Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Phosphorylation and dephosphorylation of human platelet surface proteins by an ecto-protein kinase/phosphatase system
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2014, BloodCitation Excerpt :Approval for these studies was obtained from the University of Delaware Institutional Review Board according to the Declaration of Helsinki. Washed human platelets were obtained as previously described.22,23 A detailed characterization of Jam-A knockout mice (Jam-Agt/gt) used in this study has been previously reported.24,25
Calcium- and integrin-binding protein regulates focal adhesion kinase activity during platelet spreading on immobilized fibrinogen
2003, BloodCitation Excerpt :Approval was obtained from the Univeristy of Delaware Institutional review board for these studies according to the Declaration of Helsinki. Platelets were washed as described previously.20 To obtain fixed discoid platelets, platelet-rich plasma was diluted with an equal volume of 8% paraformaldehyde in PBS as fixative for 10 minutes at room temperature.
E-NTPase/E-NTPDase: A potential regulatory role in E-kinase/PKA-mediated CD36 activation
2003, Cell Biology InternationalPhosphorylation of the β-Amyloid precursor protein at the cell surface by ectocasein kinases 1 and 2
2000, Journal of Biological ChemistryCitation Excerpt :Although the phosphorylation of βAPP during its transport to the cell surface occurs predominantly at serines 198 and 206, ecto-CK1 and ecto-CK2 can phosphorylate cell surface-located and soluble βAPPs at additional sites. Expression of ectoprotein kinases at the cell surface was shown in several cell types, including tumor cells (42, 43, 47), endothelial cells (61, 62), neutrophils (63), platelets (64), and neuronal cells (65, 66). Interestingly, both CK1 and CK2 have been shown to be released from the cell surface upon the addition of the cognate protein substrates casein and phosvitin (41, 42, 63) and appear to be constituents of a functional kinase complex (43).
Cloning of the human platelet F11 receptor: A cell adhesion molecule member of the immunoglobulin superfamily involved in platelet aggregation
2000, BloodCitation Excerpt :The cytoplasmic tail of the F11R was shown to contain 2 phosphorylable tyrosine residues at positions 260 and 279 and putative intracellular and extracellular sites of phosphorylation by casein kinase II,40 protein kinase C,41,42 and cAMP- or cGMP-dependent protein kinases.43,44 The extracellular sites suggest that the F11R is a substrate for ecto-protein kinases found in platelets.45-47 Hydrophobicity analysis of the platelet F11R amino acid sequence, shown in Figure4, was performed using the ProtScale program following the method of Kyte and Doolittle.48