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Titolo:
A carbohydrate neoepitope that is up-regulated on human mononuclear leucocytes by neuraminidase treatment or by cellular activation
Autore:
Quinn, MT; Swain, SD; Parkos, CA; Jutila, KL; Siemsen, DW; Kurk, SL; Jesaitis, AJ; Jutila, MA;
Indirizzi:
Montana State Univ, Dept Vet Mol Biol, Bozeman, MT 59717 USA Montana StateUniv Bozeman MT USA 59717 t Mol Biol, Bozeman, MT 59717 USA Montana State Univ, Dept Microbiol, Bozeman, MT 59717 USA Montana State Univ Bozeman MT USA 59717 Microbiol, Bozeman, MT 59717 USA Emory Univ, Dept Pathol & Lab Med, Atlanta, GA 30322 USA Emory Univ Atlanta GA USA 30322 t Pathol & Lab Med, Atlanta, GA 30322 USA
Titolo Testata:
IMMUNOLOGY
fascicolo: 2, volume: 104, anno: 2001,
pagine: 185 - 197
SICI:
0019-2805(200110)104:2<185:ACNTIU>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN T-CELLS; LEUKOCYTE ADHESION DEFICIENCY; ANTIGEN-PRESENTING CELLS; NODE HOMING RECEPTOR; LYMPHOCYTES-T; HUMAN-NEUTROPHILS; L-SELECTIN; SUBCELLULAR-LOCALIZATION; CHEMOTACTIC FACTORS; SURFACE EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
81
Recensione:
Indirizzi per estratti:
Indirizzo: Quinn, MT Montana State Univ, Dept Vet Mol Biol, Bozeman, MT 59717 USA Montana State Univ Bozeman MT USA 59717 , Bozeman, MT 59717 USA
Citazione:
M.T. Quinn et al., "A carbohydrate neoepitope that is up-regulated on human mononuclear leucocytes by neuraminidase treatment or by cellular activation", IMMUNOLOGY, 104(2), 2001, pp. 185-197

Abstract

The expression of cell-surface antigens can delineate specific leucocyte developmental or functional stages. For example, certain membrane glycoproteins are expressed selectively on leucocyte subsets only after activation. Leucocyte activation can also induce changes in carbohydrate epitopes expressed on surface antigens. In the present studies, we report on a novel monoclonal immunoglobulin M antibody (mAb 13.22) that recognizes a unique carbohydrate epitope expressed on human leucocyte membrane proteins. Characterization of mAb 13.22 specificity by immunoblotting showed that it recognized proteins of MW similar to 95 000 and 150 000, including both CD18 and CD11b. The mAb 13.22 epitope was removed by N-glycosidase F but not by endoglycosidase H or fucosidase, demonstrating that it is an N-linked carbohydrate antigen. Interestingly, immunoblot staining was enhanced after neuraminidase treatment, suggesting that the antibody epitope might also be partially masked by sialic acid. In resting leucocytes, the mAb 13.22 antigen was expressed strongly on neutrophils, while dull staining was present on monocytes, and no lymphocyte staining was observed. In marked contrast, treatment of leucocytes with neuraminidase resulted in exposure of a mAb 13.22 neoepitopeon a subset of lymphocytes (primarily T lymphocytes and natural killer cells) as well as up-regulated staining more than 18-fold on monocytes. Activation of lymphocytes in culture with phytohaemagglutinin or concanavalin A also unmasked the mAb 13.22 neoepitope on similar to 37% of the CD45RO(+) lymphocytes. Furthermore, analysis of leucocytes collected from the synovial fluid of patients with rheumatoid arthritis showed that similar to 18% of the lymphocytes present expressed the mAb 13.22 neoepitope. Taken together, our results suggest that the mAb 13.22 carbohydrate neoepitope could represent a physiologically relevant marker that is up-regulated on leucocyte subsets during the inflammatory response.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/21 alle ore 04:48:53