Parvalbumins and muscle relaxation: a computer simulation study View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1982-12

AUTHORS

J. M. Gillis, D. Thomason, J. Lefèvre, R. H. Kretsinger

ABSTRACT

The distribution of Ca2+ and Mg2+ among the 'regulatory' cation binding sites of troponin (T-sites) and the strong, Ca2+-Mg2+ binding sites of troponin and parvalbumins (P-sites) in the sarcoplasm of a muscle was calculated. At rest, 60% of the T-sites were metal free, while 92% of the P-sites were loaded with Mg2+. In response to a Ca2+ pulse, troponin-calcium (T-Ca) complexes were rapidly formed, while the binding of Ca2+ to P-sites was limited by the slow rate of dissociation of the parvalbumin-magnesium (P-Mg) complexes. Muscle activation was not prevented by a high content of parvalbumins. Parvalbumin and the sarcoplasmic reticulum (SR) pump were complementary relaxing factors that removed Ca2+ from the cytosol and from the T-sites. Parvalbumins dominated the first part of relaxation, while the action of the SR was essential to ensure the return to a very low level of free Ca2+ ion and of T-Ca. After relaxation, a large fraction of the Ca2+ pulse was still bound to parvalbumins and returned slowly to the SR during the recovery. When the SR activity was reduced, the presence of parvalbumins preserved a fast rate of relaxation, at least for a few contractions. This may have a high adaptive value in cold-blooded animals. More... »

PAGES

377-398

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00712090

DOI

http://dx.doi.org/10.1007/bf00712090

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1016510720

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7183710


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