Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0001511 (Adhesion)
 5,955 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Adhesion between lymphocytes and other cells is critical to many processes in the normal immune system. Alteration in the expression of cell adhesion molecules may be important in determining the behaviour of malignant lymphomas. In this study, the adhesion of normal lymphocytes to fibroblasts is compared with the adhesion of the T-cell lymphomas J6 and Hut 78 ICRF. J6 was significantly more adherent to fibroblasts than either Hut78 or PBL despite the fact that J6 expresses almost no LFA-1. Anti-LFA-1 had little effect on the basal adhesion of Hut78 ICRF or PBL. Addition of anti-CD2 caused enhanced adhesion of J6 and PBL but not Hut78 ICRF, which expresses little of this molecule. This enhancement was abrogated by anti-LFA-1. Anti-CD45 also caused enhanced adhesion of PBL. This was largely due to LFA-1-mediated homotypic cell adhesion. The tumour cell lines display no such homotypic adhesion and the small enhancement of fibroblast adhesion was much less affected by the anti-LFA-1 antibody. These results show the complex interactions which occur between adhesion molecules and that differences in patterns of expression between normal and neoplastic cells could be a major determinant of tumour cell behaviour.
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PMID:Adhesion of normal and neoplastic lymphoid cells to fibroblasts. 207 14

Recent research demonstrates that the beta1 integrins may be involved in neutrophil migration. Here, we investigate the role of nitric oxide in the expression and function of the very late antigen-4 (VLA-4) and Mac-1 integrins on human neutrophils. Human blood neutrophils were treated with N(omega)-nitro-L-arginine methyl ester (L-NAME) and their adhesion to fibronectin (FN) and serum observed. Adhesion of neutrophils to FN and serum increased significantly following incubation with 0.1mM L-NAME by 65.5 and 44.6%, respectively. Increased adhesions to FN and serum were abolished by a VLA-4-specific monoclonal antibody, HP2/1, and a Mac-1-specific monoclonal antibody, ICRF 44, respectively. The microfilament- and microtubule-depolymerizing agents, dihydrochalasin B and nocodazole, were also able to reverse L-NAME-induced adhesion to both FN and serum. L-NAME induced a discrete increase in the expression of CD49d (VLA-4, 25.3+/-4.8%), but not CD11b, on the neutrophil cell surface, as detected by flow cytometry. Results indicate that NO has a role in regulating VLA-4 and Mac-1 function on the human neutrophil cell surface and that this modulation in integrin function is accompanied by cytoskeletal rearrangements and changes in the ability of the neutrophil to adhere to the extracellular matrix.
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PMID:Nitric oxide has a role in regulating VLA-4-integrin expression on the human neutrophil cell surface. 1281 64