. ( J ) Cells treated with IF showed a decrease in MYOD1 nuclear expression. ( K ) Additionally, GDF11, TMSB4X, and IL6 exposure yielded similar results with respect to MYOD1+. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001.

Article Snippet: Proteins utilized included recombinant human Follistatin (Fs, 669-FO-025), recombinant human Myostatin (GDF8, 788-G8-010) or Growth Differentiation factor (GDF8), recombinant human basic Fibroblast Growth Factor 2 (FGF2, 233-FB-025), recombinant human GDF11 (1958-GD-010), recombinant human GDF15 (957-GD-025/CF), recombinant human Bone Morphogenetic Protein 4 (BMP4, 314-BP-010/CF), recombinant human BMP7 (354-BP-010), recombinant human Growth Hormone (hGH, 1067-GH-025), recombinant human Interleukin 6 (IL6, 206-IL-010), recombinant human Tumor Necrosis Factor Alpha (TNF-α, 210-TA-005) (All R&D Systems), and Thymosin β (TOCRIS, 3390).

Techniques: Derivative Assay, Transduction, Staining, Microscopy, Control, Expressing

Journal: Biology

Article Title: Transdifferentiation of Human Fibroblasts into Skeletal Muscle Cells: Optimization and Assembly into Engineered Tissue Constructs through Biological Ligands

doi: 10.3390/biology10060539

Figure Lengend Snippet: Skeletal muscle tissues were engineered from a composite fibrin/Matrigel hydrogel mixture with mouse skeletal myoblasts C2C12s, and subject to 10 ng/mL biological ligands. C2C12s were encapsulated and differentiated in a fibrin-based hybrid hydrogel over a 7-day period, 10 ng/mL biological ligands GDF11, TMSB4X, IL6 or TNF-α were administered after a week of tissue plating. ( A ) Immunohistochemical staining of C2C12 skeletal muscle constructs with ACTN2 and DAPI, demonstrated high cellular density. ( B ) Skeletal myotubes increased compactness and alignment towards central pillar regions where tensile force is maximal ( C ) Structural organization of C2C12s at pillar regions appeared disrupted due to gel contraction. ( D ) Cross-striated, multinucleated skeletal muscle form condensed tissues as demonstrated with high magnification 60× confocal microscopy. ( E ) Myotube diameter (µm) was not affected by one-week exposure to 10 ng/mL ligands. ( n > 32, mean + SD). ( F ) Nuclear density of skeletal muscle C2C12s within tissue were not impacted with ligand administration. ( n = 6, mean + SD).

Article Snippet: Proteins utilized included recombinant human Follistatin (Fs, 669-FO-025), recombinant human Myostatin (GDF8, 788-G8-010) or Growth Differentiation factor (GDF8), recombinant human basic Fibroblast Growth Factor 2 (FGF2, 233-FB-025), recombinant human GDF11 (1958-GD-010), recombinant human GDF15 (957-GD-025/CF), recombinant human Bone Morphogenetic Protein 4 (BMP4, 314-BP-010/CF), recombinant human BMP7 (354-BP-010), recombinant human Growth Hormone (hGH, 1067-GH-025), recombinant human Interleukin 6 (IL6, 206-IL-010), recombinant human Tumor Necrosis Factor Alpha (TNF-α, 210-TA-005) (All R&D Systems), and Thymosin β (TOCRIS, 3390).

Techniques: Immunohistochemical staining, Staining, Construct, Confocal Microscopy

Journal: Nature

Article Title: PTER is a N -acetyltaurine hydrolase that regulates feeding and obesity

doi: 10.1038/s41586-024-07801-6

Figure Lengend Snippet: a , b , Change in body weight ( a ) and food intake ( b ) of 26–28-week-old male DIO C57BL/6J mice following 7 days of treatment with the indicated dose of N -acetyltaurine (NAT; i.p.). For saline versus N -acetyltaurine (15 mg per kg per day), P = 5.95 × 10 –4 ; for saline versus N -acetyltaurine (50 mg per kg per day), P = 6.3 × 10 –4 . N = 5 per group for vehicle, 1 and 5 mg per kg per day; N = 6 per group for 15 and 50 mg per kg per day. c , d , Change in body weight ( c ) and food intake ( d ) of 19–21-week-old male DIO C57BL/6J mice following treatment with the indicated metabolite at a dose of 15 mg per kg per day (i.p.). N = 5 per group. e – g , Western blots with anti-PTER (top) and anti-tubulin (bottom) antibodies ( e ), N -acetyltaurine hydrolysis activity ( f ) and tissue N -acetyltaurine levels ( g ) from cortex (Cort.), hypothalamus (Hyp.) and brainstem (BS) of WT mice and Pter KO mice. For WT versus Pter KO brainstem, P = 6.65 × 10 –4 . N = 6 per group for f and g . h , Change in 24-h food intake of 6-month-old male DIO mice treated with a single dose of GDF15 (0.1 mg kg –1 , i.p.) in the presence of anti-GFRAL antibody (10 mg kg –1 , i.p.) or IgG control antibody (10 mg kg –1 , i.p.). N = 5 per group. i , j , Change in body weight ( i ) and cumulative food intake ( j ) of 16-week-old male DIO mice following saline or N -acetyltaurine (15 mg per kg per day, i.p.) treatment and with IgG or anti-GFRAL antibody co-treatment (10 mg kg –1 , i.p., once every 3 days). N = 10 per group. Data are shown as the mean ± s.e.m. For e , the loading control was performed on the same blot. In a – d and f – h , P values were calculated from two-tailed unpaired t -tests and were not corrected for multiple comparisons. In i and j , P values were calculated from two-way ANOVA with post hoc Sidak’s multiple comparisons test. All experiments were performed once.

Article Snippet: Recombinant GDF15 (957-GD) was purchased from R&D Systems.

Techniques: Saline, Western Blot, Activity Assay, Control, Two Tailed Test

Journal: Nature

Article Title: PTER is a N -acetyltaurine hydrolase that regulates feeding and obesity

doi: 10.1038/s41586-024-07801-6

Figure Lengend Snippet: Related to Fig. . a - d , Body weight ( a , b ) and food intake ( c , d ) of 6 to 7-month-old DIO male C57BL/6J mice after a 7-day treatment of saline or N-acetyltaurine (15 mg/kg/day, IP) or GLP-1 (2 mg/kg/day, IP) with or without Exendin-3 (0.1 mg/kg/day, IP). N = 7/group. NAT, N-acetyltaurine. e , f , Body weight ( e ) and food intake ( f ) of 5-month-old DIO male C57BL/6J mice or 3 to 4-month-old MC4R-KO mice on high fat diet after a 7-day treatment of saline or N-acetyltaurine (15 mg/kg/day, IP). N = 6/group. NAT, N-acetyltaurine. g , Plasma GDF15 (left), GLP-1 (middle) and leptin (right) levels of 19 to 21-week-old male DIO C57BL/6J mice following treatment with N-acetyltaurine 15 mg/kg/day (IP) or saline. N = 5 per group. NAT, N-acetyltaurine. Data are shown as mean ± SEM. P-values were calculated from two-tailed unpaired t-tests.

Article Snippet: Recombinant GDF15 (957-GD) was purchased from R&D Systems.

Techniques: Saline, Clinical Proteomics, Two Tailed Test

Journal: Molecular Neurodegeneration

Article Title: Network-driven plasma proteomics expose molecular changes in the Alzheimer’s brain

doi: 10.1186/s13024-016-0095-2

Figure Lengend Snippet: GDF3 regulates neurogenesis and is reduced in AD brains. a To test whether GDF3 levels are also reduced in AD brains, Human AD and control cortical grey matter regions were lysed and the detergent soluble protein fraction was probed by western blot. Levels of active GDF3 ( b ) were quantified relative to neuron-specific enolase (NSE). c To identify areas in the brain where GDF3 may have a functional role, we referred to The Allen Brain Atlas, which showed strong RNA expression in the mouse hippocampus (blue = high expression). d Using qPCR, GDF3 mRNA expression was detected in non-differentiated adult mouse NPCs and NPCs cultured in differentiating conditions. e To determine whether GDF3 affects stem cell function, adult mouse NPCs were provided recombinant mouse GDF3 and NPC proliferation was assessed using BrdU. f Recombinant mouse GDF3 was also provided to dissociated adult mouse neurospheres and the number of newly formed neurospheres was subsequently quantified. g To investigate whether GDF3 promotes neurogenesis, human-derived NTERA cells stably transfected with Dcx promoter-controlled eGFP were provided recombinant human GDF3. Shown are representative images of DCX-GFP fluorescence expression from an entire well of NTERA cells treated with GDF3 or control for 30 days. h DCX-GFP fluorescence area was quantified relative to the cellular area detected by brightfield microscopy. Results were compared by a one-way ANOVA with a Dunnett's post-test ( b , e ), an unpaired Student’s t test ( d ), or a two-way ANOVA with a Bonferroni post-test ( f , h ) and are representative of at least 2 independent experiments (b n = 16 –18 per group, d,e,f,h; n = 3 per group). Values are mean ± s.e.m.. * p < 0.05, ** p < 0.01, *** p < 0.001 compared to respective control groups

Article Snippet: One day after seeding, 10 μM of retinoic acid and designated concentrations of recombinant carrier-free human GDF3 (R&D Systems, Minneapolis, MN; at 0, 10, 50, or 150 ng/mL) were added to the culture media of each corresponding NTERA treatment well.

Techniques: Control, Western Blot, Functional Assay, RNA Expression, Expressing, Cell Culture, Cell Function Assay, Recombinant, Derivative Assay, Stable Transfection, Transfection, Fluorescence, Microscopy

Journal: Clinical and Experimental Medicine

Article Title: GDF15 activates human fibroblast MRC5 cells via miR-338/STAT1 in silicosis

doi: 10.1007/s10238-025-01627-w

Figure Lengend Snippet: Increased blood GDF15 expression in patients with silicosis. A , Serum GDF15 expression in patients with silicosis was higher than that in controls ( P = 0.0003, compared to control). B , Increased serum GDF15 expression did not relate to the FEV1% of patients with silicosis; P = 0.2002. C , Increased serum GDF15 expression did not relate to the clinical stages of silicosis, P = 0.5979

Article Snippet: Recombinant human GDF15 was purchased from R&D Systems (Minneapolis, MN, USA).

Techniques: Expressing, Control

Journal: Clinical and Experimental Medicine

Article Title: GDF15 activates human fibroblast MRC5 cells via miR-338/STAT1 in silicosis

doi: 10.1007/s10238-025-01627-w

Figure Lengend Snippet: GDF15 activates human embryonic lung fibroblast MRC5 cells. The effect of GDF15 on col1a and α-SMA protein expression in MRC5 cells was detected using western blotting. A , dosage course. B , time course. C , GDF15 increased the proliferation of MRC cells, as detected in the CCK-8 assay. D, GDF15 increased the migration of MRC cells, which was detected in the wound healing assay. Data represent the mean ± SD from three independent experiments.*,**, ♯ , P < 0.05

Article Snippet: Recombinant human GDF15 was purchased from R&D Systems (Minneapolis, MN, USA).

Techniques: Expressing, Western Blot, CCK-8 Assay, Migration, Wound Healing Assay

Journal: Clinical and Experimental Medicine

Article Title: GDF15 activates human fibroblast MRC5 cells via miR-338/STAT1 in silicosis

doi: 10.1007/s10238-025-01627-w

Figure Lengend Snippet: Effects of GDF15 on the miRNA and mRNA expression in MRC5 cells. Effect of GDF15 on the miRNA profile of MRC5 cells. A , heatmap; B , Volcano plots; C , KEGG analysis. Effect of GDF15 on the mRNA profile of MRC5 cells. D , heatmap; E, Volcano plots; F, KEGG analysis

Article Snippet: Recombinant human GDF15 was purchased from R&D Systems (Minneapolis, MN, USA).

Techniques: Expressing

Journal: Clinical and Experimental Medicine

Article Title: GDF15 activates human fibroblast MRC5 cells via miR-338/STAT1 in silicosis

doi: 10.1007/s10238-025-01627-w

Figure Lengend Snippet: GDF15 reduced the expression of miR-338 in MRC5 cells. A , qRT-PCR results showed that the expression of miR-338 was decreased in response to GDF15 expression. B , Western blotting results showed that miR-338 mimics attenuated the expression of col1a and α-SMA regardless of treatment with GDF15, whereas miR-338 inhibitors promoted the expression of col1 and α-SMA regardless of treatment with GDF15. C , CCK-8 assay results showed that miR-338 mimics reduced the growth rate and the miR-338 inhibitor increased the growth rate of MRC5 cells. Data represent the mean ± SD from three independent experiments.*,**, ♯ , P < 0.05

Article Snippet: Recombinant human GDF15 was purchased from R&D Systems (Minneapolis, MN, USA).

Techniques: Expressing, Quantitative RT-PCR, Western Blot, CCK-8 Assay

Journal: Clinical and Experimental Medicine

Article Title: GDF15 activates human fibroblast MRC5 cells via miR-338/STAT1 in silicosis

doi: 10.1007/s10238-025-01627-w

Figure Lengend Snippet: GDF15 increased STAT1 expression in MRC5 cells. A , Western blotting results showed that GDF15 induced STAT1 expression. B , Western blotting results showed that STAT1 siRNA attenuated the expression of col1a and α-SMA, whereas STAT1 cDNA promoted their expression in the presence or absence of GDF15 treatment. C , CCK-8 assay results showed that STAT1 siRNA reduced the growth rate, whereas STAT1 cDNA increased the growth rate of MRC5 cells. Data represent the mean ± SEM from three independent experiments.*,**, ♯ , P < 0.05

Article Snippet: Recombinant human GDF15 was purchased from R&D Systems (Minneapolis, MN, USA).

Techniques: Expressing, Western Blot, CCK-8 Assay

Journal: Clinical and Experimental Medicine

Article Title: GDF15 activates human fibroblast MRC5 cells via miR-338/STAT1 in silicosis

doi: 10.1007/s10238-025-01627-w

Figure Lengend Snippet: GDF15 activated MRC5 cells through the miR-338/STAT1 pathway. A , Using TargetScan ( http://www.targetscan.org/ ), the conserved miR-338 binding site in the 3’-UTR of STAT1 mRNA was constructed in the pmirGLO dual-luciferase miRNA target expression vector. Luciferase activity was analyzed in the MRC5 cells. MRC5 cells were co-transfected with miR-30 mimics and a luciferase reporter. B , miR-338 regulated STAT1 protein expression. C , miR-338 mimics attenuated the expression of col1 and α-SMA protein induced by STAT1 overexpression upon co-treatment with GDF15. D, STAT1 knockdown attenuated col1 and α-SMA protein expression induced by the miR-338 inhibitor upon co-treatment with GDF15. Data represent the means ± SD from three independent experiments. *,**, ♯ , ♯♯ , P < 0.05

Article Snippet: Recombinant human GDF15 was purchased from R&D Systems (Minneapolis, MN, USA).

Techniques: Binding Assay, Construct, Luciferase, Expressing, Plasmid Preparation, Activity Assay, Transfection, Over Expression, Knockdown

Journal: Theriogenology

Article Title: Effect of BMP15 and GDF9 in the IVM medium on subsequent oocyte competence and embryo development of prepubertal goats.

doi: 10.1016/j.theriogenology.2024.12.015

Figure Lengend Snippet: Fig. 1. Transzonal projections (TZP) density of COCs during IVM with BMP15 (A) and/or GDF9 (B). Phalloidin-FITC fluorescence intensity (mean ± S.E.M.) in the zona pellucida area of COCs after 0h, 6h, 12h and 24h of IVM. A total of 20–30 COCs per group were assessed in 3 replicates. (A) Values with different letters differ significantly (p < 0.05). (B) Different letters between groups in the same timepoint (a,b) and different symbols between timepoints in the same group (α,β,γ for control and GDF9 groups; and σ,τ for GDF9+BMP15 group) indicate significant differences (p < 0.05). (C) Representative confocal images of phalloidin-FITC staining. TZP are observed as thin filaments going through the zona pellucida from the cumulus cells to the oocyte. Scale bar: 100 μm.

Article Snippet: The IVM medium was supplemented with 100 ng/mL of recombinant human mature region BMP15 (R&D systems, Minnesota, USA) and/or 100 ng/mL of recombinant human mature region GDF9 (R&D systems), according to the experimental design, at the same concentrations as used in bovine [23,24] and porcine [25,26] IVM.

Techniques: Fluorescence, Control, Staining

Journal: Theriogenology

Article Title: Effect of BMP15 and GDF9 in the IVM medium on subsequent oocyte competence and embryo development of prepubertal goats.

doi: 10.1016/j.theriogenology.2024.12.015

Figure Lengend Snippet: Fig. 2. Mitochondrial activity of MII-oocytes after IVM with BMP15 and/or GDF9. (A) Relative fluorescence intensity (mean ± S.E.M.) of Mitotracker stained oocytes. Columns with different letters differ significantly (p < 0.05). A total of 20–27 oocytes per group were assessed in 3 replicates. (B) Representative images. Scale bar: 100 μm.

Article Snippet: The IVM medium was supplemented with 100 ng/mL of recombinant human mature region BMP15 (R&D systems, Minnesota, USA) and/or 100 ng/mL of recombinant human mature region GDF9 (R&D systems), according to the experimental design, at the same concentrations as used in bovine [23,24] and porcine [25,26] IVM.

Techniques: Activity Assay, Fluorescence, Staining

Journal: Theriogenology

Article Title: Effect of BMP15 and GDF9 in the IVM medium on subsequent oocyte competence and embryo development of prepubertal goats.

doi: 10.1016/j.theriogenology.2024.12.015

Figure Lengend Snippet: Fig. 3. ROS and GSH levels after IVM with BMP15 and/or GDF9. Relative fluorescence intensity (mean ± S.E.M.) of (A) ROS and (B) GSH. A total of 24–31 oocytes per group were assessed in 3 replicates. (C) Representative images. Scale bar: 200 μm.

Article Snippet: The IVM medium was supplemented with 100 ng/mL of recombinant human mature region BMP15 (R&D systems, Minnesota, USA) and/or 100 ng/mL of recombinant human mature region GDF9 (R&D systems), according to the experimental design, at the same concentrations as used in bovine [23,24] and porcine [25,26] IVM.

Techniques: Fluorescence

Journal: Theriogenology

Article Title: Effect of BMP15 and GDF9 in the IVM medium on subsequent oocyte competence and embryo development of prepubertal goats.

doi: 10.1016/j.theriogenology.2024.12.015

Figure Lengend Snippet: Fig. 4. EGFR expression of MII-oocytes after IVM with BMP15 (A) and/or GDF9 (B). Relative fluorescence intensity (mean ± S.E.M.) of EGFR immunostained oocytes. Columns with different letters differ significantly (p < 0.05). A total of 26–40 oocytes per group were assessed in 4 replicates. (C) Representative images. Scale bar: 30 μm.

Article Snippet: The IVM medium was supplemented with 100 ng/mL of recombinant human mature region BMP15 (R&D systems, Minnesota, USA) and/or 100 ng/mL of recombinant human mature region GDF9 (R&D systems), according to the experimental design, at the same concentrations as used in bovine [23,24] and porcine [25,26] IVM.

Techniques: Expressing, Fluorescence

Journal: Theriogenology

Article Title: Effect of BMP15 and GDF9 in the IVM medium on subsequent oocyte competence and embryo development of prepubertal goats.

doi: 10.1016/j.theriogenology.2024.12.015

Figure Lengend Snippet: Fig. 5. EGFR expression of cumulus cells after IVM with BMP15 (A) and/or GDF9 (B). Relative EGFR expression (mean ± S.E.M.). Columns with different letters differ significantly (p < 0.05). Four independent blots were used for relative quantification. (C) Western blot analyses of EGFR expression. EGFR from 70 to 80 COCs/ replicate was quantified by western blotting and standardized to vinculin protein levels.

Article Snippet: The IVM medium was supplemented with 100 ng/mL of recombinant human mature region BMP15 (R&D systems, Minnesota, USA) and/or 100 ng/mL of recombinant human mature region GDF9 (R&D systems), according to the experimental design, at the same concentrations as used in bovine [23,24] and porcine [25,26] IVM.

Techniques: Expressing, Quantitative Proteomics, Western Blot

Journal: Theriogenology

Article Title: Effect of BMP15 and GDF9 in the IVM medium on subsequent oocyte competence and embryo development of prepubertal goats.

doi: 10.1016/j.theriogenology.2024.12.015

Figure Lengend Snippet: Fig. 6. Cumulus expansion index after IVM with BMP15 (A) and/or GDF9 (B). Cumulus expansion of each COC was scored on a 0 to 4 scale and cumulus expansion index (mean ± S.E.M) was calculated as the arithmetic mean value scored of all COCs evaluated per replica. Columns with different letters differ significantly (p < 0.05). A total of 367–441(A) and 278–323 (B) oocytes per group were assessed in 5 replicates.

Article Snippet: The IVM medium was supplemented with 100 ng/mL of recombinant human mature region BMP15 (R&D systems, Minnesota, USA) and/or 100 ng/mL of recombinant human mature region GDF9 (R&D systems), according to the experimental design, at the same concentrations as used in bovine [23,24] and porcine [25,26] IVM.

Techniques:

Journal: Theriogenology

Article Title: Effect of BMP15 and GDF9 in the IVM medium on subsequent oocyte competence and embryo development of prepubertal goats.

doi: 10.1016/j.theriogenology.2024.12.015

Figure Lengend Snippet: Fig. 7. Effect of IVM supplementation with BMP15 (A) and/or GDF9 (B) on 8-day blastocyst quality after parthenogenic activation (PA). Cell number (mean ± S.E. M.) of the inner cell mass (ICM) and the trophectoderm (TE) of 8-days blastocysts. Columns with different letters differ significantly (p < 0.05). A total of 15–29 blastocysts per group were assessed.

Article Snippet: The IVM medium was supplemented with 100 ng/mL of recombinant human mature region BMP15 (R&D systems, Minnesota, USA) and/or 100 ng/mL of recombinant human mature region GDF9 (R&D systems), according to the experimental design, at the same concentrations as used in bovine [23,24] and porcine [25,26] IVM.

Techniques: Activation Assay

Journal: Theriogenology

Article Title: Effect of BMP15 and GDF9 in the IVM medium on subsequent oocyte competence and embryo development of prepubertal goats.

doi: 10.1016/j.theriogenology.2024.12.015

Figure Lengend Snippet: Fig. 8. Effect of IVM supplementation with BMP15 (A) and/or GDF9 (B) on 8-day blastocyst quality after IVF. Cell number (mean ± S.E.M.) of 8-day blastocysts in the inner cell mass (ICM) and the trophectoderm (TE). Columns with different letters differ significantly (p < 0.05). A total of 14–22 blastocysts per group were assessed.

Article Snippet: The IVM medium was supplemented with 100 ng/mL of recombinant human mature region BMP15 (R&D systems, Minnesota, USA) and/or 100 ng/mL of recombinant human mature region GDF9 (R&D systems), according to the experimental design, at the same concentrations as used in bovine [23,24] and porcine [25,26] IVM.

Techniques: