Matrix (Stuttgart, Germany). Supplement最新文献_第5页

Vibrio alginolyticus ("Achromobacter") collagenase: biosynthesis, function and application. 溶藻弧菌胶原酶:生物合成、功能及应用。

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

B Keil

{"title":"Vibrio alginolyticus (\"Achromobacter\") collagenase: biosynthesis, function and application.","authors":"B Keil","doi":"","DOIUrl":"","url":null,"abstract":"Bacterial collagenase from aerobic non-pathogenic Vibrio alginolyticus chemovar iophagus (\"Achromobacter\" collagenase, EC 3.4.24.08) is an inducible extracellular metallo-proteinase. Production of Vibrio collagenase is induced specifically by collagen or by its macromolecular fragments. On the cell surface is expressed a specific receptor recognizing collagen structure. The study of natural inducers led to synthetic peptides with inducing properties. Vibrio collagenase cleaves collagen helical chains preferentially at 3/4 from the N-terminal. Its specific activity on synthetic substrate, 180,000 ukat/mg, represents the highest value for known collagenases. Its specificity differs from that of Clostridium: The enzyme cleaves preferentially sequences with Gly or Ala in position P'1 and Pro in position P2 or P'2. Highly specific cleavages were obtained in beta-casein, prolactin, myosin, adenylate kinase and fibronectin. Autolysis yields partially degraded forms still active on native collagen and peptide substrate. The determination of the sequence of Vibrio collagenase is nearly achieved; the enzyme was not yet obtained in crystalline form. On basis of the already known sequence and structure of Hypoderma collagenase (EC 3.4.21.49), a hypothesis is advanced on the character of collagen binding site loops. Vibrio collagenase can be produced in kilogram quantities at low cost. It was found highly efficient in debridement of necrotic burns, ulcers and decubitus.","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"127-33"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650829","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 hemorrhagic (basement membrane degrading) zinc metalloproteinase from southern copperhead venom. 一种从南铜头蛇毒中提取的出血性(基底膜降解)锌金属蛋白酶。

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

Z Takacs, A D Retzios, F S Markland

引用次数: 0

Inhibition of human fibroblast collagenase by phthaloyl-glycylP-isoleucyl-tryptophan benzylamide (PP607). 邻苯甲酰-甘酰基-异亮氨酸-色氨酸苄胺对人成纤维细胞胶原酶的抑制作用。

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

T Y Lin, D Kuo, B Chang, L Walakovits, M W Lark

引用次数: 0

Strategies for production of inhibitory monoclonal antibodies against matrix-degrading proteinases. 抗基质降解蛋白酶抑制单克隆抗体的制备策略。

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

B Birkedal-Hansen, J G Lyons, L J Windsor, M C Pierson, W G Moore, H Birkedal-Hansen

引用次数: 0

Inhibition of human skin fibroblast collagenase by phosphorus-containing peptides. 含磷肽对人皮肤成纤维细胞胶原酶的抑制作用。

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

R E Galardy, D Grobelny, Z P Kortylewicz, L Poncz

引用次数: 0

Regulation of TIMP gene expression in cell culture and during mouse embryogenesis. 细胞培养和小鼠胚胎发生过程中TIMP基因表达的调控。

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

A M Flenniken, C E Campbell, B R Williams

引用次数: 0

Expression of TIMP in fetal and adult mouse tissues studied by in situ hybridization. 原位杂交法研究了TIMP在胎鼠和成年鼠组织中的表达。

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

D R Edwards, J K Heath, B L Hogan, S Nomura, A J Wills

引用次数: 0

Relative roles of collagenase and lysosomal cysteine-proteinases in bone resorption. 胶原酶和溶酶体半胱氨酸蛋白酶在骨吸收中的相对作用。

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

G Vaes, J M Delaissé, Y Eeckhout

{"title":"Relative roles of collagenase and lysosomal cysteine-proteinases in bone resorption.","authors":"G Vaes, J M Delaissé, Y Eeckhout","doi":"","DOIUrl":"","url":null,"abstract":"Both lysosomal cysteine-proteinases and collagenase appear to be necessary for the resorption of actively growing, immature woven bone, but their relative roles are not yet clearly elucidated. The present evidence indicates that, during bone resorption, the osteoclast first solubilizes the mineral by a secretion of acid and then removes the exposed demineralized collagen by the action of secreted lysosomal collagenolytic cysteine-proteinases. Collagenase in bone seems to be mainly a product of osteoblasts and related cells, not osteoclasts. Its role could be limited in the removal of any non-mineralized collagen layers which could be covering mineralized bone surfaces and which seem to prevent the activation of osteoclasts and thus their action; such a \"shield\" of unmineralized osteoid is well-established at the surface of actively growing woven bone, although not on the resorbing surfaces of mature lamellar bone. Moreover, some osteoblast-derived procollagenase is stored in the mineralized bone matrix from which it can be released by demineralization. It is therefore possible that it may also contribute to the degradation of demineralized bone collagen once it has been released and activated by lysosomal cysteine-proteinases under the osteoclast.","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"383-8"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649748","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

Activation mechanisms of the precursors of matrix metalloproteinases 1, 2 and 3. 基质金属蛋白酶1、2和3前体的活化机制。

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

H Nagase, K Suzuki, T Morodomi, J J Enghild, G Salvesen

{"title":"Activation mechanisms of the precursors of matrix metalloproteinases 1, 2 and 3.","authors":"H Nagase, K Suzuki, T Morodomi, J J Enghild, G Salvesen","doi":"","DOIUrl":"","url":null,"abstract":"The zymogens of matrix metalloproteinase 1 (MMP-1: tissue collagenase), MMP-2 (gelatinase/type IV collagenase) and MMP-3 (stromelysin) were purified from the culture medium of human rheumatoid synovial fibroblasts and the mechanisms of activation of each zymogen by proteinases and 4-aminophenylmercuric acetate (APMA) were studied by kinetic and sequence analyses. The treatment of proMMP-1 (M(r) = 52,000) with proteinases or APMA converted the zymogen to M(r) = 43,000, but it exhibited only 14-25% of the maximal activity. Incubation of a partially active MMP-1 with MMP-3 resulted in rapid, full activation by generating the 41,000-M(r) MMP-1 with Phe81 as the NH2-terminus. MMP-3 directly activated proMMP-1 by cleaving the Gln80-Phe81 bond, but this reaction was extremely slow, indicating that the Gln80-Phe81 bond is not readily available to MMP-3 in the native proMMP-1 molecule. ProMMP-2 (M(r) = 72,000) was activated only by APMA, but not by proteinases. The activation by APMA was rapid and generated an active MMP-2 of M(r) 68,000, but the enzymic activity declined rapidly after activation by autolysis. The NH2-terminal sequence analysis of active MMP-2 indicated that the Asn80-Tyr81 bond was cleaved upon APMA treatment. In contrast, proMMP-3 (M(r) = 57,000) was activated by a variety of proteinases with different specificities. The initial attacks of these proteinases are on a stretch of highly charged groups at the position 34-39 in the propeptide.(ABSTRACT TRUNCATED AT 250 WORDS)","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"237-44"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650047","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

Site-directed mutagenesis of type I collagen: effect on susceptibility to collagenase. I型胶原的定点突变:对胶原酶易感性的影响。

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

S M Krane, R Jaenisch

{"title":"Site-directed mutagenesis of type I collagen: effect on susceptibility to collagenase.","authors":"S M Krane, R Jaenisch","doi":"","DOIUrl":"","url":null,"abstract":"A genetic approach to define the role of collagenase in physiological and pathological bone remodeling is to identify spontaneous mutations in the collagenase gene which alter enzymatic activity. Alternatively it is possible, though site-directed mutagenesis, to alter genes encoding critical amino acid sequences in the collagen substrate, in a manner analogous to the successful development of animal models for osteogenesis imperfecta. We have thus utilized this approach to alter the Col1a1 gene to encode amino acid substitutions in sequences around the known collagenase cleavage site (glycine-isoleucine at positions 775-776) in type I collagen, and transfect these genes into homozygous Mov-13 fibroblasts, in which the endogenous Col1a1 gene is inactive. Nonconservative substitutions of proline for isoleucine at the P1' site and double substitutions of proline for glutamine (P2) and alanine (P2') resulted in type I collagen resistant to hydrolysis by collagenase. Furthermore, in normal fibroblasts transfected with a mutant Col1a1 gene encoding collagenase resistance in which an additional methionine substitution at position 776 provided a marker for the mutant protein, mutant and wild type triple helical molecules were synthesized and secreted as heterotrimers. A single mutant alpha 1(I) chain did not prevent cleavage of the wild type alpha 1(I) chain but it is likely that the uncleaved alpha 1(I) chain would prevent dissociation of the triple helical fragments containing the other cleaved chains. Introduction of these genes into transgenic mice should result in abnormal phenotypes characterized by altered connective tissue remodeling.","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"64-7"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650427","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