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rdf:type |
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lifeskim:mentions |
umls-concept:C0005456,
umls-concept:C0016006,
umls-concept:C0028778,
umls-concept:C0030957,
umls-concept:C0032521,
umls-concept:C0078056,
umls-concept:C0185027,
umls-concept:C0292863,
umls-concept:C0330390,
umls-concept:C0332206,
umls-concept:C1334087,
umls-concept:C1413006,
umls-concept:C1420426,
umls-concept:C1517880
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pubmed:issue |
3
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pubmed:dateCreated |
1998-4-23
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pubmed:abstractText |
The alpha 4 integrin LPAM-1 (alpha 4 beta 7) mediates lymphocyte attachment within the extracellular matrix (ECM) by adhering to the connecting segment (CS)-1 site of fibronectin (FN). Here we reveal that very late antigen (VLA)-4 LPAM-1+ T cell lymphoma TK-1 cells bind via LPAM-1 to multiple copies of the RGD sequence engineered within an FN-like polymer. Further, the small conformationally restrained RGD-like cyclic peptides 1-adamantaneacetyl-Cys-Gly-Arg-Gly-Asp-Ser-Pro-Cys and Arg-Cys-Asp-thioproline-Cys inhibit the adhesion of TK-1 cells to immobilized CS-1 peptide, and to endothelial counterreceptors for LPAM-1, namely mucosal addressin cell adhesion molecule (MAdCAM)-1 and vascular cell adhesion molecule (VCAM)-1. Spontaneous adhesion of the VLA-4- LPAM-1+ B lymphoma cell line RPMI 8866 to CS-1 was likewise inhibited, confirming a previously undocumented ability of LPAM-1 to recognize the RGD tripeptide. The RGD-binding site in LPAM-1 either overlaps or is identical to sites required for interaction with MAdCAM-1, VCAM-1, and the CS-1. The binding of LPAM-1 and VLA-4 to RGD-containing ligands may have relevance in vivo given that fibrinogen at physiological concentrations is able to partially block the binding of TK-1 cells to MAdCAM-1. Hence fibrinogen and other vascular RGD-containing proteins may have mild anti-inflammatory activity required for maintaining effective homeostasis, analogous to the anti-thrombogenic activity of the vascular endothelium.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Fibrinogen,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulins,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/MADCAM1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Madcam1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Mucoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides, Cyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Vascular Cell Adhesion Molecule-1,
http://linkedlifedata.com/resource/pubmed/chemical/arginyl-glycyl-aspartic acid,
http://linkedlifedata.com/resource/pubmed/chemical/glutamyl-isoleucyl-leucyl-aspartyl-v...,
http://linkedlifedata.com/resource/pubmed/chemical/integrin alpha4beta7
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0014-2980
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
995-1004
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9541595-Amino Acid Sequence,
pubmed-meshheading:9541595-Animals,
pubmed-meshheading:9541595-Binding, Competitive,
pubmed-meshheading:9541595-Binding Sites,
pubmed-meshheading:9541595-Carrier Proteins,
pubmed-meshheading:9541595-Cell Adhesion Molecules,
pubmed-meshheading:9541595-Cell Line,
pubmed-meshheading:9541595-Fibrinogen,
pubmed-meshheading:9541595-Fibronectins,
pubmed-meshheading:9541595-Humans,
pubmed-meshheading:9541595-Immunoglobulins,
pubmed-meshheading:9541595-Integrins,
pubmed-meshheading:9541595-Mice,
pubmed-meshheading:9541595-Molecular Sequence Data,
pubmed-meshheading:9541595-Mucoproteins,
pubmed-meshheading:9541595-Oligopeptides,
pubmed-meshheading:9541595-Peptides, Cyclic,
pubmed-meshheading:9541595-Protein Binding,
pubmed-meshheading:9541595-Vascular Cell Adhesion Molecule-1
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pubmed:year |
1998
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pubmed:articleTitle |
LPAM-1 (integrin alpha 4 beta 7)-ligand binding: overlapping binding sites recognizing VCAM-1, MAdCAM-1 and CS-1 are blocked by fibrinogen, a fibronectin-like polymer and RGD-like cyclic peptides.
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pubmed:affiliation |
Department of Molecular Medicine, School of Medicine, University of Auckland, New Zealand.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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