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Titolo:
Antibody binding to a conformation-dependent epitope induces L-selectin association with the detergent-resistant cytoskeleton
Autore:
Leid, JG; Steeber, DA; Tedder, TF; 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 Duke Univ, Med Ctr, Dept Immunol, Durham, NC 27710 USA Duke Univ Durham NC USA 27710 Med Ctr, Dept Immunol, Durham, NC 27710 USA
Titolo Testata:
JOURNAL OF IMMUNOLOGY
fascicolo: 8, volume: 166, anno: 2001,
pagine: 4899 - 4907
SICI:
0022-1767(20010415)166:8<4899:ABTACE>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
LEUKOCYTE ADHESION MOLECULE-1; HIGH ENDOTHELIAL VENULES; HUMAN NEUTROPHILS; CROSS-LINKING; CELL-SURFACE; P-SELECTIN; CHEMOTACTIC FACTORS; HYDRODYNAMIC SHEAR; CYTOPLASMIC DOMAIN; REPERFUSION INJURY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Jutila, MA Montana State Univ, Dept Vet Mol Biol, Bozeman, MT 59717 USA Montana State Univ Bozeman MT USA 59717 Bozeman, MT 59717 USA
Citazione:
J.G. Leid et al., "Antibody binding to a conformation-dependent epitope induces L-selectin association with the detergent-resistant cytoskeleton", J IMMUNOL, 166(8), 2001, pp. 4899-4907

Abstract

L-Selectin mediates leukocyte rolling on endothelium and immobilized leukocytes. Its regulation has been the subject of much study, and the conformation of the molecule may play an important role in its function. Here we report that a conformational change in L-selectin, induced by an anti-lectin domain mAb (LAM1-116) and recognized by another mAb directed to a conserved epitope on L-selectin (EL-246), predisposed L-selectin to cytoskeletal association. This effect was due to direct binding of the mAb, not to overt signaling events, and was specific to LAM1-116. Nineteen other anti-L-selectinmAbs directed against the lectin, epidermal growth factor, or short consensus repeat domains lacked this activity. The induced conformational change occurred at 37 degreesC, at 4 degreesC, in the presence of sodium azide andtyrosine kinase inhibitors herbimycin A and genistein, and with soluble detergent-extracted L-selectin. In the presence of LAM1-116, EL-246 induced cytoskeletal association of L-selectin in the absence of Ab cross-linking asvisualized by L-selectin staining after low dose detergent treatment of the cells. We propose that the conformational change described herein regulates L-selectin-mediated events by exposing a high avidity binding site that,when engaged, triggers association of L-selectin with the cytoskeleton, which may lead to stronger tethers with physiological ligands.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 12:35:35