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: Endocrinology

Article Title: TGFβ Superfamily Members Mediate Androgen Deprivation Therapy-Induced Obese Frailty in Male Mice.

doi: 10.1210/en.2016-1580

Figure Lengend Snippet: Figure 7. Castration induces myostatin protein levels in skeletal muscle. A, Representative immunoblots of myostatin and -actin (reprobing of the myostatin blot) expression in GAS muscle. B, Quantification of mean myostatin levels in GAS muscles from 4 mice at each time, assessed by 3 independent measurements. C, Representative immunoblot of myostatin and - actin (reprobing of the myostatin blot) expression level in TRI muscle. Lanes of immunoblots marked (C) contain identical control sample for interblot comparison. D, Quantification of mean myostatin levels in TRI muscles from 4 mice at each time, assessed by 3 independent measurements. The values shown in B and D are relative to the sham-castrated (0-wk castrate) animals. Sham-castrated (blue) and castrated groups (red) were compared by one-way ANOVA with Dunnett’s testing. Bars are SEM; *, P .05; **, P .01; ***, P .001 vs sham-castrated group.

Article Snippet: Target Antigen Sequence (if Known) Name of Antibody Manufacturer, Catalog Number, and/or Name of Individual Providing the Antibody Species Raised in; Monoclonal or Polyclonal Dilution Used Myostatin Mouse GDF8 Asn25Ser376 MAb (clone 84214) R&D Systems, MAB788 Monoclonal; rat IgG2B 1:1000 Phospho-Smad2 Smad3S423/5 MAb (clone EP823Y) Abcam, 52903 Monoclonal; rabbit 1:2000 Smad2 Amino terminus hSmad2 L16D3 Cell Signaling, 3103 Monoclonal; mouse 1:2000 Eukaryotic EF2 Complete protein G270 Nastiuk (Ref. 63) Rabbit 1:2000 -Actin -Actin aa 1–14 AC15 Sigma, A5441 Monoclonal; mouse 1:5000 Rat IgG (H L) Rabbit antirat unconjugated Pierce, 31218 Rabbit 1:20 000 Rabbit IgG (H L) Goat antirabbit HRP- conjugated secondary Pierce, 31460 Goat 1:20 000 Mouse IgG (H L) Goat antimouse HRPconjugated secondary Pierce, 31430 Goat 1:20 000 D ow nloaded from https://academ ic.oup.com /endo/article/157/11/4461/2758425 by G ITAM (D eem ed to be U niversity) user on 01 January 2025 tion are an acutely sensitive biological measure of circulating androgen elimination (34, 35).

Techniques: Western Blot, Expressing, Muscles, Control, Comparison

Journal: Biomolecules

Article Title: The Influence of Stress and Binge-Patterned Alcohol Drinking on Mouse Skeletal Muscle Protein Synthesis and Degradation Pathways

doi: 10.3390/biom14050527

Figure Lengend Snippet: Changes in the ubiquitin-proteasome pathway and myostatin following acute stress and alcohol access. Both representative blots ( A ) and relative protein expression ( B – E ) are presented. Data are presented as mean ± SEM ( n = 9/group). A two-way ANOVA was used to compare the individual effects of stress exposure and binge-patterned drinking, as well as to compare and interaction between factors (reported next to each figure).

Article Snippet: Therefore, we assessed changes in relative protein expression of the precursor myostatin protein (#sc-134345; Santa Cruz Biotechnology), commonly used to determine myostatin protein expression [ , ].

Techniques: Ubiquitin Proteomics, Expressing

Journal: Journal of Cachexia, Sarcopenia and Muscle

Article Title: Fibro‐Adipogenic Progenitors Regulate Orofacial Neuromuscular Junction Regeneration via Myostatin

doi: 10.1002/jcsm.70264

Figure Lengend Snippet: Recombinant MSTN suppressed AChR clustering and miR‐206 expression. (a) AChR and MyHC staining of MuSCs cultures treated with or without recombinant MSTN (100 ng/mL) and follistatin (500 ng/mL). Scale bar = 50μm. (b) Graphs show (from left to right) the quantification of differentiation index, myotube area, AChR cluster counts normalized to myotube area and ratio of AChR/myotube area. n = 3. (c) The levels of miR‐206 expression in MuSCs cultures. Mature myotubes differentiated from MAS‐derived MuSCs were treated with control, agrin alone, agrin plus MSTN or agrin plus MSTN and follistatin. (d) AChR and MyHC staining of myotubes transfected with miR‐206 mimics or negative control (NC) prior to treatment with agrin and MSTN. Scale bar = 50 μm. (e) Graphs show (from left to right) the quantification of differentiation index, myotube area, AChR cluster counts normalized to myotube area and ratio of AChR/myotube area. n = 3. The data are shown as mean ± SD. One‐way ANOVA followed by Tukey's post hoc test was used. ns, not significant, * p < 0.05, ** p < 0.01, *** p < 0.001.

Article Snippet: Mature myotubes were treated with 100 ng/mL agrin (HY‐ P79236 , MedChemExpress, China) in DM or conditioned medium (CM) of 7 dpi FAPs supplemented with 2% HS for 16 h. For recombinant MSTN treatment, 100 ng/mL MSTN (HY‐ P72632 , MedChemExpress, China) with or without 500 ng/mL follistatin (HY‐ P70315 , MedChemExpress, China) was administered together with agrin treatment.

Techniques: Recombinant, Expressing, Staining, Derivative Assay, Control, Transfection, Negative Control