ArticleThe Biochemical journal1985
Relationship between cytoplasmic free calcium and myosin light chain phosphorylation in intact platelets.
Article in The Biochemical journal, 1985. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 57 citations in OpenAlex.
- Review
- Current concepts of platelet activation: possibilities for therapeutic modulation of heterotypic vs. homotypic aggregation.British journal of clinical pharmacology · 2011Review
- Identification and localization of myosin phosphatase in human platelets.The Biochemical journal · 1998Article
- Phosphorylation of smooth muscle myosin by type II Ca2+/calmodulin-dependent protein kinase.Molecular and cellular biochemistry · 1990Article
- Signal transduction in human platelets and inflammatory mediator release induced by genetically cloned hemolysin-positive and -negative Escherichia coli strains.Infection and immunity · 1990Article
- Stimulus-response coupling in human platelets activated by monoclonal antibodies to the CD9 antigen, a 24 kDa surface-membrane glycoprotein.The Biochemical journal · 1990Article
- [Relation between post-thrombotic syndrome, ADP-induced thrombocyte aggregation and intrathrombocyte calcium content].Klinische Wochenschrift · 1989Article
- Cytosolic calcium in platelet activation.Experientia · 1988Review
- Fluorescence and bioluminescence measurement of cytoplasmic free calcium.The Biochemical journal · 1987Review
- Ionophore A23187 induces a refractory state in thrombin-activated release of inositol phosphates.The Biochemical journal · 1986Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human platelets were prepared and loaded with the fluorescent Ca2+ indicator quin2. The relation between cytoplasmic free calcium concentration, [Ca2+]i, and the extent of the phosphorylation of myosin light chains of Mr 20 000 could then be examined. When the calcium ionophore ionomycin is used to stimulate platelets, little phosphorylation is seen until [Ca2+]i exceeds 400 nM; half-maximal response occurs at 600 nM with a full response at about 1 microM-[Ca2+]i. Under optimal conditions, physiological stimuli such as platelet-activating factor and thrombin can increase [Ca2+]i to sufficiently high levels [Rink, Smith & Tsien (1982) FEBS Lett. 148, 21-26; Hallam, Sanchez & Rink (1984) Biochem. J. 218, 819-827] that Ca2+ ions could be the trigger for the myosin phosphorylation evoked by these agonists. However, in this paper we show that, in the absence of external calcium, platelet-activating factor and thrombin can stimulate myosin phosphorylation while [Ca2+]i remains at levels which are well below those needed when the calcium ionophore is the stimulus. This observation suggests that myosin light chain phosphorylation may be controlled by an additional pathway.
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