Matrix (Stuttgart, Germany). Supplement最新文献_第7页

The effect of a synthetic metalloproteinase inhibitor on corneal ulceration in alkali burns and pseudomonas keratitis. 合成金属蛋白酶抑制剂对碱烧伤和假单胞菌性角膜炎角膜溃疡的影响。

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

F R Burns, R D Gray, J T Wells, C A Paterson

引用次数: 0

A bovine hyaline cartilage proteinase inhibitor is active against some serine proteinases and inhibits the IL-1 alpha-mediated matrix degradation of bovine articular cartilage explants. 牛透明软骨蛋白酶抑制剂对某些丝氨酸蛋白酶具有抑制IL-1 α介导的牛关节软骨外植体基质降解的活性。

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

C Arsenis

引用次数: 0

Significance of tissue inhibitor of metalloproteinases (TIMP) in synovial fluid of rheumatoid arthritis. 类风湿性关节炎滑液中金属蛋白酶组织抑制剂(TIMP)的意义。

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

K Iwata, K Yamashita, S Kodama, H Iwata, T Hayakawa

引用次数: 0

Structure and function of murine TIMP gene. 小鼠TIMP基因的结构与功能。

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

B Coulombe, A Ponton, R S Kerbel, D Skup

{"title":"Structure and function of murine TIMP gene.","authors":"B Coulombe, A Ponton, R S Kerbel, D Skup","doi":"","DOIUrl":"","url":null,"abstract":"Specific inhibitors of metalloproteinases, such as TIMP, are potential regulators of tissue integrity. In order to understand their exact role in both normal and pathological processes we have initiated molecular studies on the TIMP gene and its product(s). We have used cDNA and genomic clones corresponding to the murine TIMP gene to define the intron-exon structure of the gene and to map multiple clustered sites where transcription is initiated; we have also partially characterized the cis-acting DNA sequences required for transcriptional activity. The murine TIMP cDNA has also been used in transcription/translation experiments to produce polypeptides which can be processed by endoplasmic reticulum membranes and which are biochemically active in inhibition of fibroblast interstitial collagenase. As a result of our analysis of the expression of the TIMP gene in different cell types and under varied conditions, we have observed an important increase of TIMP mRNA levels in mouse fibroblasts in response to physiological modulators (whole serum and double-stranded RNA) as well as a pathogen (NewCastle Disease Virus). In addition, an analysis of TIMP mRNA in several variants of a cell line derived from a spontaneous mammary adenocarcinoma, which possess different levels of metastatic potential indicated that the serum dependence of TIMP mRNA accumulation is different in metastatic as compared to nonmetastatic cells. The significance of these results in view of the role of TIMP in matrix maintenance is discussed.","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"269-74"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649206","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

Fluorogenic peptide substrates optimized for five human matrix metalloproteinases. 五种人基质金属蛋白酶的荧光肽底物优化。

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

E L Angleton, H Nagase, H Birkedal-Hansen, H E Van Wart

引用次数: 0

Neutral proteinase expression by human mononuclear phagocytes: a prominent role of cellular differentiation. 中性蛋白酶在人单核吞噬细胞中的表达:在细胞分化中的重要作用。

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

H G Welgus, R M Senior, W C Parks, A J Kahn, T J Ley, S D Shapiro, E J Campbell

{"title":"Neutral proteinase expression by human mononuclear phagocytes: a prominent role of cellular differentiation.","authors":"H G Welgus, R M Senior, W C Parks, A J Kahn, T J Ley, S D Shapiro, E J Campbell","doi":"","DOIUrl":"","url":null,"abstract":"Human mononuclear phagocytes have the capacity to participate directly in extracellular matrix turnover via the secretion of neutral proteinases. These neutral proteinases include the serine proteinases, elastase and cathepsin G and the metalloproteinases, interstitial collagenase, 92 kD type IV collagenase, 72 kD type IV collagenase and stromelysin. Mononuclear phagocytes also produce the counter-regulatory metalloproteinase inhibitor, TIMP (tissue inhibitor of metalloproteinases). We have studied the capacity of normal human mononuclear phagocytes and of the human monocytic tumor line U937 to elaborate proteinases and inhibitors. The serine proteinases, elastase and cathepsin G, are present only at the earliest stages of mononuclear phagocyte differentiation (U937 cells in the basal state, freshly isolated peripheral blood monocytes) and are stored within intracellular granules. As human mononuclear phagocytes differentiate (U937 cells exposed to phorbol esters, human monocytes cultured in vitro), the cellular content of these serine proteinases declines rapidly. Accompanying the acquisition of a more differentiated state, the ability for regulated secretion of the neutral metalloproteinases is attained. This capacity is acquired in a sequential manner, with secretion of the 92 kD type IV collagenase observed at earlier states of differentiation while release of stromelysin requires a fully differentiated and LPS (lipopolysaccharide)-stimulated alveolar macrophage. Interstitial collagenase and 72 kD type IV collagenase are synthesized at intermediate stages of differentiation. In comparison to human fibroblasts, human mononuclear phagocytes produce approximately 10-30% of the interstitial collagenase, 10% of the stromelysin and 1-2% of the 72 kD type IV collagenase on a per cell basis. Synthesis of the 92 kD type IV collagenase is restricted to the inflammatory cell (but also occurs in neutrophils and keratinocytes).","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"363-7"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12649744","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

Proteases in seminiferous epithelium remodeling. 精原上皮重构中的蛋白酶。

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

Q X Sang, M Dym, S W Byers

引用次数: 0

Activation of extracellular matrix metalloproteases by proteases and organomercurials. 蛋白酶和有机聚合物对细胞外基质金属蛋白酶的激活。

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

G A Grant, G I Goldberg, S M Wilhelm, C He, A Z Eisen

{"title":"Activation of extracellular matrix metalloproteases by proteases and organomercurials.","authors":"G A Grant, G I Goldberg, S M Wilhelm, C He, A Z Eisen","doi":"","DOIUrl":"","url":null,"abstract":"Extracellular matrix metalloproteases are synthesized as proenzymes and are activated by certain physiological agents after secretion into the extracellular space. The identity of these agents and the stimulus that elicits their response in vivo is only recently becoming clear, but a variety of agents or stimuli are capable of activating these metalloproteases in vitro also. Of these, the most well studied and characterized are trypsin, plasmin and the organomercurials. These agents appear to have in common an ability to disrupt the structure of the stable latent enzyme in such a way as to allow the generation of a proteolytic active site. In the case of organomercurial activation, intramolecular proteolytic cleavage of the amino-terminus of the enzyme occurs subsequent to generation of activity. A similar intramolecular process is seen with trypsin and plasmin activation except that it is initiated by a single trypsin or plasmin catalyzed cleavage in the amino-terminus prior to the autocatalytic cleavages. A possible explanation for organomercurial activation is that the mercurial disrupts a cysteinyl residue coordination bond with the active site zinc that prevents interaction with substrate. Disruption of this complex would allow productive enzyme-substrate interaction via the newly available coordination site. In addition, activated stromelysin is capable of increasing the specific activity of active interstitial collagenase by approximately ten-fold through what appears to be proteolytic removal of a small peptide.","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"217-23"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650044","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 latency of the human fibroblast collagenase precursor depends on an internal cysteine residue. 人成纤维细胞胶原酶前体的潜伏期取决于内部的半胱氨酸残基。

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

J A Engler, L J Windsor, B Birkedal-Hansen, H Birkedal-Hansen

引用次数: 0

Latent collagenase and gelatinase from human neutrophils and their activation. 人中性粒细胞中潜伏的胶原酶和明胶酶及其活化。

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

H Tschesche, V Knäuper, S Krämer, J Michaelis, R Oberhoff, H Reinke

{"title":"Latent collagenase and gelatinase from human neutrophils and their activation.","authors":"H Tschesche, V Knäuper, S Krämer, J Michaelis, R Oberhoff, H Reinke","doi":"","DOIUrl":"","url":null,"abstract":"Procollagenase M(r) 85,000 (SDS-PAGE) was purified from buffy coat to homogeneity and represents a stable single polypeptide chain forming the entire proenzyme. The procollagenase can be activated by various proteinases, e.g. trypsin, chymotrypsin, cathepsin G, kallikrein and stromelysin and by different mercurial compounds. Proteolytic conversion of the latent enzyme to the active form by chymotrypsin is accompanied by a molecular weight reduction to an apparent M(r) 64,000. This active enzyme lacks the first 79 N-terminal residues. Activation by trypsin leads to a latent intermediate of apparent M(r) 70,000, lacking 48 N-terminal residues. The active enzyme is therefore generated upon prolonged incubation with trypsin by further cleavage of 22 N-terminal residues. Another latent intermediate form with apparent M(r) 69,000 is generated from the proenzyme upon incubation with leukocyte elastase by N-terminal cleavage of 53 or 64 residues, respectively. However, latent collagenase cannot be activated by plasmin. Activation by different mercurial compounds finally results in the formation of active collagenase with apparent M(r) 64,000. In contrast to the proenzyme, active collagenase can autolyse to give active M(r) 57,000 and 45,000 intermediates and two M(r) 28,000 fragments. Purification of latent leukocyte gelatinase yields three final products with apparent M(r) 98,000, 125,000 and 220,000 (SDS-PAGE; non reduced). Upon reduction, only the M(r) 98,000 form can be detected. The latent gelatinase can be activated in a similar manner as collagenase. Proteolytic activation by trypsin leads after N-terminal cleavage to an active gelatinase with sequence homology to leukocyte collagenase.","PeriodicalId":77254,"journal":{"name":"Matrix (Stuttgart, Germany). Supplement","volume":"1 ","pages":"245-55"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12650048","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