Phosphorylation Of Platelet Actin-Binding Protein During Platelet Activation
Phosphorylation Of Platelet Actin-Binding Protein During Platelet Activation
复制标题
血小板激活过程中血小板肌动蛋白结合蛋白的磷酸化
DOI:
10.1055/s-0038-1652791
复制
发表时间:
1982
影响因子:
6.7
通讯作者:
J. Gerrard
中科院分区:
文献类型:
--
作者:
R. Carroll;J. Gerrard
We have followed the 32P-labelling of actin-binding protein as a function of platelet activation. Utilizing polyacrylamide sodium dodecyl sulfate gel electrophoresis to resolve total platelet protein samples we found 2 to 3 fold labelling increases in actin-binding protein 30 to 60 seconds after thrombin stimulation. Somewhat larger increases were observed for 40,000 and 20,000 apparent molecular weight peptides. The actin-binding protein was identified on the gels by coelectrophoresis of purified actin-binding protein as well as cytoskeletal cores prepared by detergent extraction of activated 32p-iabelled platelets. In addition, these cytoskeletal cores indicated that the 32P-labelled actin-binding protein was closely associated with the activated platelet's cytoskeleton. Following the 32P-labelling of actin-binding protein over an 8 minute time course revealed that in aggregating platelet samples rapid desphosphorylation to almost initial levels occurred between 3 and 5 minutes. A similar curve was obtained for the 20,000 apparent molecular weight peptide. This rapid dephosphorylation was shown to be dependent on platelet aggregation in the absence of external calcium or in thrombastenic platelets lacking the aggregation response to activation. These results suggest that phosphorylation of actin-binding protein initiates its association with the platelet cytoskeleton during activation.
影响因子:
5.6
作者:
Zobel,CR;Jung,CY
通讯作者:
Jung,CY