Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Native thin filaments were extracted from rabbit uterus by the procedure of Marston and Smith. The protein content was actin, tropomyosin, and caldesmon in molar ratios of 1:0.2:0.03. Some filamin, myosin, and calcium-binding protein were also present. The thin filaments activated skeletal or smooth muscle myosin magnesium adenosine triphosphatase at least 30-fold. Activation was regulated by Ca2+; maximum observed Ca2+ sensitivity was greater than 10 times. The thin filaments were dismantled into component proteins by the method of Smith and Marston. Actin and actin-tropomyosin-activated myosin magnesium adenosine triphosphatase, but the activation was not Ca2+-regulated. Added caldesmon inhibited adenosine triphosphatase activation by as much as 80%, with 50% inhibition at 1 caldesmon per 50 actin. Caldesmon inhibition was not Ca2+ dependent, but inhibition could be reversed by further addition of Ca2+ and calmodulin. It is concluded that the thin filaments of uterine smooth muscle are Ca2+ regulated and that this regulatory system could be involved in control of uterine smooth muscle contractility. A mechanism for thin filament regulation, mediated by caldesmon, is proposed.
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PMID:Calcium ion-dependent regulation of uterine smooth muscle thin filaments by caldesmon. 291 89

Calcium initiates smooth muscle contraction by binding to calmodulin and activating the enzyme myosin light chain kinase. The activated form of myosin light chain kinase phosphorylates myosin on the 20,000-dalton light chain and contractile activity ensues. Calcium may also enhance smooth muscle contractile activity by binding directly to myosin, the main component of the thick filament. Recent studies raise the possibility that the calcium-calmodulin complex may also modulate smooth muscle contractile activity by removing the inhibition imposed by caldesmon, a protein that is bound to the thin (i.e., actin-containing) filaments of smooth muscle. In vitro studies have demonstrated that the calcium-activated, phospholipid-dependent kinase, protein kinase C, can phosphorylate smooth muscle myosin at a different site than does myosin light chain kinase and down-regulate its actin-activated magnesium adenosine triphosphatase activity. This raises the possibility that protein kinase C phosphorylation of myosin may play a role in modulating vascular contractile activity in vivo.
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PMID:Effects of calcium on vascular smooth muscle contraction. 302 18