Biomedica biochimica acta最新文献_第6页

Metalloendopeptidase activity in urine of rodents. 啮齿类动物尿液中金属内肽酶的活性。

Biomedica biochimica acta Pub Date : 1991-01-01

R J Beynon, A V Flannery, G C Macadam

引用次数: 0

A group of novel latent serine proteinases degrading myosin heavy chain in fish muscle. 一组降解鱼类肌球蛋白重链的新型潜伏丝氨酸蛋白酶。

Biomedica biochimica acta Pub Date : 1991-01-01

H Toyohara, M Kinoshita, Y Shimizu, M Sakaguchi

引用次数: 0

Biological and clinical relevance of the urokinase-type plasminogen activator (uPA) in breast cancer. 尿激酶型纤溶酶原激活剂(uPA)在乳腺癌中的生物学和临床意义。

Biomedica biochimica acta Pub Date : 1991-01-01

M Schmitt, L Goretzki, F Jänicke, J Calvete, M Eulitz, H Kobayashi, N Chucholowski, H Graeff

{"title":"Biological and clinical relevance of the urokinase-type plasminogen activator (uPA) in breast cancer.","authors":"M Schmitt, L Goretzki, F Jänicke, J Calvete, M Eulitz, H Kobayashi, N Chucholowski, H Graeff","doi":"","DOIUrl":"","url":null,"abstract":"Tumor cell invasion and metastasis is a multifactorial process, which at each step may require the action of proteolytic enzymes such as collagenases, cathepsins, plasmin, or plasminogen activators. An enzymatically inactive proenzyme form of the urokinase-type plasminogen activator (pro-uPA) is secreted by tumor cells which may be converted to an enzymatically active two-chain uPA-molecule (HMW-uPA) by plasmin-like enzymes. Action of proteases on pro-uPA may generate the enzymatically active or inactive high-molecular-weight form of uPA (HMW-uPA). Some proteases (plasmin, cathepsin B and L, kallikrein, trypsin or thermolysin) activate pro-uPA by cleaving the peptide bond Lys158 and IIe159. Other proteases (elastase, thrombin) cleave pro-uPA at different positions to yield enzymatically inactive HMW-uPA. HMW-uPA may be split into the enzymatically active LMW-uPA and the enzymatically inactive ATF (amino terminal fragment). ATF may be cleaved between peptide sequence 20 and 40 within the receptor binding domain of uPA (GFD). Such impaired ATF does not bind to uPA-receptors. Action of the bacterial endoproteinase Asp-N from Pseudomonas fragi mutant on pro-uPA or HMW-uPA, however, generates intact ATF which efficiently competes for binding of HMW-uPA or pro-uPA to receptors on tumor cells. High uPA-antigen content (pro-uPA, HMW-uPA, or LMW-uPA) in breast cancer tissue (not in plasma) indicates an elevated risk for the patient of recurrences and shorter overall survival. Thus pro-uPA/uPA-antigen content in breast cancer tissue serves as an independent prognostic parameter for the outcome of the disease. Cathepsin D is also an independent prognostic factor for recurrences and overall survival. High content of cathepsin D in breast cancer tumors is, however, not correlated with elevated levels of pro-uPA/uPA indicating that synthesis and release of cathepsin D and pro-uPA/uPA are independent events.","PeriodicalId":8948,"journal":{"name":"Biomedica biochimica acta","volume":"50 4-6","pages":"731-41"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12963389","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

Molecular diversity of erythrocyte calpastatin. 红细胞钙pastatin的分子多样性。

Biomedica biochimica acta Pub Date : 1991-01-01

E Takano, M Ueda, S Tsunekawa, T Murakami, M Maki, M Hatanaka, T Murachi

引用次数: 0

Tumor necrosis factor induction of urokinase-type plasminogen activator in human endothelial cells. 肿瘤坏死因子对人内皮细胞尿激酶型纤溶酶原激活物的诱导作用。

Biomedica biochimica acta Pub Date : 1991-01-01

M J Niedbala, M Stein

{"title":"Tumor necrosis factor induction of urokinase-type plasminogen activator in human endothelial cells.","authors":"M J Niedbala, M Stein","doi":"","DOIUrl":"","url":null,"abstract":"Vascular endothelial cells undergo morphological and functional changes at sites of cell-mediated immune responses which may serve to promote the pathogenesis of inflammation. These changes, described as \"endothelial cell activation\" can be invoked by a variety of cytokines which include interleukin I (IL-1), tumor necrosis factor (TNF), and lipopolysaccharide (LPS). We report here on the regulation of the plasminogen activator (PA) proteolytic system by human recombinant TNF alpha in short term cultures (less than 4 passages) of human umbilical vein endothelial cells (HUVECs). TNF alpha treatment of HUVECs enhanced the production of 55 kDa urokinase (u) PA activity and uPA antigen by fourfold, in a concentration dependent manner (5-100 U/ml), following a 24 h treatment as determined by PA zymography and micro-ELISA assays, respectively. This response was specific for uPA since, no change in extracellular tissue type PA activity and tPA antigen levels were noted under analogous conditions. A similar 4-fold increase in the de novo synthesis of [35S]-methionine radiolabeled uPA was observed by immunoprecipitation following a 24 h TNF treatment. The induction of uPA by TNF was inhibited by actinomycin D and cycloheximide implying the necessity of RNA and protein synthesis, respectively. The effect of TNF could not be prevented by the addition of IL-1 neutralizing antibodies. Therefore, it is unlikely that TNF acts through the induction of IL-1 secretion. Time course studies using PA zymography indicate that within 8 h after TNF exposure, a 2-fold increase in uPA activity above untreated basal levels was observed. Upregulation of extracellular uPA production in HUVECs following TNF treatment suggests yet a new aspect of cellular and interstitial PA regulation in endothelium during inflammation and angiogenesis.","PeriodicalId":8948,"journal":{"name":"Biomedica biochimica acta","volume":"50 4-6","pages":"427-36"},"PeriodicalIF":0.0,"publicationDate":"1991-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12964696","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

Proteinase-protein inhibitor interaction. 蛋白酶-蛋白抑制剂相互作用。

Biomedica biochimica acta Pub Date : 1991-01-01

W Bode, R Huber

引用次数: 0

Regulation of cystatin C activity by serine proteinases. 丝氨酸蛋白酶对胱抑素C活性的调节。

Biomedica biochimica acta Pub Date : 1991-01-01

M Abrahamson, D J Buttle, R W Mason, H Hansson, A Grubb, H Lilja, K Ohlsson

引用次数: 0

Enzymatic manipulation of protecting groups: more than deprotection. 酶对保护基团的操纵:不仅仅是去保护。

Biomedica biochimica acta Pub Date : 1991-01-01

P Hermann