title: Smooth muscle myosin isoform distribution and myosin ATPase in hypertrophied urinary bladder.
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.
authors.affiliation: Department of Pathobiology, University of Pennsylvania, Philadelphia 19104-6051.
authors.forename: M
authors.initials: M
authors.lastname: Samuel
authors.forename: Y
authors.initials: Y
authors.lastname: Kim
authors.forename: K Y
authors.initials: KY
authors.lastname: Horiuchi
authors.forename: R M
authors.initials: RM
authors.lastname: Levin
authors.forename: S
authors.initials: S
authors.lastname: Chacko
mesh_terms: D000818:Animals; D006984:Hypertrophy; D008297:Male; D008970:Molecular Weight; D009130:Muscle, Smooth / Q000378:metabolism; D009218:Myosins / Q000302:isolation & purification / Q000378:metabolism*; D011817:Rabbits; D001743:Urinary Bladder / Q000378:metabolism* / Q000473:pathology
chemical_list: D009218:Myosins