title: Activation of pancreatic islet myosin ATPase by ATP and actin.
abstract: Previous work from our laboratory indicated that pancreatic islets contain myosin light chain kinase, a calcium- and calmodulin-activated enzyme. This enzyme catalyzes phosphorylation of myosin which, in tissues containing smooth muscle, is believed to permit the ATPase of myosin to be activated by actin. The current report shows that incubating islet cytosol with ATP under conditions that should permit phosphorylation of myosin markedly enhances islet myosin ATPase activity in the presence of actin. It has been suggested that contractile proteins power insulin granule movements in the beta cell. Phosphorylation of myosin may be one of the means of coupling stimuli to insulin secretion.
authors.forename: M J
authors.initials: MJ
authors.lastname: MacDonald
authors.forename: C M
authors.initials: CM
authors.lastname: Chang
authors.forename: A
authors.initials: A
authors.lastname: Kowluru
mesh_terms: D000199:Actins / Q000494:pharmacology*; D000251:Adenosine Triphosphatases / Q000032:analysis* / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000818:Animals; D004789:Enzyme Activation; D007515:Islets of Langerhans / Q000187:drug effects / Q000201:enzymology*; D010766:Phosphorylation; D051381:Rats; D014268:Trifluoperazine / Q000494:pharmacology
chemical_list: D000199:Actins; D014268:Trifluoperazine; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases