Matrix (Stuttgart, Germany). Supplement最新文献

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Localization of cleavage sites for human fibroblast collagenase in the bait region of five mammalian alpha-macroglobulins. 五种哺乳动物α -巨球蛋白诱饵区人成纤维细胞胶原酶裂解位点的定位。
L Sottrup-Jensen, H Birkedal-Hansen
{"title":"Localization of cleavage sites for human fibroblast collagenase in the bait region of five mammalian alpha-macroglobulins.","authors":"L Sottrup-Jensen,&nbsp;H Birkedal-Hansen","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The interaction between human fibroblast collagenase and five mammalian alpha-macroglobulins (human alpha 2-macroglobulin and pregnancy zone protein, rat alpha 1- and alpha 2-macroglobulin and rat alpha 1-inhibitor 3) is discussed. Complex formation involves specific limited proteolysis in the alpha-macroglobulin bait regions, activation of the internal beta-cysteinyl-gamma-glutamyl thiol esters, conformational changes and covalent complex formation. For human alpha 2-macroglobulin, and rat alpha 1-macroglobulin and alpha 2-macroglobulin it is estimated that the overall rate constant of complex formation is greater than 1.10(6) M-1s-1, while it is much lower for human pregnancy zone protein and rat alpha 1-inhibitor 3. More than 95% of the complexed collagenase is covalently bound. The identification of the sites of specific limited proteolysis in the bait regions of the five alpha-macroglobulins shows that cleavage may take place in sequences that are not related to those identified earlier in the collagens. These results greatly expand the repertoire of sequences known to be cleaved by fibroblast collagenase, and suggest that this proteinase has a primary substrate specificity resembling that of the microbial proteinase thermolysin as it preferentially cleaves at the NH2-terminal side of large hydrophobic residues. In addition, the results highlight the unique structure of the flexible alpha-macroglobulin bait region in that it can accommodate a conformation required by the highly restrictive fibroblasts collagenase. It is suggested that alpha-macroglobulins may play an important role in locally controlling the activity of collagenases and perhaps other proteinases of the extracellular matrix.</p>","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"263-8"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12456807","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}
引用次数: 0
Tetracyclines (TETs) inhibit the synthesis and/or activity of cartilage proteinases in vivo and in vitro. 四环素(TETs)在体内和体外抑制软骨蛋白酶的合成和/或活性。
C Arsenis, S A Moak, R A Greenwald
{"title":"Tetracyclines (TETs) inhibit the synthesis and/or activity of cartilage proteinases in vivo and in vitro.","authors":"C Arsenis,&nbsp;S A Moak,&nbsp;R A Greenwald","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"314"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649171","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}
引用次数: 0
A Mr 21,000 inhibitor of matrix metalloproteinases from human fibroblasts. 从人成纤维细胞提取的mr21,000基质金属蛋白酶抑制剂。
W G Moore, B Birkedal-Hansen, M Pierson, H Birkedal-Hansen
{"title":"A Mr 21,000 inhibitor of matrix metalloproteinases from human fibroblasts.","authors":"W G Moore,&nbsp;B Birkedal-Hansen,&nbsp;M Pierson,&nbsp;H Birkedal-Hansen","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"319-20"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649174","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}
引用次数: 0
Salivary gland morphogenesis: possible involvement of collagenase. 唾液腺形态发生:可能与胶原酶有关。
T Hayakawa, J Kishi, Y Nakanishi
{"title":"Salivary gland morphogenesis: possible involvement of collagenase.","authors":"T Hayakawa,&nbsp;J Kishi,&nbsp;Y Nakanishi","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>When 12-day rudiments of mouse submandibular glands were cultured, they formed an average two clefts within 24 h. The average number of the clefts, however, increased up to five in the presence of bovine tissue inhibitor of metalloproteinases (TIMP). Contrary to this, either bacterial or bovine interstitial collagenase in the medium completely inhibited the cleft formation of the glands. Electron microscopic observations revealed that the amounts of collagen bundles at the cleft points significantly increased with TIMP, but decreased with bacterial collagenase. These results strongly support the idea that endogenous collagenase regulates the cleft formation through the modulation of fibrillar architectures containing collagen in the extracellular matrix. Recently, our immunohistochemical studies clarified that collagen III, known to be rich in embryonic tissue, accumulated preferentially at the cleft points of the epithelium, and may play a crucial role in submandibular gland morphogenesis.</p>","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"344-51"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649183","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}
引用次数: 0
Cleavage of alpha 1-antitrypsin by human neutrophil collagenase. 人中性粒细胞胶原酶对α 1-抗胰蛋白酶的裂解作用。
J Michaelis, M C Vissers, C C Winterbourn
{"title":"Cleavage of alpha 1-antitrypsin by human neutrophil collagenase.","authors":"J Michaelis,&nbsp;M C Vissers,&nbsp;C C Winterbourn","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"80-1"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649577","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}
引用次数: 0
Studies on purified neutral proteoglycan-degrading enzyme (stromelysin/matrix metalloproteinase 3) from human articular cartilage. 纯化的人关节软骨中性蛋白聚糖降解酶(基质金属蛋白酶3)的研究。
Z Gunja-Smith, H Nagase, J F Woessner
{"title":"Studies on purified neutral proteoglycan-degrading enzyme (stromelysin/matrix metalloproteinase 3) from human articular cartilage.","authors":"Z Gunja-Smith,&nbsp;H Nagase,&nbsp;J F Woessner","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"82-3"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649578","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}
引用次数: 0
A new proteinase degrading type IV collagen. 一种降解IV型胶原蛋白的新蛋白酶。
Y Yamagishi, M Tsuda, T Tsuda, M Yamamura
{"title":"A new proteinase degrading type IV collagen.","authors":"Y Yamagishi,&nbsp;M Tsuda,&nbsp;T Tsuda,&nbsp;M Yamamura","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"93-4"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649584","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}
引用次数: 0
A new 500-kDa form of type I procollagen N-proteinase from chick embryo tendons. 从鸡胚肌腱中提取一种新的500 kda型I型前胶原n蛋白酶。
Y Hojima, J McKenzie, K E Kadler, D J McBride, M van der Rest, M M Mörgelin, J Engel, D J Prockop
{"title":"A new 500-kDa form of type I procollagen N-proteinase from chick embryo tendons.","authors":"Y Hojima,&nbsp;J McKenzie,&nbsp;K E Kadler,&nbsp;D J McBride,&nbsp;M van der Rest,&nbsp;M M Mörgelin,&nbsp;J Engel,&nbsp;D J Prockop","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"97-8"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649585","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}
引用次数: 0
An in vivo model of collagen degradation. 胶原蛋白降解的体内模型。
E H Karran, G P Harper
{"title":"An in vivo model of collagen degradation.","authors":"E H Karran,&nbsp;G P Harper","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"389-90"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649749","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}
引用次数: 0
Physiological mechanisms for metalloproteinase activation. 金属蛋白酶活化的生理机制。
G Murphy, R Ward, J Gavrilovic, S Atkinson
{"title":"Physiological mechanisms for metalloproteinase activation.","authors":"G Murphy,&nbsp;R Ward,&nbsp;J Gavrilovic,&nbsp;S Atkinson","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The activation of procollagenase and prostromelysin by mechanisms that might be functional in vivo has been investigated. Studies with cell monolayers plated onto collagen films have indicated key roles for plasmin and TIMP in these processes. Prostromelysin activation could be rapidly effected by fibroblast monolayers in the presence of plasminogen, with identical kinetics to plasminogen-streptokinase generated plasmin. Procollagenase activation by plasmin was shown to be poor, although an M(r) shift of 11,000 occurred. Activation was enhanced ten-fold by the presence of active stromelysin even at a very low molar ratio. A tumour cell line secreting procollagenase but not stromelysin was found to be dependent upon the addition of both stromelysin and plasminogen to effect degradation of collagen films. Biochemical studies of metalloproteinase activation were carried out using other purified proteinases synthesized by connective tissue cells including endopeptidase 24.11, endopeptidase-2, cathepsin B and cathepsin L. None was a particularly effective activator relative to plasmin, but cathepsin B was shown to activate stromelysin. By use of both cell model systems and biochemical studies of purified enzymes we have found that the role of plasmin as the major metalloproteinase activator in normal connective tissue cells remains unchallenged.</p>","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"224-30"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650045","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}
引用次数: 0
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