13 research outputs found
Lipids derived from the mevalonate pathway in HL-60 cells modulate the interactions of β2 integrins with their ligands
No full textAnti-sense to secretory type II phospholipase A2 inhibits fMLP induced arachidonic acid release in differentiated HL-60's
No full textA human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases
No full textConserved His and Asp residues are critical for enzyme activity in human homologues of lysophosphatidic acid acyl transferases
No full textIdentification and Cloning of novel yeast Saccharomyces cerevisiae Lysophosphatidic acid acyl transferase (LPAAT) homologues
No full textTyrosine-Specific Phosphorylation of Gpiiia in Platelet Membranes
Get PDFAbstractIn vitro phosphorylation of platelet subcellular fractions revealed that most of the alkali-resistant phosphoproteins and the majority of pp60c-src were 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 pp60c-src. A synthetic peptide with partial homology to a putative tyrosine phosphorylation site in the cytoplasmic domain of gpIIIa was phosphorylated by antibody-purified pp60c-src. Our results indicate that tyrosine-specific phosphorylation of gpIIIa by pp60c-src may play a role in the regulation of platelet function
