Linked Life Data

7512373

Source:http://linkedlifedata.com/resource/pubmed/id/7512373

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-5-13
pubmed:abstractText
Integrin receptors are important for regulating lymphocyte recirculation and recruitment to sites of inflammation. Transfectants of the B cell lymphoma 38C13 were generated that differ exclusively in the expression of integrin beta 1 or beta 7 subunits allowing for a functional comparison of lymphocyte Peyer's patch HEV adhesion molecule 1 (LPAM-1) (alpha 4 beta 7) and very late antigen 4 (VLA-4) (alpha 4 beta 1) in an identical cellular environment. Whereas 38-beta 7 transfectants bound to purified and cellular mucosal addressin cell adhesion molecule (MAdCAM-1), unstimulated 38-beta 1 cells failed to bind MAdCAM-1. Treatment of 38-beta 1 cells with Mn2+ but not with PMA induced low level binding to MAdCAM-1. MAdCAM-1 adhesion of 38-beta 7 cells was constitutive and not enhanced by Mn2+ treatment. Similarly, MAdCAM-1-dependent adhesion to mucosal high endothelial venules was shown for 38-beta 7 but not for 38-beta 1 cells. The results therefore establish the LPAM-1-MAdCAM-1 interaction as the functionally dominant adhesion pathway for regulating lymphocyte homing to mucosal sites. Nonetheless, the activated VLA-4 on some lymphocytes may be involved in MAdCAM-1 recognition or promote binding to MAdCAM-1 in other tissues. By contrast, 38-beta 7 and 38-beta 1 transfectants did not differ in their binding capacity for vascular cell adhesion molecule 1 (VCAM-1) or fibronectin and LPAM-1 did not display any preference for interacting with either MAdCAM-1 or VCAM-1. LPAM-1 may therefore contribute significantly to cellular functions previously attributed to VLA-4. Interestingly, functional analysis of the intraepithelial lymphocyte integrin alpha IEL beta 7 which is structurally related to LPAM-1 did not reveal detectable binding activity for MAdCAM-1, VCAM-1, or fibronectin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0953-8178
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
263-75
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7512373-Animals, pubmed-meshheading:7512373-Base Sequence, pubmed-meshheading:7512373-Blotting, Western, pubmed-meshheading:7512373-CHO Cells, pubmed-meshheading:7512373-Cell Adhesion, pubmed-meshheading:7512373-Cell Adhesion Molecules, pubmed-meshheading:7512373-Cricetinae, pubmed-meshheading:7512373-Fibronectins, pubmed-meshheading:7512373-Immunoglobulins, pubmed-meshheading:7512373-Integrin beta Chains, pubmed-meshheading:7512373-Integrins, pubmed-meshheading:7512373-Mice, pubmed-meshheading:7512373-Molecular Sequence Data, pubmed-meshheading:7512373-Mucoproteins, pubmed-meshheading:7512373-Precipitin Tests, pubmed-meshheading:7512373-Receptors, Very Late Antigen, pubmed-meshheading:7512373-Tumor Cells, Cultured, pubmed-meshheading:7512373-Vascular Cell Adhesion Molecule-1
pubmed:year
1994
pubmed:articleTitle
Distinct binding specificities of integrins alpha 4 beta 7 (LPAM-1), alpha 4 beta 1 (VLA-4), and alpha IEL beta 7.
pubmed:affiliation
Institute of Medical Microbiology and Hygiene, Technical University of Munich, FRG.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't