Platelet glycoprotein II(b)-III(a) (α(IIb)β3 integrin) confers fibrinogen- and activation-dependent aggregation on heterologous cells

M. M. Frojmovic, T. E. O'Toole, E. F. Plow, J. C. Loftus, M. H. Ginsberg

Research output: Contribution to journalArticle

32 Scopus citations

Abstract

To analyze molecular mechanisms of platelet aggregation, we have studied the aggregation of Chinese hamster ovary (CHO) cells expressing between 1 and 4 x 105 recombinant human glycoprotein (GP) II(b)-III(a) molecules per cell (A5 cells). These cells aggregated as measured by the disappearance of single cells during rotary agitation. Aggregation was dependent on the presence of extracellular fibrinogen (~500 nmol/L) and divalent cations, and required prior activation of the GPII(b)-III(a). A synthetic peptide (GRGDSP) and monoclonal anti-GPII(b)-III(a) antibody (2G12) that block platelet aggregation also blocked aggregation of these cells. Parent CHO cells or those expressing recombinant GPII(b)-III(a) containing a point mutation that causes variant thrombasthenia both failed to aggregate when stimulated in the presence of fibrinogen. These data show that GPII(b)-III(a) is the only unique platelet surface component required for aggregation.

Original languageEnglish (US)
Pages (from-to)369-376
Number of pages8
JournalBlood
Volume78
Issue number2
StatePublished - Jan 1 1991

ASJC Scopus subject areas

  • Biochemistry
  • Immunology
  • Hematology
  • Cell Biology

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