Smooth muscle myosin isoform distribution and myosin ATPase in hypertrophied urinary bladder. |
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| Authors: | M Samuel Y Kim K Y Horiuchi R M Levin S Chacko |
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| Institution: | Department of Pathobiology, University of Pennsylvania, Philadelphia 19104-6051. |
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| Abstract: | Hypertrophy of the urinary bladder was produced in rabbit by partial ligation of the urethra. Electrophoresis of the bladder smooth muscle myosin on highly porous (3.5-7% gradient) SDS-polyacrylamide gel revealed two heavy chain isoforms, SM-1 and SM-2 with approximate molecular weights of 204,000 and 200,000, respectively. The ratio of the SM-2 to SM-1 heavy chain is 3:1 for myosin isolated from normal bladder smooth muscle, and this ratio changes to about 1:1 in hypertrophied bladder. Despite a change in the ratio of SM-2 to SM-1, the myosin ATPase and the actin-activated ATPase activities are not altered in response to hypertrophy. |
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