A major endothelial plasmalemmal sialoglycoprotein, gp60, is immunologically related to glycophorin.
AUTOR(ES)
Schnitzer, J E
RESUMO
Glycophorins, the major sialoglycoproteins of red blood cells in many species, are generally considered to be specific to erythroid cells. Using polyclonal antibodies directed against mouse glycophorin (alpha gp), we have identified a glycoprotein antigenically related to glycophorin on the surface of bovine and rat cultured endothelial cells. Immunoblotting with alpha gp identified a single 60-kDa polypeptide on transfers of SDS/polyacrylamide gels of solubilized confluent endothelial monolayers. In addition, a 60-kDa polypeptide was immunoprecipitated by alpha gp from lysates of 125I-labeled intact endothelial cells. Controls with preimmune serum were negative. This antibody interaction was inhibited by murine erythrocyte ghosts and purified glycophorins. Our past work identified several endothelial surface sialoglycoproteins including a 60-kDa glycoprotein (gp60) that (i) interacts with albumin, (ii) binds Limax flavus, Ricinus communis, and Triticum vulgare agglutinins but not other lectins, (iii) is sequentially precipitated from 125I-labeled cell lysates by using R. communis agglutinin followed by T. vulgare agglutinin, and (iv) is sensitive to sialidase digestion. Immunoblotting of such precipitates with alpha gp demonstrates that lectins recognize the same glycoprotein, namely gp60. These results indicate that gp60, a major endothelial surface sialoglycoprotein, shares antigenic epitope(s) with glycophorin.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=54634Documentos Relacionados
- Differentiation of human erythroid cells is associated with increased O-glycosylation of the major sialoglycoprotein, glycophorin A.
- The cytolytic toxin aerolysin must aggregate to disrupt erythrocytes, and aggregation is stimulated by human glycophorin.
- Immunohistochemical identification of erythroid precursors in paraffin embedded bone marrow sections: spectrin is a superior marker to glycophorin.
- Amino-acid sequence and oligosaccharide attachment sites of human erythrocyte glycophorin.
- Senescent cell antigen is immunologically related to band 3.