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Carlson, C. J., Booth, F. W. and Gordon, S. E. (1999): Skeletal muscle myostatin mRNA expression is fiber-type specific and increases during hindlimb unloading. Am. J. Physiol. 277 , R601-R606

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regulation appear to be two signal transduction pathways: insulin-like growth factor-I/Akt/mammalian target of rapamycin (IGF-I/Akt/mTOR) and myostatin/Smad [ 1 ]. Increased protein synthesis induced by activation of the IGF-I/Akt/mTOR signal transduction

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circulating myostatin in patients with type 2 diabetes mellitus. J. Huazhong Univ. Sci. Technolog. Med. Sci., 2012, 32 (4), 534–539. Guo, T., Jou, W., Chanturiya, T., et al.: Myostatin inhibition in muscle, but not

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Acta Veterinaria Hungarica
Authors: Valentina Nikolić, Gordana Teofilovski-Parapid, Gordana Stanković, Biljana Parapid, S. Malobabić, and V. Stojić

The objective of the present study was to determine the effects of follistatin addition on myostatin and follistatin gene expression patterns in C2C12 muscle cells. C2C12 cells were administered with 100 ng/ml recombinant human (rh) follistatin in Dulbecco's modified Eagle medium (DMEM) containing 10% fetal bovine serum (FBS), 4 mM glutamine and antibiotics daily for three days. Rh follistatin was not added in the control wells. Follistatin and myostatin gene cDNAs were synthesised by reverse transcriptase polymerase chain reaction (RT-PCR).The time course of follistatin gene expression pattern was similar in both the control and the follistatin-treated group. Myostatin mRNA level significantly increased in the follistatin-treated group after 24 h of culture (Fig. 3, P < 0.01). Amounts then sharply decreased (Fig. 3, P < 0.01) at 48 h of culture, whereas there was no significant difference between the control and the follistatin-treated group at 72 h of culture. Our results demonstrated that myostatin and follistatin mRNA were expressed in C2C12 cells and rh follistatin changed the myostatin expression pattern.

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Orvosi Hetilap
Authors: Krisztina Marosi, Endre Horváth, Péter Nagy, Bernadett Köles, and Zsolt B. Nagy

Grobet, L., Martin, L. J., Poncelet, D., et al.: A deletion in the bovine myostatin gene causes the double-muscled phenotype in cattle. Nat. Genet., 1997, 17 , 71–74. Poncelet D. A

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, Ugrinowitsch C, Roschel CH, Aoki MS, Soares AG, Neves M, Jr., Aihara AY, Fernandes Ada R, Tricoli V: Strength training with blood flow restriction diminishes myostatin gene expression. Med. Sci. Sports Exerc. 44, 406–412 (2012) Tricoli V

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Kim, J. S., Cross, J. M., Bamman, M. M.: Impact of resistance loading on myostatin expression and cell cycle regulation in young and older men and women. Am. J. Physiol. Endocrinol. Metab., 2005, 288 , E1110

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P, Brimioulle S, Naeije R, McEntee K: Activin-A, transforming growth factor-beta, and myostatin signaling pathway in experimental dilated cardiomyopathy. J. Card. Fail. 14, 703–709 (2008) McEntee K Activin-A, transforming

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). I JIRI , D. , I SHITANI , K. , S HIMAMOTO , S. , I SHIMARU , Y. & O HTSUKA , A. ( 2014 ): The effects of intraperitoneal clenbuterol injection on protein degradation and myostatin expression differ between the sartorius and pectoral

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-based selection studies have identified hundreds of domesticated genes in Thoroughbreds, suggesting that myostatin (MSTN) gene is not the only determinant of athletic phenotype and competitive performance ( Lee, 2007 ; Gu et al., 2009 ). The horse

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