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Proteases during the growth of Ehrlich ascites tumor. II. The kallikrein-kinin system.
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Ascitic fluid and ascites tumor cells from Swiss mice bearing Ehrlich ascites tumor were assayed for components of the kallikrein-kinin system at various times during tumor growth. Changes in component levels were correlated with those in the plasma. Ascitic fluid contained an acetone-activated
Effect of the serine protease inhibitor, aprotinin, on systemic haemodynamics and renal function in patients with hepatic cirrhosis and ascites.
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1. Previous studies have documented activation of protease enzymes, such as the plasma kallikrein-kinin system, in hepatic cirrhosis. Increased plasma kinin generation could contribute to pathological systemic vasodilatation in cirrhosis, and reduced systemic vascular resistance has been suggested
Proteases and antiproteases related to the coagulation system in plasma and ascites. Prediction of coagulation disorder in ascites retransfusion.
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To improve the ability to predict the occurrence of coagulation disorders in ascites retransfusion and, in addition, to better define the nature of the coagulation disorder, several proteases and antiproteases were analyzed in ascites and plasma before ascites retransfusion in 17 patients.
Identification and characterization of a Kunitz-type protease inhibitor in ascites fluid from patients with ovarian carcinoma.
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Urinary trypsin inhibitor (UTI; Mr 40 kDa) is a Kunitz-type protease inhibitor that efficiently inhibits cell-associated trypsin and plasmin activities. The aim of this study is to examine the expression pattern of UTI in the human ovarian carcinoma ascites fluid by Western blotting, zymography,
Inhibition properties of Sepharose-bound trypsin and a protease on the surface of Ehrlich ascites tumour cells.
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Ehrlich ascites cells have been shown to possess a protease with beta-naphthylamidase activity located on the surface of these cells. This enzyme is protected from the inhibitory action of protein inhibitors of trypsin (EC 3.4.21.4) in free solution, but is inhibited by high concentrations of active
Serine protease-induced enhancement of blood-borne metastasis of rat ascites tumour cells and its prevention with deoxyribonuclease.
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Serine proteases, such as alpha-chymotrypsin or elastase, caused an aggregation of rat ascites tumour cell lines, AH-130, AH-109A and YS, in a protein free medium which preserved the cell viability. This aggregation, which was monitored spectrophotometrically, was dependent upon the protease
A trypsin-like neutral protease on Ehrlich ascites cell surfaces: its role in the activation of tumour-cell zymogen of collagenase.
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Ehrlich ascites cells in mice have been shown to have a cell-surface trypsin-like neutral protease (TLNP) with proteolytic and beta-naphthylamidase activity. This activity is inhibited by low-mol.-wt inhibitors of trypsin but not by 11 high-mol.-wt inhibitors of trypsin in free solution. We believe
Inhibition of cell-surface neutral protease of Ehrlich ascites tumor cells by potassium p-(3,3-dimethyl-1-triazeno) benzoate.
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Ehrlich ascites tumour (EAT) cells possess a trypsin-like neutral protease on the cell surface. The antimetastatic triazene drug potassium p-(3,3-dimethyl-1-triazeno) benzoate (DM-COOK) inhibits this neutral protease, and also trypsin. Incubation of EAT cells with human erythrocytes (ratio of 1 to
Crystal structures of yellowtail ascites virus VP4 protease: trapping an internal cleavage site trans acyl-enzyme complex in a native Ser/Lys dyad active site.
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Yellowtail ascites virus (YAV) is an aquabirnavirus that causes ascites in yellowtail, a fish often used in sushi. Segment A of the YAV genome codes for a polyprotein (pVP2-VP4-VP3), where processing by its own VP4 protease yields the capsid protein precursor pVP2, the ribonucleoprotein-forming VP3,
Proteases and antiproteases related to the coagulation system in plasma and ascites--influence of dexamethasone.
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Fibrinolysis induced by the infusion of plasminogen activators into the circulation has been shown to cause coagulation disorders in ascites retransfusion. Dexamethasone is known to inhibit the synthesis of plasminogen activators by peritoneal macrophages. We therefore assessed its potential in
Proteases and antiproteases related to the coagulation system in plasma and ascites--an approach to differentiate between malignant and cirrhotic ascites.
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The concentrations of several proteases and antiproteases known to be present in ascites were tested in plasma and ascitic fluid with regard to their ability to separate ascites according to malignant or nonmalignant disease. Seventeen patients with proven malignant ascites and 37 with ascites due
Acid stable protease inhibitor in ascites of ovarian carcinoma.
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In patients with ovarian tumors, a novel protease inhibitor which is very stable in acid (AS-PI, acid stable protease inhibitor) was identified in the ascites and tumor fluid as well as in the urine and plasma. The highest AS-PI activity was observed in the tumor fluid of ovarian carcinomas (10.7
[Studies on fibrinolysis and ascites accumulation associated with peritonitis carcinomatosa--effects of protease inhibitors (PI) on MM2 ascites tumor growth, ascites accumulation and fibrinolysis].
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The effects of protease inhibitors(PI), t-AMCHA, gabexate, aprotinin and heparin on the growth of mouse MM2 ascites tumor (MAT) and on several components of fibrinolysis were studied. The drugs were administered intraperitoneally one time daily for 12 days, one day after the tumor transplant. The
Properties of Ca2+-activated protease specific for the intermediate-sized filament protein vimentin in Ehrlich-ascites-tumour cells.
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A Ca2+-activated neutral protease is described which, when tested against various native proteins, appears to be specific for vimentin, the 58,000-Mr subunit protein of intermediate-sized (7--11 nm) filaments in Ehrlich-ascites-tumour cells. The protein subunits of other classes of
Effect of a protease inhibitor on the adhesion of Ehrlich ascites cells to host cells in vivo.
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Ehrlich ascites tumours (EAT) were grown in mice by injecting 1 × 10(6) cells intraperitoneally. In mice which received one or more injections of 30 mg soybean trypsin inhibitor (TI) i.p. during tumour growth, the number of recoverable tumour cells was significantly reduced by up to 92%. Also, the
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