Ca2+ -calmodulin-dependent phosphorylation and platelet secretion
- 1 October 1980
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 287 (5785) , 863-865
- https://doi.org/10.1038/287863a0
Abstract
Non-muscle actomyosin e.g., that isolated from [human] platelets may be regulated by Ca2+-calmodulin-dependent L chain phosphorylation, but the precise relationship between phosphorylation and the function of platelets has not been clearly established. Pharmacological evidence that a calmodulin-mediated system, such as Ca2+-dependent myosin L chain phosphorylation, plays an important role in the phenomenon of the release reaction is presented. N-(o-aminohexyl)-5-chloro-1-naphthalene-sulfonamide binds selectively to calmodulin in vitro and inhibits its biological activity.Keywords
This publication has 17 references indexed in Scilit:
- Interaction of Ca2+ and protein phosphorylation in the rabbit platelet release reaction.Journal of Clinical Investigation, 1980
- Effect of novel specific myosin light chain kinase inhibitors on Ca2+-activated Mg2+-ATPase of chicken gizzard actomyosinBiochemical and Biophysical Research Communications, 1979
- Human platelet myosin light chain kinase requires the calcium-binding protein calmodulin for activity.Proceedings of the National Academy of Sciences, 1979
- Effects of collagen, ionophore A23187 and prostaglandin E1 on the phosphorylation of specific proteins in blood plateletsBiochemical Journal, 1979
- Characterization of a platelet protein phosphorylated during the thrombin-induced release reactionBiochemistry, 1979
- A Ca2+- and modulator-dependent myosin light chain kinase from non-muscle cellsBiochemical and Biophysical Research Communications, 1978
- Interrelations of Platelet Aggregation and SecretionJournal of Clinical Investigation, 1977
- Relationship between phosphorylation of blood platelet proteins and secretion of platelet granule constituents I. Effects of different aggregating agentsBiochemical and Biophysical Research Communications, 1977
- Phosphorylation of platelet myosin increases actin-activated myosin ATPase activityNature, 1975
- A phosphorylated light-chain component of myosin from skeletal muscleBiochemical Journal, 1973