The heavy chain of smooth muscle myosin is phosphorylated in aorta cells.
The 204-kDa smooth muscle myosin heavy chain (MHC) from rat aorta smooth muscle cells was found to be phosphorylated following isolation of myosin from strips of intact aorta as well as from primary cultures of aorta cells. Two-dimensional maps of the tryptic peptides revealed that the phosphate was confined to only three peptides and gave a similar pattern for the MHC isolated from intact aorta strips and cultured cells. This map was quite different from the phosphopeptide map found for the 196-kDa MHC of nonmuscle myosin isolated from the same cell culture. Smooth muscle MHC purified from primary cell cultures was found to contain approximately 0.7 mol of phosphate/mol of MHC while the nonmuscle MHC contained approximately 0.8 mol of phosphate/mol of MHC. These observations raise the possibility of an additional regulatory mechanism in smooth muscle operating via MHC phosphorylation.
Kawamoto
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Laboratory of Molecular Cardiology, National Heart, Lung, and Blood Institute, Bethesda, Maryland 20892.
Adelstein
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RS
D000818:Animals; D001013:Aorta, Thoracic / Q000378:metabolism; D002478:Cells, Cultured; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D009131:Muscle, Smooth, Vascular / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism*; D010449:Peptide Mapping; D010766:Phosphorylation; D051381:Rats; D011919:Rats, Inbred Strains
D009218:Myosins