| pubmed-article:12138159 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12138159 | lifeskim:mentions | umls-concept:C0175677 | lld:lifeskim |
| pubmed-article:12138159 | lifeskim:mentions | umls-concept:C0022646 | lld:lifeskim |
| pubmed-article:12138159 | lifeskim:mentions | umls-concept:C0001511 | lld:lifeskim |
| pubmed-article:12138159 | lifeskim:mentions | umls-concept:C0034963 | lld:lifeskim |
| pubmed-article:12138159 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:12138159 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:12138159 | pubmed:issue | 42 | lld:pubmed |
| pubmed-article:12138159 | pubmed:dateCreated | 2002-10-15 | lld:pubmed |
| pubmed-article:12138159 | pubmed:abstractText | KIM-1 (kidney injury molecule-1) is a type I transmembrane glycoprotein expressed on dedifferentiated renal proximal tubule epithelial cells undergoing regeneration after toxic or ischemic injury. The extracellular domain of KIM-1 is composed of an immunoglobulin-like domain topping a long mucin-like domain, a structure that points to a possible role in cell adhesion by homology to several known adhesion proteins. Two splice variants (a and b), of the human KIM-1 having identical extracellular domains, differ in their cytoplasmic domains and tissue distributions. In this study, we report that the KIM-1b transcript is expressed predominantly in adult human kidney. We describe the generation of 10 monoclonal antibodies against the extracellular domain of human KIM-1, the mapping of their binding sites, and their use in identifying various forms of the protein. We show that human KIM-1b is expressed in adult kidney cell lines, and we demonstrate that a soluble form of KIM-1 is shed constitutively into the culture medium of the cell lines expressing endogenous or recombinant KIM-1b by membrane-proximal cleavage. A monoclonal antibody that binds at or close to the proteolytic site can partially block the shedding of KIM-1. Release of soluble KIM-1 is enhanced by activating the cells with phorbol 12-myristate 13-acetate and can be inhibited with two metalloproteinase inhibitors, BB-94 (Batimastat) and GM6001 (Ilomastat), suggesting that the cleavage is mediated by a metalloproteinase. We propose that the shedding of KIM-1 in the kidney undergoing regeneration constitutes an active mechanism allowing dedifferentiated regenerating cells to scatter on denuded patches of the basement membrane and reconstitute a continuous epithelial layer. | lld:pubmed |
| pubmed-article:12138159 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12138159 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12138159 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12138159 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:12138159 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:12138159 | pubmed:author | pubmed-author:BonventreJose... | lld:pubmed |
| pubmed-article:12138159 | pubmed:author | pubmed-author:SanicolaMiche... | lld:pubmed |
| pubmed-article:12138159 | pubmed:author | pubmed-author:BaillyVeroniq... | lld:pubmed |
| pubmed-article:12138159 | pubmed:author | pubmed-author:ZhangZhiweiZ | lld:pubmed |
| pubmed-article:12138159 | pubmed:author | pubmed-author:MeierWernerW | lld:pubmed |
| pubmed-article:12138159 | pubmed:author | pubmed-author:CateRichardR | lld:pubmed |
| pubmed-article:12138159 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12138159 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:12138159 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:12138159 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12138159 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12138159 | pubmed:pagination | 39739-48 | lld:pubmed |
| pubmed-article:12138159 | pubmed:dateRevised | 2008-7-8 | lld:pubmed |
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| pubmed-article:12138159 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12138159 | pubmed:articleTitle | Shedding of kidney injury molecule-1, a putative adhesion protein involved in renal regeneration. | lld:pubmed |
| pubmed-article:12138159 | pubmed:affiliation | BIOGEN Inc., Cambridge, Massachusetts 02142, USA. Veronique_Bailly@biogen.com | lld:pubmed |
| pubmed-article:12138159 | pubmed:publicationType | Journal Article | lld:pubmed |
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