Regulation of shortening velocity by calponin in intact contracting smooth muscles.
To elucidate the function of calponin in intact contracting smooth muscle cells in vivo, we generated mice with a mutated basic calponin (h1) locus (Yoshikawa et al., Genes Cells 3, 685-695, 1998). Crossbridge cycling rates were estimated in aortic smooth muscle by the force redevelopment following an isometric step shortening as a function of time after K(+) depolarization. Evidence is presented that calponin is involved in the inhibition of shortening velocity in the tonic phase of contraction. The phosphorylation levels of myosin regulatory light chain and cytosolic calcium concentrations were not significantly different in paired comparisons between calponin-deficient (-/-) and wild-type (+/+) muscles at any time point after stimulation. The force-velocity relationships in vas deferens smooth muscle showed that the maximum shortening velocity of -/- muscle was significantly faster than that of +/+ muscle. There was no change in the length-force relationships in both -/- and +/+ muscles of aorta and vas deferens. The results suggest that calponin plays a role in regulation of the crossbridge cycling and that it may be responsible for reduced shortening velocity during a maintained contraction of mammalian smooth muscle.
Takahashi
K
K
Department of Medicine, Osaka Medical Center for Cancer and Cardiovascular Diseases, Osaka University, Japan. katakahas@mail.mc.pref.osaka.jp
Yoshimoto
R
R
Fuchibe
K
K
Fujishige
A
A
Mitsui-Saito
M
M
Hori
M
M
Ozaki
H
H
Yamamura
H
H
Awata
N
N
Taniguchi
S
S
Katsuki
M
M
Tsuchiya
T
T
Karaki
H
H
D000818:Animals; D002135:Calcium-Binding Proteins / Q000235:genetics / Q000502:physiology*; D051379:Mice; D008840:Microfilament Proteins; D008854:Microscopy, Electron; D009119:Muscle Contraction / Q000502:physiology; D009130:Muscle, Smooth / Q000502:physiology* / Q000648:ultrastructure; D000096985:Calponins
D002135:Calcium-Binding Proteins; D008840:Microfilament Proteins; D000096985:Calponins