Matrix (Stuttgart, Germany). Supplement最新文献

{"title":"Clostridium histolyticum collagenases: a new look at some old enzymes.","authors":"K A Mookhtiar,&nbsp;H E Van Wart","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Seven collagenases denoted by the letters alpha, beta, gamma, delta, epsilon, zeta and eta have been purified to homogeneity from the culture filtrate of Clostridium histolyticum. All seven enzymes are zinc proteinases that require calcium ions for activity and have essential carboxyl, tyrosyl and lysyl residues. These enzymes can be divided into two classes on the basis of the sequence homologies in their polypeptide chains, as revealed from a comparison of their tryptic digests. This division into classes is also supported by a comparison of their specificities toward peptide substrates, their interaction with substrate-analog inhibitors, and their mode of attack of triple helical collagens. The sequence specificities of these enzymes have been studied in detail. The specificities of the two classes are similar, but complementary. Both classes exhibit both endopeptidase and tripeptidylcarboxypeptidase activities, where the latter is thought to facilitate removal of Gly-X-Y triplets from the C-terminus of collagen fragments. The mode of attack of these collagenases on triple helical type I, II and III collagens is very similar for the enzymes within each class, but different for the two classes. The class I enzymes first hydrolyze loci near the ends of the triple helical domains of these collagen molecules, while the class II enzymes make their initial cleavages in the interior. The sites of these initial cleavages are being sequenced and preliminary results indicate that they do not resemble the tissue collagenase cleavage site with respect to either their imino acid content or distribution. The kinetic parameters for the hydrolysis of type I, II and III collagens have been measured and are similar in magnitude to those for the tissue collagenases. Synthetic peptide substrate-analog inhibitors have been prepared for both classes of collagenases and shown to be transition-state-analog inhibitors.</p>","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"116-26"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12508934","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 assay of procollagenase and collagenase inhibitors in crude biological media.","authors":"V Lefebvre,&nbsp;G Vaes","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"326-7"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649178","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":"Tissue inhibitor of metalloproteinases is induced by nerve damage.","authors":"J L Underwood,&nbsp;D A Rappolee,&nbsp;M Flannery,&nbsp;Z Werb","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"330-1"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649180","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":"Expression and function of matrix metalloproteinases in development.","authors":"Z Werb,&nbsp;C M Alexander,&nbsp;R R Adler","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Extracellular matrix (ECM) remodeling accompanies cell migration, cell-cell interactions, embryo expansion, uterine implantation and tissue invasion during mammalian embryogenesis. We have found that mouse embryos express mRNA transcripts for collagenase, stromelysin and the tissue inhibitor of metalloproteinases (TIMP) and secrete functional ECM-degrading metalloproteinases, including collagenase and stromelysin. These metalloproteinases are inhibitable by TIMP and are regulated during peri-implantation development and endoderm differentiation. The involvement of a controlled proteolytic reaction, dependent on metalloproteinases, during the implantation of mouse embryos is suggested by the secretion of proteinases by trophoblast during its invasive phase and by the reciprocal expression of TIMP in the maternal deciduum. Exogenous TIMP affects the migration of parietal endoderm cells during blastocyst outgrowth in vitro. Taken together, these data suggest that metalloproteinases function in cell-ECM interactions during mammalian development.</p>","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"337-43"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649182","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":"TIMP-2: identification and characterization of a new member of the metalloproteinase inhibitor family.","authors":"W G Stetler-Stevenson,&nbsp;H C Krutzsch,&nbsp;L A Liotta","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Human melanoma cells secrete a 21 kDa protein which binds with 1:1 molar stoichiometry to the matrix metalloproteinase type IV collagenase proenzyme (70 kDa gelatinase) secreted by the same cells. We have purified this binding protein and determined its complete primary structure by directly sequencing overlapping peptide fragments which span the entire protein. We refer to this protein as CSC-21K based on the amino-terminal amino acids CSC and the apparent molecular weight of 21,000 daltons on gel electrophoresis. The amino acid sequence of CSC-21K demonstrates that this protein shares significant homology with human TIMP (tissue inhibitor of metalloproteinase), including conservation of the positions of the twelve cysteine residues and three of four tryptophan residues. The identification of CSC-21K now indicates that a family of TIMP-related proteins exists. Individual members of this family may possess selective affinities for different members of the matrix metalloproteinase family. Based on its sequence homology to TIMP and ability to inhibit type IV collagenolysis we propose the name TIMP-2 for this inhibitor. TIMP-2 produced by tumor cells can also be considered as an onco-suppressor gene product, because it could play an important role in regulating the metalloproteinases involved in tumor invasion and angiogenesis.</p>","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"299-306"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649211","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":"Biochemical basis for multiple modes of activation of human fibroblast collagenase.","authors":"E B Springman,&nbsp;E L Angleton,&nbsp;H Birkedal-Hansen,&nbsp;H E Van Wart","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"76-7"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649576","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":"Immunolocalization of metalloproteinases in collagen autoimmune arthritis.","authors":"R A Reife,&nbsp;K A Hasty,&nbsp;C L Mainardi,&nbsp;J M Stuart","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"397"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649753","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":"Fragments of human fibroblast collagenase: purification and characterisation.","authors":"I M Clark,&nbsp;T E Cawston","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"73"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650430","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":"Expression of stromelysin and stromelysin-2 in rabbit and human fibroblasts.","authors":"C E Brinckerhoff,&nbsp;K L Sirum-Connolly,&nbsp;M J Karmilowicz,&nbsp;D T Auble","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Stromelysin and stromelysin 2, closely related members of the metalloproteinase gene family degrade many non-collagenous components of the extracellular matrix and may play a role in the activation of latent procollagenase. Because we use monolayer cultures of rabbit and human fibroblasts as model systems to study these enzymes, we compared their expression in fibroblasts from both species. Rabbit stromelysin purified from fibroblast culture medium often appears as a protein doublet, while human stromelysin is a single protein band. Hybrid selection with a cDNA clone for rabbit stromelysin and in vitro translation of mRNA from rabbit fibroblasts stimulated with phorbol myristate acetate (PMA) reveals two translation products, Mr54 and 56KD, as measured by SDS polyacrylamide gel electrophoresis. In vitro transcription and translation of a 1.8 kb cDNA for rabbit stromelysin gives a single protein product, preprostromelysin, MR 56KD. We do not yet know whether the rabbit doublet represents two distinct gene products or whether it results from posttranscriptional/posttranslational processing of a single transcript or protein. To study human stromelysin, we cloned a cDNA from a rheumatoid synovial cell cDNA library and we used it to isolate genes for stromelysin and a related gene, stromelysin-2. Both genes are contained on approximately 14 kilobase pairs of DNA. With an exon containing fragment of the human stromelysin-2 genomic clone as a specific probe in Northern blot analysis, we demonstrate the differential expression of stromelysin and stromelysin 2 in rheumatoid synovial cells, human foreskin fibroblasts, and rabbit synovial fibroblasts. Chimeric constructs containing 302 bp of the human stromelysin promoter DNA linked to the bacterial gene chloramphenicol acetyl transferase (CAT) can be induced by PMA, epidermal growth factor (EGF) and interleukin-1 beta (IL-1 beta). Since the genes for stromelysin and stromelysin 2 are so conserved and since mechanisms regulating their expression appear to be distinctive, identification of these mechanisms in both rabbits and humans will increase our understanding of the relative role of these enzymes in normal and disease processes.</p>","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"165-75"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650835","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":"A new 500-kDa form of type I procollagen N-proteinase from chick embryo tendons.","authors":"Y. Hojima, J. Mckenzie, K. Kadler, D. McBride, M. E. van der Rest, M. Mörgelin, J. Engel, D. Prockop","doi":"10.1016/s0021-9258(18)60469-7","DOIUrl":"https://doi.org/10.1016/s0021-9258(18)60469-7","url":null,"abstract":"","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 1","pages":"97-8"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/s0021-9258(18)60469-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"55519117","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}