S Zucker, U M Moll, R M Lysik, E I DiMassimo, J W Schwedes, L A Liotta
{"title":"Extraction of type IV collagenase/gelatinase from plasma membranes of human pancreatic cancer cells.","authors":"S Zucker, U M Moll, R M Lysik, E I DiMassimo, J W Schwedes, L A Liotta","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"411"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650416","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The production of collagenase and an inhibitor of collagenase by rat mammary carcinoma cells.","authors":"J M Whitelock, R L O'Grady","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"413-4"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650418","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Unique features of the tissue collagenase cleavage site in interstitial collagens.","authors":"G B Fields, H E Van Wart","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"68-70"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650428","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Limited proteolysis of types I, II and III collagens at hyper-reactive sites by Clostridium histolyticum collagenase.","authors":"M F French, A Bhown, H E Van Wart","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"134-5"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650830","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Pz-peptidase is not a matrix metalloproteinase.","authors":"A J Barrett, U Tisljar","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"95-6"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12480524","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Dissociation of tissue inhibitor of metalloproteinases (TIMP) from enzyme complexes yields fully active inhibitor.","authors":"G Murphy","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"323-4"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649176","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Secreted inhibitors of metalloproteinases (IMPs) that are distinct from TIMP.","authors":"M J Banda, E W Howard, G S Herron, G Apodaca","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The tissue inhibitor of metalloproteinases (TIMP, M(r) 30,000) is secreted by many cell and tissue types and has been shown to inhibit most secreted mammalian metalloproteinases. In matrix and tissue invasion assays, the inactivation or removal of TIMP enhances invasiveness. However, many of the cells that secrete TIMP also secrete other metalloproteinase inhibitors. By analysis of medium conditioned by various endothelial, mesenchymal, and neural cells on SDS-.substrate-polyacrylamide-inhibitor gels (reverse zymograms), we have detected at least three other distinct inhibitors of metalloproteinases (IMPs). Some or all of these IMPs have been detected in secretions of mouse, rabbit, sheep, and human cells and are all smaller in apparent molecular size than TIMP (IMP-1, M(r) 26,000; IMP-2, M(r) 21,000; IMP-3, M(r) 18,000). These IMPs are not proteolytic degradation products of TIMP nor do they represent nonglycosylated TIMP. The IMPs do not cross-react in the native or denatured state with any of several anti-TIMP antibodies. The IMPs appear to be regulated independently of each other and of TIMP. In vitro, the complex consisting of one of the IMPs, or TIMP, and a metalloproteinase can be dissociated into functional inhibitor and metalloproteinase. Whether this characteristic is significant in vivo is not known. IMP-2 has been purified from several sources and shares sequence homology with TIMP, suggesting that the IMPs and TIMP may constitute a gene family. The most significant characteristic of IMP-2 is that it appears to preferentially inhibit, on a mole:mole basis, the M(r) 68,000 gelatinase rather than collagenase or stromelysin.(ABSTRACT TRUNCATED AT 250 WORDS)</p>","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"294-8"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649210","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Structure of the human 70 K type IV collagenase gene and assignment of the gene to the q21 region of chromosome 16.","authors":"P Huhtala, L Chow, T Shows, K Tryggvason","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"84"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649579","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
J G Lyons, B Birkedal-Hansen, W G Moore, G Harber, H Birkedal-Hansen
{"title":"Mr 95,000 metalloproteinase produced by rat mammary epithelial cells.","authors":"J G Lyons, B Birkedal-Hansen, W G Moore, G Harber, H Birkedal-Hansen","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"85-6"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649581","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
H Le Moual, A Beaumont, B P Roques, P Crine, G Boileau
{"title":"Identification of two arginine residues involved in the binding of substrate to neutral endopeptidase 24-11.","authors":"H Le Moual, A Beaumont, B P Roques, P Crine, G Boileau","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"99"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649586","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}