Phosphorylation of two sites on smooth muscle myosin. Effects on contraction of glycerinated vascular smooth muscle.
作者： J R Haeberle , T A Sutton , B A Trockman
DOI: 10.1016/S0021-9258(18)68943-4
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摘要: Contraction of glycerinated porcine carotid artery smooth muscle in response to calcium (20 microM), calmodulin (10 and MgATP was associated with phosphorylation the 20,000-dalton myosin light chain (LC20) an average stoichiometry 1.47 mol PO4/mol LC20. Tryptic chymotryptic phosphopeptide maps mono- diphosphorylated forms LC20 purified from skinned muscles demonstrated presence a single all cases. Phosphoamino acid analysis indicated that monophosphorylated form contained primarily phosphoserine, whereas both phosphoserine phosphothreonine. Thiophosphorylation by adenosine 5'-O-(thiotriphosphate) resulted incorporation 1 thiophosphate into phosphoserine. Thiophosphorylated could be subsequently phosphorylated at threonine residue 1.7 incubation MgATP, calcium, calmodulin. The extent multiple site dependent upon ionic strength free Mg2+ concentration bath; increasing either (0.07-0.15 M) or [Mg2+] (1-20 mM) lower stoichiometries phosphorylation. effect on contraction examined which were seqentially serine followed threonine. Full activation (21 degrees C) isometric force (1.4 newtons/cm2) unloaded shortening velocity (0.016 L0/s) achieved following thiophosphorylation 1.1 No further (1.5 (0.015 occurred
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