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

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...

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Veröffentlicht in:	Biochemical and biophysical research communications 1992-10, Vol.188 (2), p.760-766
Hauptverfasser:	Steininger, Christina N., Eddy, Christopher A., Leimgruber, Richard M., Mellors, Alan, Welply, Joseph K.
Format:	Artikel
Sprache:	eng
Schlagworte:	Antigens, CD - metabolism Biochemistry & Molecular Biology Biological and medical sciences Biophysics Cell Adhesion Molecules - metabolism Cell interactions, adhesion Cysteine - metabolism E-Selectin Electrophoresis, Gel, Two-Dimensional Fundamental and applied biological sciences. Psychology Humans Leukemia, Promyelocytic, Acute Leukocyte Common Antigens - metabolism Leukosialin Life Sciences & Biomedicine Mannheimia haemolytica - enzymology Membrane Glycoproteins - biosynthesis Membrane Glycoproteins - isolation & purification Membrane Glycoproteins - metabolism Metalloendopeptidases - metabolism Metalloendopeptidases - pharmacology Molecular and cellular biology Neutrophils - metabolism P-Selectin Pasteurella haemolytica Platelet Membrane Glycoproteins - metabolism Protein Binding Receptors, Lymphocyte Homing - metabolism Science & Technology Sialoglycoproteins - biosynthesis Sialoglycoproteins - isolation & purification Sialoglycoproteins - metabolism Tumor Cells, Cultured
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Zusammenfassung:	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.
ISSN:	0006-291X 1090-2104
DOI:	10.1016/0006-291X(92)91121-6