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Titolo:
LIGATION OF L-SELECTIN ON T-LYMPHOCYTES ACTIVATES BETA(1) INTEGRINS AND PROMOTES ADHESION TO FIBRONECTIN
Autore:
GIBLIN PA; HWANG ST; KATSUMOTO TR; ROSEN SD;
Indirizzi:
UNIV CALIF SAN FRANCISCO,DEPT ANAT,513 PARNASSUS AVE SAN FRANCISCO CA94143 UNIV CALIF SAN FRANCISCO,DEPT ANAT SAN FRANCISCO CA 94143 UNIV CALIF SAN FRANCISCO,PROGRAM IMMUNOL SAN FRANCISCO CA 94143
Titolo Testata:
The Journal of immunology
fascicolo: 7, volume: 159, anno: 1997,
pagine: 3498 - 3507
SICI:
0022-1767(1997)159:7<3498:LOLOTA>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-ADHESION; HIGH ENDOTHELIUM; HUMAN NEUTROPHILS; IN-VIVO; RECEPTOR; EXPRESSION; MIGRATION; MOLECULE; AFFINITY; BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
66
Recensione:
Indirizzi per estratti:
Citazione:
P.A. Giblin et al., "LIGATION OF L-SELECTIN ON T-LYMPHOCYTES ACTIVATES BETA(1) INTEGRINS AND PROMOTES ADHESION TO FIBRONECTIN", The Journal of immunology, 159(7), 1997, pp. 3498-3507

Abstract

Lymphocyte recirculation is dependent on families of adhesion molecules expressed on lymphocytes and their sequential interaction with ligands expressed on high endothelial venules in secondary lymphoid organssuch as peripheral lymph nodes, By binding its carbohydrate-based ligands, L-selectin initiates this cascade of molecular interactions, supporting the rolling of lymphocytes along high endothelial venules. Subsequent activation of lymphocyte integrins leads to cell arrest followed by lymphocyte extravasation, Here, we demonstrate stimulated adhesion of PBL and Jurkat T cells to immobilized fibronectin following treatment with (1) GlyCAM-1, a physiologic ligand for L-selectin, and (2) cross-linked anti-L-selectin mAbs, We also utilize a solution binding assay to detect early changes in integrin activity, including affinitymodulation and/or integrin clustering, and distinguish these from later postreceptor binding events such as changes in cell shape and spreading, With the Jurkat cell line, GlyCAM-1 and fucoidin (an L-selectin ligand mimetic) induce the binding of soluble fibronectin. In contrast, stimulation through the Jurkat TCR fails to promote binding to soluble ligand even though TCR cross-linking markedly enhances adhesion to immobilized fibronectin, These data suggest that L-selectin and the TCR promote adhesion through distinct mechanisms, Finally, we demonstrate that beta(1) integrins are preferentially activated on naive T cellsthrough the L-selectin pathway, Together with our previous studies showing similar activation of beta(2) integrins on the naive T cell subset, these data suggest that signals delivered though L-selectin participate in the preferential recruitment of these cells to peripheral lymph nodes.

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Documento generato il 30/11/20 alle ore 07:18:11