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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
35
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pubmed:dateCreated |
1993-1-12
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pubmed:abstractText |
The leukocyte integrin alpha 4 beta 1 (VLA-4, CD49d/CD29) is a receptor for the extracellular matrix protein fibronectin and the endothelial adhesion protein VCAM-1. We have analyzed the biosynthesis and post-translational modifications of the two subunits of this receptor complex. The alpha 4 subunit was initially synthesized as a single-chain polypeptide that underwent the formation of complex endoglycosidase H-resistant oligosaccharide side chains and which could be proteolytically cleaved into two noncovalently associated fragments. The level and rate of alpha 4 subunit cleavage was dependent on the cell studied. The T cell tumor line HPB-ALL expressed both intact and fragmented alpha 4 on the cell surface. The interleukin-2-dependent natural killer line NK 3.3 and long term interleukin-2-dependent activated T lymphocytes cleaved the alpha 4 polypeptide earlier and more efficiently than did HPB-ALL cells and did not have detectable levels of intact alpha 4 on the cell surface. The proteolysis of alpha 4 was blocked by treating cells with either the lysosomotrophic amine NH4Cl or the carboxylic ionophore monensin. The presence of complex N-linked oligosaccharides did not seem to be necessary for alpha 4 cleavage or for binding of the alpha 4 beta 1 complex to a synthetic peptide corresponding to the binding site for this receptor on fibronectin.
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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/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin alpha4beta1,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Very Late Antigen
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
25274-81
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1281155-Amino Acid Sequence,
pubmed-meshheading:1281155-Antibodies, Monoclonal,
pubmed-meshheading:1281155-Epitopes,
pubmed-meshheading:1281155-Fibronectins,
pubmed-meshheading:1281155-Glycoside Hydrolases,
pubmed-meshheading:1281155-Humans,
pubmed-meshheading:1281155-Immunoblotting,
pubmed-meshheading:1281155-Integrin alpha4beta1,
pubmed-meshheading:1281155-Integrins,
pubmed-meshheading:1281155-Interleukin-2,
pubmed-meshheading:1281155-Leukocytes,
pubmed-meshheading:1281155-Macromolecular Substances,
pubmed-meshheading:1281155-Molecular Sequence Data,
pubmed-meshheading:1281155-Peptides,
pubmed-meshheading:1281155-Precursor Cell Lymphoblastic Leukemia-Lymphoma,
pubmed-meshheading:1281155-Protease Inhibitors,
pubmed-meshheading:1281155-Protein Processing, Post-Translational,
pubmed-meshheading:1281155-Receptors, Very Late Antigen,
pubmed-meshheading:1281155-T-Lymphocytes,
pubmed-meshheading:1281155-Tumor Cells, Cultured
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pubmed:year |
1992
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pubmed:articleTitle |
Post-translational processing of the leukocyte integrin alpha 4 beta 1.
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pubmed:affiliation |
Department of Immunology, University of Texas M. D. Anderson Cancer Center, Houston 77030.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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