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We have characterized changes in [Ca2+]i in primary mouse megakaryocytes in response to fibrillar collagen and in response to cross-linking of the collagen receptor, the integrin alpha2beta1. The response to collagen was markedly different from that seen to a triple helical collagen-related peptide (CRP), which signals via the tyrosine kinases p59(fyn) and p72(syk). This peptide binds to the collagen receptor glycoprotein VI (GPVI), but not to the integrin alpha2beta1. Collagen elicited a sustained increase in [Ca2+]i composed primarily of influx of extracellular Ca2+ with some Ca2+ release from internal stores. In contrast to CRP, this response was only partially (approximately 30%) inhibited by the src-family kinase inhibitor PP1 (10 micromol/L) or by microinjection of the tandem SH2 domains of p72(syk). Collagen also caused an increase in [Ca2+]i in megakaryocytes deficient in either p59(fyn) or p72(syk), although the response was reduced by approximately 40% in both cases: Cross-linking of the alpha2 integrin increased [Ca2+]i in these cells exclusively via Ca2+ influx. This response was reduced by approximately 50% after PP1 pretreatment, but was significantly increased in fyn-deficient megakaryocytes. Collagen therefore increases [Ca2+]i in mouse megakaryocytes via multiple receptors, including GPVI, which causes Ca2+ mobilization, and alpha2beta1, which stimulates a substantial influx of extracellular Ca2+.


Journal article



Publication Date





3847 - 3855


Animals, Calcium, Cells, Cultured, Collagen, Enzyme Precursors, Integrins, Intracellular Signaling Peptides and Proteins, Ion Transport, Megakaryocytes, Mice, Protein-Tyrosine Kinases, Receptors, Collagen, Signal Transduction, Syk Kinase