Characterization of cDNA encoding full-length mouse platelet glycoprotein IX

Blood Coagul Fibrinolysis. 1998 Jun;9(4):381-5. doi: 10.1097/00001721-199806000-00011.

Abstract

Glycoprotein (GP) IX is a platelet membrane 20 kD protein, which is associated with GPIbalpha, GPIb beta, and GPV to form GPIb/IX/V complex. GPIb/IX/V complex is a major receptor for von Willebrand factor, which mediates platelet adhesion and aggregation under high shear stress conditions. The relevance of this receptor for hemostasis has been implicated by a congenital bleeding disorder lacking the receptor, Bernard-Soulier syndrome. All subunits for the human receptor have been cloned and characterized. However, the function of GPIX is still elusive. To obtain further information of GPIX, we have determined a cDNA sequence of mouse GPIX (811 bp). The deduced amino-acid sequence (177aa) was 71% identical to the human GPIX protein. All cysteine residues in extracytoplasmic domain and putative N-linked glycosylation site (Asn44) were conserved. Mouse GPIX contained a leucine-rich glycoprotein sequence composed of 24 amino acids, as did human GPIX.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cysteine / analysis
  • DNA Primers / genetics
  • DNA, Complementary / analysis*
  • Databases as Topic
  • Leucine / analysis
  • Mice
  • Mice, Inbred C57BL
  • Molecular Sequence Data
  • Platelet Glycoprotein GPIb-IX Complex / chemistry
  • Platelet Glycoprotein GPIb-IX Complex / genetics*
  • Polymerase Chain Reaction
  • Protein Conformation
  • Sequence Deletion / genetics
  • Sequence Homology, Amino Acid

Substances

  • DNA Primers
  • DNA, Complementary
  • Platelet Glycoprotein GPIb-IX Complex
  • Leucine
  • Cysteine

Associated data

  • GENBANK/AB007464