Calcyclin and calvasculin exist in human platelets.
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.
Tomida
Y
Y
Department of Pharmacology, Nagoya University School of Medicine, Japan.
Terasawa
M
M
Kobayashi
R
R
Hidaka
H
H
D000595:Amino Acid Sequence; D000818:Animals; D001011:Aorta / Q000502:physiology; D001792:Blood Platelets / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000097:blood* / Q000302:isolation & purification; D002417:Cattle; D018797:Cell Cycle Proteins; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D051381:Rats; D000075383:S100 Calcium Binding Protein A6; D000071999:S100 Calcium-Binding Protein A4; D009418:S100 Proteins; D017386:Sequence Homology, Amino Acid
D002135:Calcium-Binding Proteins; D018797:Cell Cycle Proteins; D000075383:S100 Calcium Binding Protein A6; D000071999:S100 Calcium-Binding Protein A4; D009418:S100 Proteins; C499413:S100A4 protein, Bos taurus; C499412:S100a4 protein, rat; C489132:S100a6 protein, rat; C055351:S100A6 protein, human; C077591:S100A4 protein, human; D002118:Calcium