{"title":"Oxidant-mediated inactivation of TIMP.","authors":"G P Stricklin, J R Hoidal","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"325"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649177","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}
D T Denhardt, R Khokha, S Yagel, C M Overall, R S Parhar
{"title":"Oncogenic consequences of down-modulating TIMP expression in 3T3 cells with antisense RNA.","authors":"D T Denhardt, R Khokha, S Yagel, C M Overall, R S Parhar","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>We have used recombinant DNA technology to engineer a set of murine 3T3 cell lines that vary in the extent to which they express TIMP, tissue inhibitor of metalloproteinases, and we have found that both invasiveness and tumorigenic potential are conferred when TIMP production is impaired. These cell clones were produced by transfecting immortal Swiss 3T3 cells with plasmid constructs capable of expressing antisense TIMP RNA under the control of the mouse metallothionein promoter (Khokha & Denhardt, AntiCancer Res. 7: 653-660, 1987). The ability of these cells to invade the amnion membrane in vitro was dependent upon metalloproteinase expression (Yagel et al., JNCI 81: 768-775, 1989). Cells expressing TIMP at a reduced level acquired the ability to form tumors in nude mice (Khokha et al. SCIENCE 243: 947-950, 1989). These results suggest not only that TIMP controls the invasive character of the immortal 3T3 cell, but also that it determines cellular tumorigenic potential in the mouse. We presume that these phenotypes are conferred as a consequence of a net increase in extracellular matrix metalloproteinase activity resulting from the reduced quantities of TIMP secreted. The lag in formation of tumors by the cells down-modulated for TIMP production suggests that further changes in gene expression may be necessary. In support of this hypothesis, recent experiments indicate that the expression of genes encoding one or more matrix metalloproteinases is increased in cell lines derived from tumors that have developed from the engineered cells. Thus, in the immortal 3T3 cell line, TIMP has the properties of a tumor-suppressor gene, or anti-oncogene.</p>","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"281-5"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649208","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":"Metalloproteinases in regions of the embryonic chick tibiotarsus.","authors":"A Cole, K Kuettner, T Schmid","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"393-4"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649751","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}
T Mukaida, N Morioka, C Zhu, T A Butler, W J Lemaire, J F Woessner
{"title":"Plasmin activation of collagenase during ovulation in the perfused rat ovary.","authors":"T Mukaida, N Morioka, C Zhu, T A Butler, W J Lemaire, J F Woessner","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"402-3"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649756","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":"Synthetic triple helical models for the collagen cleavage site in interstitial collagens.","authors":"U B Goli, G B Fields, H E Van Wart","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"71-2"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650429","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}
S J Netzel-Arnett, G B Fields, H Nagase, K Suzuki, W G Moore, H Birkedal-Hansen, H E Van Wart
{"title":"Comparative sequence specificities of human fibroblast and neutrophil matrix metalloproteinases.","authors":"S J Netzel-Arnett, G B Fields, H Nagase, K Suzuki, W G Moore, H Birkedal-Hansen, H E Van Wart","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"74-5"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650431","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}
C Jonat, B Stein, H Ponta, P Herrlich, H J Rahmsdorf
{"title":"Positive and negative regulation of collagenase gene expression.","authors":"C Jonat, B Stein, H Ponta, P Herrlich, H J Rahmsdorf","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Transcription of the human collagenase I gene is induced by phorbol esters and repressed by glucocorticoids. Both types of regulation are mediated by the major enhancer element of the gene, which is localized between positions -73 and -65. The enhancer suffices to transmit positive and negative signals to a heterologous promoter or to a minimal promoter carrying only the TATA-box, both detected by the appearance of chloramphenicol-acetyl-transferase transcribed from the reporter gene linked to the promoters. Sequences 5' of the enhancer modulate its activity. Up- and down-regulation of gene constructs which contain only the collagenase enhancer linked to a heterologous promoter, are independent of ongoing protein synthesis, suggesting posttranslational modification of the transcription factor binding to the enhancer. Repression by glucocorticoids depends on an activated glucocorticoid receptor; a tenfold lower glucocorticoid concentration is needed for repression of the collagenase gene as compared to the activation of the mouse mammary tumor virus long terminal repeat. Immunoprecipitates of the dexamethasone receptor contain AP-1, suggesting a direct interaction of both transcription factors; this interaction may lead to the inactivation of AP-1. The action mechanism of phorbol esters and dexamethasone confirms the central role of AP-1 in proliferation control and tumor promotion. It appears that the most effective tumor promoter 12-O-tetradecanoyl-phorbol-13-acetate (TPA) and the most effective anti-tumor promoter dexamethasone exert their action through the modulation of the same transcription factor.</p>","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"145-55"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650834","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":"Human neutrophil collagenase.","authors":"H E Van Wart","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Human neutrophil collagenase (HNC) has been purified from extracts of fresh and outdated buffy coats and from the exudates of phorbol myristate acetate-stimulated neutrophils. The HNC present in the starting material from such preparations can be either latent or active, or have an approximate molecular weight of 75 or 58 kDa, depending upon whether the extraction buffer contains protease inhibitors and/or antioxidants. The purification of these different forms of HNC is described and is made possible by taking appropriate precautions to stabilize the HNC. For example, a purification protocol is described that allows the purification to homogeneity of the active and PCMB-active latent 58 kDa forms of HNC in high yield with specific collagenase activities that greatly exceed that of trypsin-activated human fibroblast collagenase (HFC). The pattern of activation of the latent 58 and 75 kDa species by trypsin, organomercurials and oxidants has been investigated. HNC is shown to preferentially hydrolyze type I over types II and III collagens in solution. The specificity of HNC toward the hydrolysis of 60 octapeptides has been examined and compared with HFC. HNC is shown to be a glycoprotein that contains complex N-linked oligosaccharides.</p>","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"31-6"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649168","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}
L Golub, R Greenwald, N Ramamurthy, S Zucker, L Ramsammy, T McNamara
{"title":"Tetracyclines (TCs) inhibit matrix metalloproteinases (MMPs): in vivo effects in arthritic and diabetic rats and new in vitro studies.","authors":"L Golub, R Greenwald, N Ramamurthy, S Zucker, L Ramsammy, T McNamara","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"315-6"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649172","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}