Matrix metalloproteinases are less essential for the in-situ gelatinolytic activity in heart muscle than in skeletal muscle

Comparative Biochemistry and Physiology - A Molecular and Integrative Physiology

Volumn 156, Issue 4, 2010, Pages 518-522

  Cha, M C ^a   Purslow, P P ^a  

^a UNIVERSITY OF GUELPH   (Canada)

Author keywords

Gelatinase; In situ zymography; MMP; Myoblast; Myocardium; Skeletal muscle

Indexed keywords

EDETIC ACID; GELATINASE; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE INHIBITOR; ORGANOMERCURY COMPOUND; PROTEINASE;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; CYTOPLASM; ENDOMYSIUM; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME INHIBITION; GELATINIZATION; HEART MUSCLE; MUSCLE TISSUE; MYOBLAST; NONHUMAN; PERIMYSIUM; PROTEIN DEGRADATION; PROTEIN EXPRESSION; RAT; SKELETAL MUSCLE; SOLEUS MUSCLE; TISSUE HOMOGENATE; TISSUE SECTION; ZYMOGRAPHY;

RATTUS; RODENTIA;

EID: 77953020283     PISSN: 10956433     EISSN: 15314332     Source Type: Journal    
DOI: 10.1016/j.cbpa.2010.04.014     Document Type: Article

References (17)

1. Chen X., and Li Y. Role of matrix metalloproteinases in skeletal muscle: migration, differentiation, regeneration and fibrosis. Cell Adh. Migr. 3 (2009) 337-341
2. Formigli L., Perna A.M., Meacci E., Cinci L., Margheri M., Nistri S., Tani A., Silvertown J., Orlandini G., Porciani C., Zecchi-Orlandini S., Medin J., and Bani D. Paracrine effects of transplanted myoblasts and relaxin on post-infarction heart remodeling. J. Cell Mol. Med. 11 (2007) 1087-1100
3. Frisdal E., Teiger E., Lefaucheur J.P., Adnot S., Planus E., Lafuma C., and d'Ortho M.P. Increased expression of gelatinases and alteration of basement membrane in rat soleus muscle following femoral artery ligation. Neuropathol. Appli. Neurobiol. 26 (2000) 11-21
4. Geesink G.H., and Veiseth E. Muscle enzymes: proteinases. In: Nollet L.M.L., and Toldra F. (Eds). Hand Book of Muscle Foods Analysis (2009), CRC Press, Boca Raton
5. Goll D.E., Thompson V.F., Li H., Wei W., and Cong J. The calpain system. Physiol. Revs. 83 (2003) 731-801
6. Jones C.B., Sane D.C., and Herrington D.M. Matrix metalloproteinases: a review of their structure and role in acute coronary syndrome. Cardiovasc. Res. 59 (2003) 812-823
7. Lodemel J.B., Maehre H.K., Winberg J.O., and Olsen R.L. Tissue distribution, inhibition and activation of gelatinolytic activities in Atlantic cod (Gadus morhua). Comp. Biochem. Physiol. B. 137 (2004) 363-371
8. Milner J.M., Patel A., and Rowan A.D. Emerging role of serine proteinases in tissue turnover in arthritis. Arthritis Rheum. 58 (2008) 3644-3656
9. Perez-lizarbe M., Agbulut O., Pelacho B., Ciorba C., San Jose-Eneriz E., Desnos M., Hagege A.A., Aranda P., Andreu E.J., Menasche P., and Prosper F. Characterization of the paracrine effects of human skeletal myoblasts transplanted in infarcted myocardium. Eur. J. Heart Fail. 10 (2008) 1065-1072
10. Rechsteiner M., and Hill C.P. Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors. Trends Cell Biol. 15 (2005) 27-33
11. Spinale F.G. Matrix metalloproteinases: regulation and dysregulation in the failing heart. Circ. Res. 90 (2002) 520-530
12. Spinale F.G. Myocardial matrix remodeling and the matrix metalloproteinases: influence on cardiac form and function. Physiol. Revs. 87 (2007) 1285-1342
13. Schultz E., and McCormick K.M. Skeletal muscle satellite cells. Rev. Physiol. Biochem. Pharmacol. 123 (1994) 213-257
14. Turk V., Turk B., and Turk D. Lysosomal cysteine proteases: facts and opportunities. EMBO J. 20 (2001) 4629-4633
15. Visse R., and Nagase H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function and biochemistry. Circ. Res. 92 (2003) 827-839
16. Wilkie D.R. Muscle (Second edition) (1976), Edward Arnold Publishers Ltd, London
17. Zimowska M., Brzoska E., Swierczynska M., Streminska W., and Moraczewski J. Distinct patterns of MMP-9 and MMP-2 activity in slow and fast twitch skeletal muscle regeneration in vivo. Int. J. Dev. Biol. 52 (2008) 307-314