Abstract:
:Pancreatic islets contain enzyme activity which catalyzes the phosphorylation by MgATP of cardiac, skeletal, or smooth muscle myosin light chains. The enzyme is activated by calcium (Ka = 10 microM) and calmodulin (Ka = 2 nM) and inhibited by trifluoperazine (Ki = 10 microM), a known inhibitor of calmodulin and of insulin secretion. The enzyme binds to a calmodulin affinity column when Ca2+ is present and is eluted when Ca2+ is omitted. These are the properties of myosin light chain kinase. Since phosphorylation of smooth muscle myosin is necessary for its activation by actin, the kinase may have a key role in coupling stimuli that increase intracellular calcium to the contractile processes involved in insulin secretion.
journal_name
Diabetesjournal_title
Diabetesauthors
MacDonald MJ,Kowluru Adoi
10.2337/diab.31.6.566subject
Has Abstractpub_date
1982-06-01 00:00:00pages
566-70issue
6 Pt 1eissn
0012-1797issn
1939-327Xjournal_volume
31pub_type
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