Literature DB >> 2936345

Calcium-dependent proteolysis of calcium-binding proteins.

I Sohar, J W Bird, P B Moore.   

Abstract

In several myopathic disorders, the internal muscle cell calcium concentration increases significantly as compared to normal muscle cells. We report that in the presence of elevated calcium levels, the calcium-binding proteins troponin C and calmodulin are protected from digestion by the chymotrypsin-like serine proteinase that co-purifies with isolated myofibrils. Degradation of the 67k calcimedin in the presence of calcium shows altered major cleavage fragments while degradation of myosin is unaffected by the presence of calcium. A role for this serine proteinase in muscle-wasting diseases is suggested.

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Year:  1986        PMID: 2936345     DOI: 10.1016/0006-291x(86)90387-6

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  67 kDa calcimedin, a new Ca2+-binding protein.

Authors:  P B Moore
Journal:  Biochem J       Date:  1986-08-15       Impact factor: 3.857

2.  67 k calcimedin (67 kDa) is distinct from p67 calelectrin and lymphocyte 68 kDa Ca2+-binding protein.

Authors:  S S Morse; P B Moore
Journal:  Biochem J       Date:  1988-04-01       Impact factor: 3.857

  2 in total

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