The glycoprotease of Pasteurella haemolytica A1 eliminates binding of myeloid cells to P-selectin but not to E-selectin

Biochem Biophys Res Commun. 1992 Oct 30;188(2):760-6. doi: 10.1016/0006-291x(92)91121-6.

Abstract

HL-60 cells and neutrophils treated with the glycoprotease from Pasteurella haemolytica A1, an enzyme which is specific for O-sialoglycoproteins, were found to be incapable of binding P-selectin but still bound E-selectin. Comparative analysis of [35-S] cysteine labeled proteins from HL-60 cells by 2-dimensional electrophoresis indicated that two major proteins with M(r) 100 and 115 kd were significantly removed from cells which had been treated.

Publication types

  • Comparative Study

MeSH terms

  • Antigens, CD / metabolism
  • Cell Adhesion Molecules / metabolism*
  • Cysteine / metabolism
  • E-Selectin
  • Electrophoresis, Gel, Two-Dimensional
  • Humans
  • Leukemia, Promyelocytic, Acute
  • Leukocyte Common Antigens / metabolism
  • Leukosialin
  • Mannheimia haemolytica / enzymology*
  • Membrane Glycoproteins / biosynthesis
  • Membrane Glycoproteins / isolation & purification
  • Membrane Glycoproteins / metabolism*
  • Metalloendopeptidases / metabolism*
  • Metalloendopeptidases / pharmacology
  • Neutrophils / metabolism*
  • P-Selectin
  • Platelet Membrane Glycoproteins / metabolism*
  • Protein Binding
  • Receptors, Lymphocyte Homing / metabolism
  • Sialoglycoproteins / biosynthesis
  • Sialoglycoproteins / isolation & purification
  • Sialoglycoproteins / metabolism*
  • Tumor Cells, Cultured

Substances

  • Antigens, CD
  • Cell Adhesion Molecules
  • E-Selectin
  • Leukosialin
  • Membrane Glycoproteins
  • P-Selectin
  • Platelet Membrane Glycoproteins
  • Receptors, Lymphocyte Homing
  • SPN protein, human
  • Sialoglycoproteins
  • Leukocyte Common Antigens
  • Metalloendopeptidases
  • O-sialoglycoprotein endopeptidase
  • Cysteine