The maximal velocity of vascular smooth muscle shortening is independent of the expression of calponin
- 1 January 2000
- journal article
- research article
- Published by Springer Nature in Journal of Muscle Research and Cell Motility
- Vol. 21 (4) , 367-373
- https://doi.org/10.1023/a:1005680614296
Abstract
In smooth muscle, the phosphorylation/dephosphorylation of the 20-kDa regulatory light chain of myosin (MLC20) is known to regulate actomyosin interaction and force. However, a thin filament based...Keywords
This publication has 37 references indexed in Scilit:
- Expression and epitopic conservation of calponin in different smooth muscles and during developmentBiochemistry and Cell Biology, 1996
- Calponin reduces shortening velocity in skinned taenia coli smooth muscle fibresFEBS Letters, 1995
- Mammalian calponinFEBS Letters, 1993
- The mechanism of inhibition of the actin-activated myosin MgATPase by calponinBiochemical and Biophysical Research Communications, 1992
- Involvement of calponin and caldesmon in sustained contraction of arterial smooth muscleBiochemical and Biophysical Research Communications, 1992
- Calponin and the composition of smooth muscle thin filamentsJournal of Muscle Research and Cell Motility, 1991
- Absence of calponin phosphorylation in contracting or resting arterial smooth muscleFEBS Letters, 1991
- Effects of modulators of myosin light-chain kinase activity in single smooth muscle cellsNature, 1989
- Vascular smooth muscle calponin. A novel troponin T-like protein.Hypertension, 1988
- Isolation and characterization of a 34000-dalton calmodulin- and F-actin-binding protein from chicken gizzard smooth muscleBiochemical and Biophysical Research Communications, 1986