Matrix (Stuttgart, Germany). Supplement最新文献_第2页

Metal sensitive protease(s) associated with corneal proteoglycans. 与角膜蛋白聚糖相关的金属敏感蛋白酶。

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

S S Twining, P M Wilson

引用次数: 0

Primary structure and function of stromelysin/transin in cartilage matrix turnover. 软骨基质转换中基质溶解素/转蛋白的基本结构和功能。

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

S M Wilhelm, D Wunderlich, C A Maniglia, A Z Eisen, G I Goldberg

{"title":"Primary structure and function of stromelysin/transin in cartilage matrix turnover.","authors":"S M Wilhelm, D Wunderlich, C A Maniglia, A Z Eisen, G I Goldberg","doi":"","DOIUrl":"","url":null,"abstract":"Stromelysin/Transin is a member of the matrix metalloprotease gene family. This metalloprotease is synthesized as a preproenzyme with a predicted size of 53,977 Da including a 17 amino acid signal peptide. Prostromelysin is secreted from normal and transformed cells in two forms with apparent molecular masses on NaDodSO4 gels of 60 and 58-kDa. The minor 60-kDa species contains N-linked oligosaccharide(s). Stromelysin consists of three domains the amino terminal propeptide(s) domain contains the tribasic amino acid sequence RRK which is important in the proteolytic activation of this zymogen by trypsin-like serine proteases. The second domain consists of the catalytic domain which contains the zinc binding site. The carboxyl-terminal hemopexin domain has no known function and can be removed without a loss of enzymatic activity. Stromelysin has a broad range of substrate specificity including proteoglycans, casein, fibronectin, laminin, native type IV and IX collagen and gelatin but not type I collagen. In the presence of trypsin or plasmin, catalytic amounts of this enzyme can also fully activate interstitial fibroblast collagenase. We have developed a panel of monoclonal antibodies against stromelysin which will be useful for the tissue localization of the various species of this enzyme in tissues. In addition, we have demonstrated that either human rIL-1 (alpha) or rTNF (alpha) can stimulate the expression of this enzyme in cultured bovine articular cartilage at least 10-fold. Based on western blot analysis, the zymogen form of the enzyme was the major enzyme species detected in either the media or cartilage matrix compartments of cytokine treated cultures.","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"37-44"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649746","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

Ultrastructural pathway of human fibroblast collagenase and distribution in tissues of rheumatoid joint destruction. 人成纤维细胞胶原酶的超微结构途径及其在类风湿关节破坏组织中的分布。

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

A Trabandt, R E Gay, H Birkedal-Hansen, S Gay

引用次数: 0

Plasminogen activator expression and matrix degradation. 纤溶酶原激活物表达和基质降解。

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

D B Rifkin

引用次数: 0

Transcriptional regulation of matrix metalloproteinase genes: role of AP-1 sequences. 基质金属蛋白酶基因的转录调控:AP-1序列的作用。

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

D T Auble, K L Sirum-Connolly, C E Brinckerhoff

引用次数: 0

70 K type IV collagenase (gelatinase). 70k IV型胶原酶(明胶酶)。

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

K Tryggvason, P Huhtala, M Höyhtya, E Hujanen, T Hurskainen

{"title":"70 K type IV collagenase (gelatinase).","authors":"K Tryggvason, P Huhtala, M Höyhtya, E Hujanen, T Hurskainen","doi":"","DOIUrl":"","url":null,"abstract":"Type IV collagenase (gelatinase) is a 70,000 dalton neutral metalloproteinase that specifically cleaves type IV collagen in addition to degrading denatured collagen (gelatin). It is secreted in a latent proenzyme form that is converted proteolytically in the extracellular space to a 62,000 dalton active enzyme. The primary structure, enzymatic properties as well as gene structure, demonstrate that type IV collagenase is closely related with the other well characterized metalloproteinases, interstitial collagenase and stromelysin. However, the structure of type IV collagenase differs from the others in that it is larger and contains three internal repeats that resemble the type II domains of fibronectin. Also, initial characterization of the promoter region of the gene indicates that its regulation differs from the other proteinase genes. Type IV collagenase is presumably required for the normal turnover of basement membranes. Augmented activity is linked with the invasive potential of tumor cells and the enzyme is believed to play a major role in the penetration of basement membranes by metastatic cells. Measurements of enzyme activity and mRNA levels as well as immunostaining of a variety of tumor cells and tissues suggest that assays for the enzyme may have value in the follow-up of malignant growth.","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"45-50"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650423","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

Active zinc binding sites of zinc metalloenzymes. 锌金属酶的活性锌结合位点。

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

B L Vallee, D S Auld

{"title":"Active zinc binding sites of zinc metalloenzymes.","authors":"B L Vallee, D S Auld","doi":"","DOIUrl":"","url":null,"abstract":"The participation of zinc in widely diversified biological reactions focuses attention on its chemistry. A number of its properties relate to its biological utilization and versatility. Its amphoteric properties allow the zinc-coordinated water to exist as a \"hydronium\" or hydroxide ion even at neutrality. Its coordination sphere is flexible and adapts to a wide variety of ligands, allowing for a multiplicity of types and numbers of coordination complex geometries. Its stable d shell signifies that it is neither oxidized nor reduced; yet it participates in enzymatic oxidoreduction reactions in coordination with an organic cofactor. X-ray crystallographic analyses of twelve zinc enzymes now show that catalytic zinc is bound by three protein ligands, whereas structural zinc atoms are fully coordinated by four ligands. Water is always a ligand to the catalytic zinc while the protein ligands occur in an order of frequency of His >> Glu > Asp = Cys. The zinc-bound water is the critical component of the active site; it is activated for enzymatic catalysis by the identity and arrangement of the ligands coordinated to zinc. Thus, ultimately, it is this water molecule which, upon entering the zinc coordination sphere, is activated either by ionization, polarization or displacement. As a result of the properties of this metal, zinc metalloenzymes and zinc proteins participate in a wide variety of metabolic processes including carbohydrate, lipid, protein and nucleic acid synthesis, regulation and degradation.","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"5-19"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650424","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

The glycoprotein nature of human neutrophil collagenase. 人中性粒细胞胶原酶的糖蛋白性质。

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

Y Gao, K A Mookhtiar, H E Van Wart

引用次数: 0

The collagenolytic activity of Treponema denticola. 密螺旋体的溶胶原活性。

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

V J Uitto, D Grenier, Y M Pan, B McBride, T Cawston

引用次数: 0

The role of C-Fos in growth factor regulation of stromelysin/transin gene expression. C-Fos在生长因子调控基质溶解素/转蛋白基因表达中的作用。

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

L D Kerr, B E Magun, L M Matrisian

引用次数: 0