Identification of the minimum peptide from mouse myostatin prodomain for human myostatin inhibition

Journal of Medicinal Chemistry

Volumn 58, Issue 3, 2015, Pages 1544-1549

  Takayama, Kentaro ^a   Noguchi, Yuri ^a   Aoki, Shin ^a   Takayama, Shota ^a   Yoshida, Momoko ^a   Asari, Tomo ^a   Yakushiji, Fumika ^a   Nishimatsu, Shin Ichiro ^b   Ohsawa, Yutaka ^b   Itoh, Fumiko ^a   Negishi, Yoichi ^a   Sunada, Yoshihide ^b   Hayashi, Yoshio ^a  

^a TOKYO UNIVERSITY OF PHARMACY AND LIFE SCIENCES   (Japan)

^b KAWASAKI MEDICAL SCHOOL   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

MYOSTATIN; PEPTIDE DERIVATIVE; PEPTIDE;

ALPHA HELIX; AMINO ACID SEQUENCE; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CONTROLLED STUDY; DRUG EFFECT; DRUG IDENTIFICATION; DRUG SYNTHESIS; DUCHENNE MUSCULAR DYSTROPHY; HEPG2 CELL LINE; HUMAN; MALE; MOUSE; MUSCLE MASS; NONHUMAN; PEPTIDE SYNTHESIS; PROTEIN INTERACTION; PROTEIN STRUCTURE; SOLID PHASE SYNTHESIS; ANIMAL; ANTAGONISTS AND INHIBITORS; CHEMICAL STRUCTURE; CHEMISTRY; DISEASE MODEL; DOSE RESPONSE; METABOLISM; SKELETAL MUSCLE; STRUCTURE ACTIVITY RELATION; X CHROMOSOME LINKED MUSCULAR DYSTROPHIC MOUSE;

ANIMALS; DISEASE MODELS, ANIMAL; DOSE-RESPONSE RELATIONSHIP, DRUG; HEP G2 CELLS; HUMANS; MICE; MICE, INBRED MDX; MOLECULAR STRUCTURE; MUSCLE, SKELETAL; MYOSTATIN; PEPTIDES; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84922789318     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm501170d     Document Type: Article

References (21)

1. McPherron, A. C.; Lawler, A. M.; Lee, S.-J. Regulation of skeletal muscle in mice by a new TGF-β superfamily member Nature 1997, 387, 83-90
2. Zimmers, T. A.; Davies, M. V.; Koniaris, L. G.; Haynes, P.; Esquela, A. F.; Tomkinson, K. N.; McPherron, A. C.; Wolfman, N. M.; Lee, S.-J. Induction of cachexia in mice by systemically administrated myostatin Science 2002, 296, 1486-1488
3. Bogdanovich, S.; Krag, T. O.; Barton, E. R.; Morris, L. D.; Whittemore, L. A.; Ahima, R. S.; Khurans, T. S. Functional improvement of dystrophic muscle by myostatin blockade Nature 2002, 420, 418-421
4. Zhou, X.; Wang, J. L.; Lu, J.; Song, Y.; Kwak, K. S.; Jiao, Q.; Rosenfeld, R.; Chen, Q.; Boone, T.; Scott Simonet, W.; Lacey, D. L.; Goldberg, A. L.; Han, H. Q. Reversal of cancer cachexia and muscle wasting by ActRIIB antagonism leads to prolonged survival Cell 2010, 142, 531-543
5. Lee, S.-J.; McPherron, A. C. Regulation of myostatin activity and muscle growth Proc. Natl. Acad. Sci. U. S. A. 2001, 98, 9306-9311
6. Wrana, J. L.; Attisano, L.; Wieser, R.; Ventura, F.; Massagué, J. Mechanism of activation of the TGF-β receptor Nature 1994, 370, 341-347
7. Wolfman, N. M.; McPherron, A. C.; Pappano, W. M.; Davies, M. V.; Song, K.; Tomkinson, K. N.; Wright, J. F.; Zhao, L.; Sebald, S. M.; Greenspan, D. S.; Lee, S.-J. Activation of latent myostatin by the BMP-1/tolloid family of metalloproteinases Proc. Natl. Acad. Sci. U. S. A. 2003, 100, 15842-15846
8. Hinck, A. P. Structural studies of the TGF-βs and their receptors-insights into evolution of the TGF-β superfamily FEBS Lett. 2012, 586, 1860-1870
9. Anderson, S. B.; Goldberg, A. L.; Whitman, M. Identification of a novel pool of extracellular pro-myostatin in skeletal muscle J. Biol. Chem. 2008, 283, 7027-7035
10. Hill, J. J.; Davies, M. V.; Pearson, A. A.; Wang, J. W.; Hewick, R. M.; Wolfman, N. M.; Qiu, Y. The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum J. Biol. Chem. 2002, 277, 40735-40741
11. Cash, J. N.; Angerman, E. B.; Kattamuri, C.; Nolan, K.; Zhao, H.; Sidis, Y.; Keutmann, H. T.; Thompson, T. B. Structure of myostatin·follistatin-like 3: N-terminal domains of follistatin-type molecules exhibit alternate mode of binding J. Biol. Chem. 2012, 287, 1043-1053
12. Shi, M.; Zhu, J.; Wang, R.; Chen, X.; Mi, L.; Walz, T.; Springer, T. A. Latent TGF-β structure and activation Nature 2011, 474, 343-349
13. Walton, K. L.; Makanji, Y.; Chen, J.; Wilce, M. C.; Chan, K. L.; Robertson, D. M.; Harrison, C. A. Two distinct region of latency-associated peptide coordinate stability of the latent transforming growth factor-β1 complex J. Biol. Chem. 2010, 285, 17029-17037
14. Jiang, M.-S.; Liang, L.; Wang, S.; Ratovitski, T.; Holmstrom, J.; Barker, C.; Stotish, R. Characterization and identification of the inhibitory domain of GDF-8 propeptide Biochem. Biophys. Res. Commun. 2004, 315, 525-531
15. Ohsawa, Y.; Takayama, K.; Nishimatsu, S.; Okada, T.; Fujino, M.; Fukai, Y.; Murakami, T.; Hagiwara, H.; Itoh, F.; Tsuchida, K.; Hayashi, Y.; Sunada, Y. unpublished results.
16. Takayama, K.; Suehisa, Y.; Fujita, T.; Nguyen, J.-T.; Futaki, S.; Yamamoto, A.; Kiso, Y.; Hayashi, Y. Oligoarginine-based prodrugs with self-cleavable spacers for caco-2 cell permeation Chem. Pharm. Bull. 2008, 56, 1515-1520
17. Sohma, Y.; Sasaki, M.; Hayashi, Y.; Kimura, T.; Kiso, Y. Novel and efficient synthesis of difficult sequence-containing peptides through O-N intramolecular acyl migration reaction of O -acyl isopeptides Chem. Commun. 2004, 1, 124-125
18. Dennler, S.; Itoh, S.; Vivien, D.; Dijke, P.; Huet, S.; Gauthier, J.-M. Direct binding of Smad3 and Smad4 to critical TGF β-inducible elements in the promoter of human plasminogen activator inhibitor-type 1 gene EMBO J. 1998, 17, 3091-3100
19. Callahan, J. F.; Burgess, J. L.; Fornwald, J. A.; Gaster, L. M.; Harling, J. D.; Harrington, F. P.; Heer, J.; Kwon, C.; Lehr, R.; Mathur, A.; Olson, B. A.; Weinstock, J.; Laping, N. J. Identification of novel inhibitors of the transforming growth factor β1 (TGF-β1) type 1 receptor (ALK5) J. Med. Chem. 2002, 45, 999-1001
20. Roccatano, D.; Colombo, G.; Fioroni, M.; Mark, A. E. Mechanism by which 2,2,2-trifluoroethanol/water mixtures stabilize secondary-structure formation in peptides: a molecular dynamics study Proc. Natl. Acad. Sci. U. S. A. 2002, 99, 12179-12184
21. Nakatani, M.; Takehara, Y.; Sugino, H.; Matsumoto, M.; Hashimoto, O.; Hasegawa, Y.; Murakami, T.; Uezumi, A.; Takeda, S.; Noji, S.; Sunada, Y.; Tsuchida, K. Transgenic expression of a myostatin inhibitor derived from follistatin increases skeletal muscle mass and ameliorates dystrophic pathology in mdx mice FASEB J. 2008, 222, 477-487