| pubmed-article:14761956 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14761956 | lifeskim:mentions | umls-concept:C0567416 | lld:lifeskim |
| pubmed-article:14761956 | lifeskim:mentions | umls-concept:C0599851 | lld:lifeskim |
| pubmed-article:14761956 | lifeskim:mentions | umls-concept:C0085103 | lld:lifeskim |
| pubmed-article:14761956 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:14761956 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:14761956 | lifeskim:mentions | umls-concept:C2754100 | lld:lifeskim |
| pubmed-article:14761956 | lifeskim:mentions | umls-concept:C1412206 | lld:lifeskim |
| pubmed-article:14761956 | lifeskim:mentions | umls-concept:C1413393 | lld:lifeskim |
| pubmed-article:14761956 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:14761956 | pubmed:dateCreated | 2004-4-12 | lld:pubmed |
| pubmed-article:14761956 | pubmed:abstractText | The neural cell adhesion molecule "close homologue of L1," termed CHL1, has functional importance in the nervous system. CHL1 is expressed as a transmembrane protein of 185 kDa, and ectodomain shedding releases soluble fragments relevant for its physiological function. Here we describe that ADAM8, a member of the family of metalloprotease disintegrins cleaves a CHL1-Fc fusion protein in vitro at two sites corresponding to release of the extracellular domain of CHL1 in fibronectin (FN) domains II (125 kDa) and V (165 kDa), inhibited by batimastat (BB-94). Cleavage of CHL1-Fc in the 125-kDa fragment was not detectable under non-reducing conditions arguing that cleavage resulting in the 165-kDa fragment is more relevant in releasing soluble CHL1 in vivo. In cells transfected with full-length ADAM8, membrane proximal cleavage of CHL1 was similar and not stimulated by phorbol ester 12-O-tetradecanoylphorbol-13-acetate and pervanadate. No cleavage of CHL1 was observed in cells expressing either inactive ADAM8 with a Glu330 to Gln exchange (EQ-A8), or active ADAM10 and ADAM17. Consequently, processing of CHL1 was hardly detectable in brain extracts of ADAM8-deficient mice but enhanced in a neurodegenerative mouse mutant. CHL1 processed by ADAM8 in supernatants of COS-7 cells and in co-culture with cerebellar granule neurons was very potent in stimulating neurite outgrowth and suppressing neuronal cell death, not observed in cells co-transfected with CHL1/EQ-A8, CHL1/ADAM10, or CHL1/ADAM17. Taken together, we propose that ADAM8 plays an important role in physiological and pathological cell interactions by a specific release of functional CHL1 from the cell surface. | lld:pubmed |
| pubmed-article:14761956 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14761956 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14761956 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14761956 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:14761956 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14761956 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:14761956 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:14761956 | pubmed:author | pubmed-author:SchachnerMeli... | lld:pubmed |
| pubmed-article:14761956 | pubmed:author | pubmed-author:BartschJörg... | lld:pubmed |
| pubmed-article:14761956 | pubmed:author | pubmed-author:RichterMelani... | lld:pubmed |
| pubmed-article:14761956 | pubmed:author | pubmed-author:WildeboerDirk... | lld:pubmed |
| pubmed-article:14761956 | pubmed:author | pubmed-author:NausSilviaS | lld:pubmed |
| pubmed-article:14761956 | pubmed:author | pubmed-author:MossMarciaM | lld:pubmed |
| pubmed-article:14761956 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14761956 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:14761956 | pubmed:volume | 279 | lld:pubmed |
| pubmed-article:14761956 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14761956 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14761956 | pubmed:pagination | 16083-90 | lld:pubmed |
| pubmed-article:14761956 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:14761956 | pubmed:meshHeading | pubmed-meshheading:14761956... | lld:pubmed |
| pubmed-article:14761956 | pubmed:meshHeading | pubmed-meshheading:14761956... | lld:pubmed |
| pubmed-article:14761956 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14761956 | pubmed:articleTitle | Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death. | lld:pubmed |
| pubmed-article:14761956 | pubmed:affiliation | Entwicklungsbiologie & Molekulare Pathologie, W7, Universität Bielefeld, 33501 Bielefeld, Germany. | lld:pubmed |
| pubmed-article:14761956 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14761956 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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