| pubmed-article:9233649 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9233649 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:9233649 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:9233649 | lifeskim:mentions | umls-concept:C0001511 | lld:lifeskim |
| pubmed-article:9233649 | lifeskim:mentions | umls-concept:C0021701 | lld:lifeskim |
| pubmed-article:9233649 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:9233649 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:9233649 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:9233649 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:9233649 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:9233649 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:9233649 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:9233649 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:9233649 | pubmed:dateCreated | 1997-8-14 | lld:pubmed |
| pubmed-article:9233649 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9233649 | pubmed:abstractText | Beta 7 integrins serve special roles in mucosal immunity. Alpha 4 beta 7-mediated adhesion to mucosal addressin cell adhesion molecule-1 (MAdCAM-1) directs lymphocyte homing to the gut, and alpha E beta 7 mediates binding of lymphocytes to E-cadherin on epithelial cells. Since alpha 4 beta 7 mediates adhesion to MAdCAM-1 but alpha 4 beta 1 does not, we used beta 7/beta 1 chimeras to directly assess the importance of specific regions of beta 7 in MAdCAM-1 binding. We found a region of beta 7 (residues 46-386) that accounts for specificity of alpha 4 beta 7 binding to MAdCAM-1. We also used human/mouse and human/rat chimeric beta 7 subunits to map epitopes recognized by fifteen anti-beta 7 mAbs. Six of seven Abs that block adhesion to MAdCAM-1 and E-cadherin (Fib 21, 22, 27, 30, 504; Act-1) mapped to amino acid residues 176-250. Residues 176-250 lie within the region of beta 7 that specifies MAdCAM-1 binding and also within a region that has a predicted structure homologous to the metal ion-dependent adhesion site (MIDAS) domains of the integrin subunits alpha L and alpha M. Three new Abs that recognize beta 7 in the presence of Mn2+, but not Ca2+, and promote adhesion to MAdCAM-1, mapped to amino acids 46-149. One blocking and five other Abs mapped to other regions (amino acids 387-725). We conclude that a MIDAS-like domain serves a critical role in beta 7 integrin-mediated adhesion. | lld:pubmed |
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| pubmed-article:9233649 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9233649 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:9233649 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9233649 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9233649 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:9233649 | pubmed:issn | 0022-1767 | lld:pubmed |
| pubmed-article:9233649 | pubmed:author | pubmed-author:SuS CSC | lld:pubmed |
| pubmed-article:9233649 | pubmed:author | pubmed-author:ButcherE CEC | lld:pubmed |
| pubmed-article:9233649 | pubmed:author | pubmed-author:KilshawP JPJ | lld:pubmed |
| pubmed-article:9233649 | pubmed:author | pubmed-author:CochranNN | lld:pubmed |
| pubmed-article:9233649 | pubmed:author | pubmed-author:NayR MRM | lld:pubmed |
| pubmed-article:9233649 | pubmed:author | pubmed-author:AndrewD PDP | lld:pubmed |
| pubmed-article:9233649 | pubmed:author | pubmed-author:LazarovitsA... | lld:pubmed |
| pubmed-article:9233649 | pubmed:author | pubmed-author:ErleD JDJ | lld:pubmed |
| pubmed-article:9233649 | pubmed:author | pubmed-author:YednockT ATA | lld:pubmed |
| pubmed-article:9233649 | pubmed:author | pubmed-author:BrissieE OEO | lld:pubmed |
| pubmed-article:9233649 | pubmed:author | pubmed-author:DunhamEE | lld:pubmed |
| pubmed-article:9233649 | pubmed:author | pubmed-author:TidswellMM | lld:pubmed |
| pubmed-article:9233649 | pubmed:author | pubmed-author:PachynskiRR | lld:pubmed |
| pubmed-article:9233649 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9233649 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9233649 | pubmed:volume | 159 | lld:pubmed |
| pubmed-article:9233649 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9233649 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9233649 | pubmed:pagination | 1497-505 | lld:pubmed |
| pubmed-article:9233649 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:9233649 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9233649 | pubmed:articleTitle | Structure-function analysis of the integrin beta 7 subunit: identification of domains involved in adhesion to MAdCAM-1. | lld:pubmed |
| pubmed-article:9233649 | pubmed:affiliation | Lung Biology Center, Department of Medicine, University of California, San Francisco 94143, USA. easd@itsa.ucsf.edu | lld:pubmed |
| pubmed-article:9233649 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9233649 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9233649 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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