| pubmed-article:9265643 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9265643 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:9265643 | lifeskim:mentions | umls-concept:C0012984 | lld:lifeskim |
| pubmed-article:9265643 | lifeskim:mentions | umls-concept:C0553257 | lld:lifeskim |
| pubmed-article:9265643 | lifeskim:mentions | umls-concept:C0242275 | lld:lifeskim |
| pubmed-article:9265643 | lifeskim:mentions | umls-concept:C0205111 | lld:lifeskim |
| pubmed-article:9265643 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
| pubmed-article:9265643 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:9265643 | lifeskim:mentions | umls-concept:C1152589 | lld:lifeskim |
| pubmed-article:9265643 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:9265643 | lifeskim:mentions | umls-concept:C1709634 | lld:lifeskim |
| pubmed-article:9265643 | lifeskim:mentions | umls-concept:C0332324 | lld:lifeskim |
| pubmed-article:9265643 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:9265643 | pubmed:dateCreated | 1997-9-15 | lld:pubmed |
| pubmed-article:9265643 | pubmed:abstractText | EGF precursor (proEGF) is a member of the family of membrane-anchored EGF-like growth factors that bind with high affinity to the epidermal growth factor receptor (EGFR). In contrast to human transforming growth factor-alpha precursor (proTGFalpha), which is sorted basolaterally in Madin-Darby canine kidney (MDCK) cells (Dempsey, P., and R. Coffey, 1994. J. Biol. Chem. 269:16878-16889), we now demonstrate that human proEGF overexpressed in MDCK cells is found predominantly at the apical membrane domain under steady-state conditions. Nascent proEGF (185 kD) is not sorted but is delivered equally to the apical and basolateral membranes, where it is proteolytically cleaved within its ectodomain to release a soluble 170-kD EGF form into the medium. Unlike the fate of TGFalpha in MDCK cells, the soluble 170-kD EGF species accumulates in the medium, does not interact with the EGFR, and is not processed to the mature 6-kD peptide. We show that the rate of ectodomain cleavage of 185-kD proEGF is fourfold greater at the basolateral surface than at the apical surface and is sensitive to a metalloprotease inhibitor, batimastat. Batimastat dramatically inhibited the release of soluble 170-kD EGF into the apical and basal medium by 7 and 60%, respectively, and caused a concordant increase in the expression of 185-kD proEGF at the apical and basolateral cell surfaces of 150 and 280%, respectively. We propose that preferential ectodomain cleavage at the basolateral surface contributes to apical domain localization of 185-kD proEGF in MDCK cells, and this provides a novel mechanism to achieve a polarized distribution of cell surface membrane proteins under steady-state conditions. In addition, differences in disposition of EGF and TGFalpha in polarized epithelial cells offer a new conceptual framework to consider the actions of these polypeptide growth factors. | lld:pubmed |
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| pubmed-article:9265643 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9265643 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9265643 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9265643 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9265643 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9265643 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:9265643 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:9265643 | pubmed:author | pubmed-author:NishikawaKK | lld:pubmed |
| pubmed-article:9265643 | pubmed:author | pubmed-author:YoshitakeYY | lld:pubmed |
| pubmed-article:9265643 | pubmed:author | pubmed-author:DempseyP JPJ | lld:pubmed |
| pubmed-article:9265643 | pubmed:author | pubmed-author:CoffeyR JRJ | lld:pubmed |
| pubmed-article:9265643 | pubmed:author | pubmed-author:MeiseK SKS | lld:pubmed |
| pubmed-article:9265643 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9265643 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:9265643 | pubmed:volume | 138 | lld:pubmed |
| pubmed-article:9265643 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9265643 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9265643 | pubmed:pagination | 747-58 | lld:pubmed |
| pubmed-article:9265643 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9265643 | pubmed:meshHeading | pubmed-meshheading:9265643-... | lld:pubmed |
