| pubmed-article:1281155 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1281155 | lifeskim:mentions | umls-concept:C0330390 | lld:lifeskim |
| pubmed-article:1281155 | lifeskim:mentions | umls-concept:C0023516 | lld:lifeskim |
| pubmed-article:1281155 | lifeskim:mentions | umls-concept:C1334087 | lld:lifeskim |
| pubmed-article:1281155 | lifeskim:mentions | umls-concept:C0292863 | lld:lifeskim |
| pubmed-article:1281155 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:1281155 | pubmed:issue | 35 | lld:pubmed |
| pubmed-article:1281155 | pubmed:dateCreated | 1993-1-12 | lld:pubmed |
| pubmed-article:1281155 | 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. | lld:pubmed |
| pubmed-article:1281155 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1281155 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1281155 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1281155 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1281155 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1281155 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1281155 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1281155 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1281155 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1281155 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1281155 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1281155 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1281155 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:1281155 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1281155 | pubmed:author | pubmed-author:BednarczykJ... | lld:pubmed |
| pubmed-article:1281155 | pubmed:author | pubmed-author:McIntyreB WBW | lld:pubmed |
| pubmed-article:1281155 | pubmed:author | pubmed-author:SzaboM CMC | lld:pubmed |
| pubmed-article:1281155 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1281155 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1281155 | pubmed:volume | 267 | lld:pubmed |
| pubmed-article:1281155 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1281155 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1281155 | pubmed:pagination | 25274-81 | lld:pubmed |
| pubmed-article:1281155 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:1281155 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1281155 | pubmed:articleTitle | Post-translational processing of the leukocyte integrin alpha 4 beta 1. | lld:pubmed |
| pubmed-article:1281155 | pubmed:affiliation | Department of Immunology, University of Texas M. D. Anderson Cancer Center, Houston 77030. | lld:pubmed |
| pubmed-article:1281155 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1281155 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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