A monoclonal antibody, MEM-59, was prepared, which recognizes a heavily sialylated glycoprotein antigen expressed on most human leucocytes, the apparent molecular mass of which is strongly dependent on the concentration of polyacrylamide gel used for SDS-PAGE. The antigen isolated on immobilized MEM-59 reacted in Western blotting with mAbs described previously by others as recognizing antigens of similar properties. These experiments indicate that the molecules called CD43, gpL115 (sialophorin) or leukosialin are identical and different from a 75-85-kDa glycoprotein of similarly broad tissue distribution (CDw44). Most of the anti-CD43 mAbs recognize sialic acid-dependent epitopes. None of the anti-CD43 mAbs tested stimulated proliferation of peripheral blood leucocytes in vitro.
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Altered glycosylation of leukosialin, CD43, in HIV-1-infected cells of the CEM line.
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Laboratoire de Virologie, Faculté de Médecine, Hôpital de Cimiez, France.
CD43 (leukosialin, gpL115, sialophorin) is a major sialoglycoprotein widely expressed on hematopoietic cells that is defective in the congenital immunodeficiency Wiskott-Aldrich syndrome. It is thought to play an important role in cell-cell interactions and to be a costimulatory molecule for T lymphocyte activation. Using a metabolic 35SO4(2-) radiolabeling assay or biotinylation of cell surface proteins, we describe here that CD43 are sulfated molecules the glycosylation of which is altered in human immunodeficiency virus type 1 (HIV-1)-infected leukemic T cells of the CEM line.
View Article and Find Full Text PDFMechanism of mononuclear cell activation by an anti-CD43 (sialophorin) agonistic antibody.
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June 1989
Division of Allergy and Immunology, Children's Hospital, Boston, MA 02115.
CD43 (sialophorin, gpL115) is a sialoglycoprotein expressed on a wide variety of blood cells including lymphocytes, monocytes, neutrophils, and platelets. L10, an anti-CD43 mAb, has been shown to induce monocyte-dependent activation and proliferation of human T lymphocytes. We have studied the signaling mechanism involved in this activation process.
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Folia Biol (Praha)
May 1989
Institute of Molecular Genetics, Czechoslovak Academy of Sciences, Praha.
A monoclonal antibody, MEM-59, was prepared, which recognizes a heavily sialylated glycoprotein antigen expressed on most human leucocytes, the apparent molecular mass of which is strongly dependent on the concentration of polyacrylamide gel used for SDS-PAGE. The antigen isolated on immobilized MEM-59 reacted in Western blotting with mAbs described previously by others as recognizing antigens of similar properties. These experiments indicate that the molecules called CD43, gpL115 (sialophorin) or leukosialin are identical and different from a 75-85-kDa glycoprotein of similarly broad tissue distribution (CDw44).
View Article and Find Full Text PDFSialophorin, previously called gpL115, is the heavily sialylated surface protein that is defective in lymphocytes of Wiskott-Aldrich syndrome patients. Using the monoclonal antibody L10 as a probe, sialophorin expression was detected on isolated T lymphocytes and thymocytes, B cell lines, monocytes, neutrophils, and platelets, but not on erythrocytes, fibroblasts, and glioblastoma cells. This unusual distribution pattern suggests that sialophorin is expressed on all circulating cells except erythrocytes.
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Center for Blood Research, The Children's Hospital, Boston, Massachusetts 02115.
Biosynthesis was examined of sialophorin (formerly called gpL115) which is altered in the inherited immunodeficiency Wiskott-Aldrich syndrome. Sialophorin is greater than 50% carbohydrate, primarily O-linked units of sialic acid, galactose, and galactosamine. Pulse-labeling with [35S]methionine and chase incubation established that sialophorin is synthesized in CEM lymphoblastoid cells as an Mr 62,000 precursor which is converted within 45 min to mature glycosylated sialophorin, a long-lived molecule.
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