| Autor: |
Elmore, Moira A., Anand, Radhika, Horvath, Andrea R., Kellie, Stuart |
| Zdroj: |
FEBS Letters; January 1990, Vol. 269 Issue: 2 p283-287, 5p |
| Abstrakt: |
In vitro phosphorylation of platelet subcellular fractions revealed that most of the alkali-resistant phosphoproteins and the majority of pp60 c-srcwere in the surface membrane fraction. An alkali-resistant phosphoprotein of about 100 kDa was also immune precipitated by an anti-phosphotyrosine antibody and comigrated with gpIIIa. The phosphorylation of gpIIIa, but not gpIIb, was confirmed by the comparison of reduced and non-reduced gels, and this protein was phosphorylated exclusively on tyrosine. In contrast, both gpIIb and gpIIIa were phosphorylated when the purified complex was added to immunopurified, immobilised pp60 c-src. A synthetic peptide with partial homology to a putative tyrosine phosphorylation site in the cytoplasmic domain of gpIIIa was phosphorylated by antibody-purified pp60 c-src. Our results indicate that tyrosine-specific phosphorylation of gpIIIa by pp60 c-srcmay play a role in the regulation of platelet function. |
| Databáze: |
Supplemental Index |
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