Phosphorylation of platelet actin binding protein protects against proteolysis by calcium dependent sulfhydryl protease.
When Actin Binding Protein (ABP) isolated from human blood platelets is phosphorylated in vitro with a cyclic AMP dependent kinase it becomes resistant to proteolysis by the Calcium Dependent Sulfhydryl Protease (CDSP). This protection against proteolytic cleavage is specific for CDSP since phosphorylation of ABP does not protect against proteolysis by trypsin, papain and thermolysin. Thus, there appears to be a distinct phosphorylation site on the ABP molecule which is essential for regulating the initial proteolytic degradation of ABP by CDSP.
Zhang
Z
Z
Department of Biochemistry, State University of New York, Brooklyn.
Lawrence
J
J
Stracher
A
A
D001792:Blood Platelets / Q000201:enzymology / Q000378:metabolism* / Q000648:ultrastructure; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D003599:Cytoskeleton / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008840:Microfilament Proteins / Q000378:metabolism*; D010766:Phosphorylation
D008840:Microfilament Proteins; D003546:Cysteine Endopeptidases; C055094:calcium dependent sulfhydryl protease