Characterisation of a membrane receptor on ruminants and equine platelets and peripheral blood leukocytes similar to the human integrin receptor glycoprotein IIb/IIIa (CD41/61)

This paper describes two anti-glycoprotein IIb/IIIa or CD41/61 murine monoclonal antibodies (Co.35E4 and Co.2oA1). The cellular distribution and apparent molecular weight of the antigen detected by these antibodies is consistent with their reaction with ruminant and equine glycoprotein IIb/IIIa. Bio...

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Bibliographic Details
Published in:Veterinary immunology and immunopathology 1995-02, Vol.44 (3-4), p.359-368
Main Authors: Pintado, C.O. (Cordoba Univ. (Spain). Facultad de Veterinaria, Dept. de Genetica), Friend, M, Llanes, D
Format: Article
Language:English
Subjects:
Animals
Antibodies, Monoclonal - biosynthesis
ANTICORPS MONOCLONAL
ANTICUERPOS MONOCLONALES
Antigens, CD - analysis
Blood Platelets - chemistry
CABALLOS
CHEVAL
Epitopes
GLICOPROTEINAS
GLYCOPROTEINE
GLYCOPROTEINS
HORSES
Horses - blood
LEUCOCITOS
LEUCOCYTE
LEUKOCYTES
Leukocytes - chemistry
Mice
MONOCLONAL ANTIBODIES
Platelet Membrane Glycoproteins - analysis
Platelet Membrane Glycoproteins - immunology
Receptors, Cell Surface - analysis
RUMIANTE
RUMINANT
RUMINANTS
Ruminants - blood
Species Specificity
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Summary:This paper describes two anti-glycoprotein IIb/IIIa or CD41/61 murine monoclonal antibodies (Co.35E4 and Co.2oA1). The cellular distribution and apparent molecular weight of the antigen detected by these antibodies is consistent with their reaction with ruminant and equine glycoprotein IIb/IIIa. Biochemical analysis of the equine molecule using sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) revealed bands of 24, 100 and 110 kDa under reducing conditions and 115 and 80 kDa under nonreducing conditions. Biochemical analysis of ruminant antigen revealed that the 24 kDa band did not appear owing to the absence of labelling with sulpho-NHS-biotin. Co.35E4 and Co.20A1 recognised two different Ca2+ complex independent epitopes. The glycoprotein IIb/IIIa was present on ruminant and equine granulocytes, monocytes and platelets. However, binding on granulocytes and monocytes was due to the adsorption of membrane platelet fragments.
ISSN:0165-2427
1873-2534
DOI:10.1016/0165-2427(94)05310-O