Calcyclin and calvasculin exist in human platelets.

Article Details

Citation

Tomida Y, Terasawa M, Kobayashi R, Hidaka H

Calcyclin and calvasculin exist in human platelets.

Biochem Biophys Res Commun. 1992 Dec 30;189(3):1310-6.

PubMed ID
1482346 [ View in PubMed
]
Abstract

Using Ca(2+)-dependent affinity chromatography on a synthetic compound (W-7)-coupled Sepharose column, three distinct Ca(2+)-binding proteins have been identified in human platelets. The molecular mass of these three distinct proteins was estimated to be 10, 10.5, 17 kDa, respectively, by polyacrylamide gel electrophoresis in the presence of SDS. The partial amino acid sequence revealed these proteins have EF-hand structures and high homology to the predicted proteins, calcyclin, calvasculin, and calmodulin. Calcyclin and calvasculin have been considered as probably having roles in the control of cell proliferation, but the existence of these two proteins in platelets suggests that they have other intracellular functions related to the Ca(2+)-signal transduction system.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Protein S100-A6P06703Details
Protein S100-A4P26447Details