Calcium-calmodulin-dependent myosin phosphorylation by pancreatic islets.

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

Diabetes

journal_title

Diabetes

authors

MacDonald MJ,Kowluru A

doi

10.2337/diab.31.6.566

subject

Has Abstract

pub_date

1982-06-01 00:00:00

pages

566-70

issue

6 Pt 1

eissn

0012-1797

issn

1939-327X

journal_volume

31

pub_type

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