منابع مشابه
siRNA-mediated knockdown of h-caldesmon in vascular smooth muscle.
Smooth muscle contraction involves phosphorylation of the regulatory myosin light chain. However, this thick-filament system of regulation cannot account for all aspects of a smooth muscle contraction. An alternate site of contractile regulation may be in the thin-filament-associated proteins, in particular caldesmon. Caldesmon has been proposed to be an inhibitory protein that acts either as a...
متن کاملAutophosphorylation of smooth-muscle caldesmon.
Caldesmon, a major actin- and calmodulin-binding protein of smooth muscle, has been implicated in regulation of the contractile state of smooth muscle. The isolated protein can be phosphorylated by a co-purifying Ca2+/calmodulin-dependent protein kinase, and phosphorylation blocks inhibition of the actomyosin ATPase by caldesmon [Ngai & Walsh (1987) Biochem. J. 244, 417-425]. We have examined t...
متن کاملCa(2+)-dependent regulation of vascular smooth-muscle caldesmon by S.100 and related smooth-muscle proteins.
1. We have investigated the ability of bovine brain S.100, and of three related proteins from sheep aorta smooth muscle, to confer Ca(2+)-sensitivity on thin filaments reconstituted from smooth-muscle actin, tropomyosin and caldesmon. 2. At 37 degrees C in pH 7.0 buffer containing 120 mM-KCl, approximately stoichiometric amounts of S.100 reversed caldesmon's inhibition of the activation of myos...
متن کاملCaldesmon inhibits active crossbridges in unstimulated vascular smooth muscle: an antisense oligodeoxynucleotide approach.
Caldesmon is a thin-filament-associated protein believed to be important in the regulation of smooth muscle contraction, although the precise mechanism is unknown. We used antisense oligodeoxynucleotides to produce intact swine carotid smooth muscle tissue deficient in h-caldesmon. Caldesmon content was decreased by 78% after 7 days in culture with antisense oligodeoxynucleotides but was unchan...
متن کاملCa2+ can control vascular smooth-muscle thin filaments without caldesmon phosphorylation.
The Ca2+-dependent regulation of the activation of myosin MgATPase by vascular-smooth-muscle thin filaments involves caldesmon. This effect may be due to the direct interaction of caldesmon with a Ca2+-binding protein such as calmodulin or phosphorylation of caldesmon by a Ca2+-dependent kinase. I have found that Ca2+ switches on aorta thin filaments in less than 10 s, whereas the caldesmon in ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1986
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)57507-x