Matrix (Stuttgart, Germany). Supplement最新文献_第8页

Nomenclature and glossary of the matrix metalloproteinases. 基质金属蛋白酶的命名和术语。

Matrix (Stuttgart, Germany). Supplement Pub Date : 1992-01-01

H Nagase, A J Barrett, J F Woessner

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The small matrix metalloproteinase of the rat uterus. 大鼠子宫小基质金属蛋白酶。

Matrix (Stuttgart, Germany). Supplement Pub Date : 1992-01-01

J F Woessner

{"title":"The small matrix metalloproteinase of the rat uterus.","authors":"J F Woessner","doi":"","DOIUrl":"","url":null,"abstract":"The uterus of the rat contains a small metalloproteinase that digests Azocoll and proteoglycan. The activity of this enzyme is elevated in the postpartum uterus and parallels the rate of breakdown of matrix proteoglycan (Sellers, A. and Woessner, J.F., Jr., Biochem. J. 189: 521, 1980). The enzyme has been purified to homogeneity. Its molecular weight is 28,000 for the latent form of the enzyme and 19,000 for the active form, as determined by SDS/PAGE. The enzyme has no action on collagens of type I, III, IV or V, but it does digest gelatins of these 4 types. Digestion of type I gelatin is most pronounced for the alpha-2 chain, which is cleaved to two major bands. The B chain of insulin is cleaved at Ala14-Leu15 and Tyr16-Leu17. Proteoglycan is degraded, but no action can be detected against elastin. Both zinc and calcium ions are required for activity. Low levels of phosphoramidon or Zincov are not inhibitory. Detailed comparisons with human gelatinase (matrix metalloproteinase 2) and stromelysin (matrix metalloproteinase 3) show that the uterine proteinase has a distinctive pattern of specificity. The properties match those of human Pump-1 as reported by Quantin et al., Biochemistry 28: 5327, 1989. It is proposed to designate this proteinase as matrix metalloproteinase 7.","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"58-63"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650426","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}

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Inhibition of bacterial collagenase by phosphonamide peptides. 磷酰胺肽对细菌胶原酶的抑制作用。

Matrix (Stuttgart, Germany). Supplement Pub Date : 1992-01-01

V Dive, A Nikolaou, A Yioatakis, J Labadie, F Toma

引用次数: 0

Specific members of the Jun protein family regulate collagenase expression in response to various extracellular stimuli. Jun蛋白家族的特定成员在响应各种细胞外刺激时调节胶原酶的表达。

Matrix (Stuttgart, Germany). Supplement Pub Date : 1992-01-01

P Angel, M Karin

{"title":"Specific members of the Jun protein family regulate collagenase expression in response to various extracellular stimuli.","authors":"P Angel, M Karin","doi":"","DOIUrl":"","url":null,"abstract":"The transcription factor AP1 which regulates expression of collagenase in response to various extracellular signals is a multimeric complex composed of members of the Jun- and Fos families. To examine the biological role of the various components in signal transduction we analyzed the expression of two of them (cJun, JunB) and collagenase in response to phorbol esters, cAMP and TGF-beta. While all three genes are induced by phorbol ester and TGF-beta only JunB is induced by cAMP. In contrast expression of cJun and collagenase is reduced by cAMP indicating that cJun and JunB are not coordinately regulated. In addition JunB is not an efficient activator of the cJun and collagenase promoters although both cJun and JunB exhibit similar DNA binding properties, indicating that the differences in biological activity is due to differences in their activation domains. Our results imply that enhanced expression of collagenase (and cJun) depends on the activation of cJun. Expression of cJun and collagenase is inhibited under certain conditions of high levels of JunB. This suggests a negative regulatory function of JunB which greatly expands the potential of the Jun protein family in changing the transcription of specific genes involved in triggering complex biological processes.","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"156-64"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12508935","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

Mosaic structure of the secreted ECM metalloproteases and interaction of the type IV collagenases with inhibitors. 分泌的ECM金属蛋白酶的镶嵌结构和IV型胶原酶与抑制剂的相互作用。

Matrix (Stuttgart, Germany). Supplement Pub Date : 1992-01-01

G I Goldberg, I E Collier, A Z Eisen, G A Grant, B L Marmer, S M Wilhelm

{"title":"Mosaic structure of the secreted ECM metalloproteases and interaction of the type IV collagenases with inhibitors.","authors":"G I Goldberg, I E Collier, A Z Eisen, G A Grant, B L Marmer, S M Wilhelm","doi":"","DOIUrl":"","url":null,"abstract":"SV-40 transformed human lung fibroblasts and HT 1080 fibrosarcoma cells secrete a 92-kDa type IV collagenase (in addition to 72-kDa type IV collagenase identical to that found in macrophages, phorbol ester differentiated U937 cells, and keratinocytes. The expression of this protease is induced by the tumor promoter TPA, and interleukin-1 and was not detected in the parental human lung fibroblast. The 92-kDa preproenzyme has a predicted Mr of 78,426, including a 19 amino acid long hydrophobic signal peptide. The apparent discrepancy between the predicted molecular weight and the molecular weight of the secreted protein is due to a post-translational modification of the enzyme through glycosylation. The 92-kDa type IV collagenase consists of five distinct domains, including a unique 54 amino acid long collagen--like domain, and is a member of the secreted ECM metalloprotease gene family. Both the 72 and 92-kDa type IV collagenase contain a fibronectin-like collagen binding domain. The mosaic structure of the secreted ECM metalloproteases is a result of a recruitment of the functional units from ECM structural macromolecules into an enzyme protein in the process of evolution. The 92-kDa and 72-kDa type IV collagenase proenzymes form a noncovalent complex with inhibitors, which is activatable by APMA, yielding an enzymes with similar if not identical substrate specificity profile. Our results demonstrate that while the 92-kDa type IV collagenase forms a stoichiometric complex with TIMP, the 72-kDa type IV collagenase, purified from the same starting material, contains a novel 24-kDa inhibitor-TIMP-2.","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"25-30"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12508936","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

Identification of Glu 646 of neutral endopeptidase 24-11 as a zinc binding residue. 中性内肽酶24-11 Glu 646为锌结合残基的鉴定。

Matrix (Stuttgart, Germany). Supplement Pub Date : 1992-01-01

H Le Moual, P Crine, G Boileau

引用次数: 0

Design and synthesis of inhibitors of porcine synovial collagenase and gelatinase. 猪滑膜胶原酶和明胶酶抑制剂的设计与合成。

Matrix (Stuttgart, Germany). Supplement Pub Date : 1992-01-01

R D Gray, K Darlak, A F Spatola

引用次数: 0

Simultaneous production of collagenase, matrix metalloproteinase 3 (stromelysin) and tissue inhibitor of metalloproteinases by rheumatoid synovial lining cells. 类风湿性滑膜衬里细胞同时产生胶原酶、基质金属蛋白酶3(基质溶素)和金属蛋白酶组织抑制剂。

Matrix (Stuttgart, Germany). Supplement Pub Date : 1992-01-01

Y Okada, N Takeuchi, Y Gonoji, I Nakanishi, H Nagase, T Hayakawa