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rdf:type |
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lifeskim:mentions |
umls-concept:C0014257,
umls-concept:C0016055,
umls-concept:C0023688,
umls-concept:C0052350,
umls-concept:C0078056,
umls-concept:C0086574,
umls-concept:C0178719,
umls-concept:C0205263,
umls-concept:C0330390,
umls-concept:C0441471,
umls-concept:C1280500,
umls-concept:C1334087,
umls-concept:C1413006,
umls-concept:C1420426,
umls-concept:C1707455,
umls-concept:C2699006
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pubmed:issue |
4-5
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pubmed:dateCreated |
1997-4-22
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pubmed:abstractText |
The lymphocyte integrin alpha 4 beta 1 is the receptor for the Hep II domain and CS-1 site in fibronectin (Fn) as well as for VCAM-1. We recently showed that upon activation with anti-beta 1 mAb TS2/16, alpha 4 beta 1 also recognizes the RGD Fn sequence. To determine the physiological role of these multiple interactions, we have now studied some intracellular events induced by "resting" and activated alpha 4 beta 1 binding to its different ligands. Analyses of actin and tubulin reorganization upon adhesion of B lymphoid cells to Fn fragments or VCAM-1 showed that VCAM-1, a 38 kDa fragment (Hep II+CS-1), and the CS-1 synthetic peptide induced formation of transient cytoplasmic projections; however, cells attached to a 58 kDa (Hep II) or 80 kDa (RGD) fragments remained rounded. Using transfilter assays, we showed that VCAM-1, 38 kDa and CS-1 also induced dose-dependent B cell migration mediated by alpha 4 beta 1. Furthermore, these three ligands, but not the 80 kDa fragment or a synthetic peptide (H1) containing a sequence from Hep II shown to bind alpha 4 beta 1, induced tyrosine phosphorylation of a 110 kDa protein. Activation of alpha 4 beta 1 with TS2/16 inhibited the cytoplasmic protrusions and cell migration but did not affect the pattern of phosphorylation. Our results indicate that the various alpha 4 beta 1 ligands induce different cellular responses. Most importantly they show that alpha 4 beta 1 interaction with CS-1 is sufficient to trigger intracellular events in B cells. Furthermore, they suggest a regulation by the activation form of the receptor as well as by the ligand in events involving lymphocyte adhesion and migration.
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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/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin alpha4beta1,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/MARK1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Lymphocyte Homing,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Vascular Cell Adhesion Molecule-1
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1061-5385
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
251-67
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9117345-Amino Acid Sequence,
pubmed-meshheading:9117345-B-Lymphocytes,
pubmed-meshheading:9117345-Cell Adhesion,
pubmed-meshheading:9117345-Cell Line,
pubmed-meshheading:9117345-Cell Movement,
pubmed-meshheading:9117345-Cell Size,
pubmed-meshheading:9117345-Cytoskeletal Proteins,
pubmed-meshheading:9117345-Fibronectins,
pubmed-meshheading:9117345-Humans,
pubmed-meshheading:9117345-Integrin alpha4beta1,
pubmed-meshheading:9117345-Integrins,
pubmed-meshheading:9117345-Ligands,
pubmed-meshheading:9117345-Molecular Sequence Data,
pubmed-meshheading:9117345-Peptide Fragments,
pubmed-meshheading:9117345-Phosphorylation,
pubmed-meshheading:9117345-Protein-Serine-Threonine Kinases,
pubmed-meshheading:9117345-Receptors, Lymphocyte Homing,
pubmed-meshheading:9117345-Recombinant Proteins,
pubmed-meshheading:9117345-Signal Transduction,
pubmed-meshheading:9117345-Structure-Activity Relationship,
pubmed-meshheading:9117345-Vascular Cell Adhesion Molecule-1
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pubmed:year |
1996
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pubmed:articleTitle |
The alpha 4 beta 1 fibronectin ligands CS-1, Hep II, and RGD induce different intracellular events in B lymphoid cells. Comparison with the effects of the endothelial ligand VCAM-1.
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pubmed:affiliation |
Departmento de Inmunología, Centro de Investigaciones Biológicas, CSIC, Madrid, Spain.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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