{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T21:43:30Z","timestamp":1791495810157,"version":"4.3.4"},"reference-count":29,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2006,3,2]],"date-time":"2006-03-02T00:00:00Z","timestamp":1141257600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Experimental Dermatology"],"published-print":{"date-parts":[[2006,4]]},"abstract":"<jats:p><jats:bold>Abstract:\u2002<\/jats:bold> Extracellular matrix protein 1 (ECM1), an approximately 85\u2010kDa glycoprotein with broad tissue distribution, harbors mutations in lipoid proteinosis (LP), a heritable disease characterized by reduplication of basement membranes and hyalinization of dermis, associated with neurologic disorders. The mechanisms leading from ECM1 mutations to LP phenotype are unknown. In this study, we explored ECM1 protein\u2010protein interactions utilizing yeast two\u2010hybrid genetic screen of human placental library, which identified nine interacting proteins, including matrix metalloproteinase 9 (MMP9). The interactions were confirmed by \u03b2\u2010galactosidase assay with isolated clones and by co\u2010immunoprecipitation which narrowed the interacting segment in ECM1 to the C\u2010terminal tandem repeat 2 (amino acids 236\u2013361). This peptide segment also inhibited MMP9 activity in a gelatin\u2010based ELISA assay. We propose that ECM1\u2010mediated reduction in MMP9 proteolytic activity may have relevance to pathogenesis of LP.<\/jats:p>","DOI":"10.1111\/j.0906-6705.2006.00409.x","type":"journal-article","created":{"date-parts":[[2006,3,2]],"date-time":"2006-03-02T14:10:27Z","timestamp":1141308627000},"page":"300-307","source":"Crossref","is-referenced-by-count":94,"title":["Extracellular matrix protein 1 inhibits the activity of matrix metalloproteinase 9 through high\u2010affinity protein\/protein interactions"],"prefix":"10.1111","volume":"15","author":[{"given":"Norihiro","family":"Fujimoto","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joseph","family":"Terlizzi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sirpa","family":"Aho","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Raymond","family":"Brittingham","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrzej","family":"Fertala","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Noritaka","family":"Oyama","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John A.","family":"McGrath","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jouni","family":"Uitto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2006,3,2]]},"reference":[{"key":"e_1_2_7_2_2","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-2230.2002.01143.x"},{"key":"e_1_2_7_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.clindermatol.2004.09.006"},{"key":"e_1_2_7_4_2","first-page":"1","article-title":"Urbach\u2010Wiethe disease (lipoglycoproteinosis; lipoid proteinosis; hyalinosis cutis et mucosae). 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