期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1990
卷号：87
期号：17
页码：6843-6847
DOI：10.1073/pnas.87.17.6843
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
