Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.23.5 (cathepsin D)
 4,130 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Human renal renin (EC 3.4.99.19) and pseudorenin were easily separated in a single step by affinity chromatography on hemoglobin-Sepharose-2B. Renin and pseudorenin were monitored by their actions on crude and partially purified hog protein renin substrates at neutral and acidic pH and on synthetic labelled polymeric renin substrate. Under the conditions employed (0.1 M sodium acetate (pH 3.5)/1 M sodium chloride at 4 degrees C) renin does not bind to the affinity adsorbent while pseudorenin is effectively bound and can be eluted only after raising the pH to 6.5. Pseudorenin-free renin prepared by this method is devoid of proteolytic activity toward hemoglobin. The chromatographic behaviour of renal pseudorenin on hemoglobin-Sepharose-2B is similar to that of cathepsin D.
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PMID:Separation of human renal renin and pseudorenin by affinity chromatography on hemoglobin-Sepharose-2B. 65 43

Horse spleen cathepsin D (3.4.23.5.) was purified from crude extract by sodium chloride and ethanol precipitation, column chromatography fractionation on DEAE cellulose and CM Sephadex, re-chromatography on DEAE cellulose and gel filtration. The enzyme has been purified about 3.000 folds with a yield of 30 per cent. The purified enzyme seems to be homogeneous on Sephadex G100, one protein band is apparent on disc electrophoresis. Determined by dansylation the N-terminal amino acid is glycine. A molecular weight of 42,500 +/- 3,000 was obtained with Sephadex G100 gel filtration and light scattering measurements. Amino acid analysis and chemical determinations were performed: cathepsin D is a glycoprotein (2 or 3 osamine residues) including 344 amino acids and 4 disulfide bonds. Spectrophotometric data show that E1cm/1 mg/ml = 1.01 at lambda = 280 nm. ORD measurements indicate about 20 per cent of helicoidal content in the molecule.
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PMID:[Cathepsin D from horse spleen. I. Purification and study of certain physicochemical properties]. 97 59

Experiments were conducted on rats with massive prolonged blood loss to study the effect of immunoglobulins to lysosomal enzymes in combination with isotonic sodium chloride solution on the values of hemodynamics, oxygen regimen, and acid-base balance in the organism. Administration of antibodies to the lysosomal enzymes with an infusion medium leads to a decrease of cathepsin D activity to the initial level. Most probably, diminution of proteolysis is conducive to improvement of circulation. Inhibition of protease activity improves the permeability of vessels and thus facilitates an increase of the volume of circulating plasma, which may be judged from the authentic decrease of the hematocrit and hemoglobin. The oxygen budget and the acid-base balance in the organism are restored more fully. The use of immunoglobulins to lysosomal enzymes prolongs the animals' life.
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PMID:[Immunoglobulin antibodies to lysosomal enzymes as a means of proteolysis inhibition in severe blood loss]. 188 5

The effect of incubation temperature on the activity of cathepsin D from pig muscles was studied at different pH values. The highest activity of cathepsin D was observed at pH 3.0 and 37 degrees C. Heat stability of cathepsin D was studied when incubating muscle homogenates in a buffer pH 3.0 at 37 degrees, 50 degrees, 60 degrees and 70 degrees during 1 h containing sodium chloride or without it. When cathepsin D was incubated with sodium chloride it lost its activity independent of the temperature. Moreover, the higher the temperature of the process the greater the rate of cathepsin D inactivation.
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PMID:[Thermal inactivation kinetics of cathepsin D from porcine muscle tissue in the presence of sodium chloride]. 274 Mar 3

Renin-like activity in the heart and aorta of rats being slightly modified by binephrectomy, its variations in DOCA hypertension and infarcted ventricular muscle were studied. The daily i.p. administration of DOCA 12 mg/kg body weight for 35 days in male adult rats resulted in a significant decrease of renin activity in plasma and tissues of the heart, aorta, hypothalamus and hypophysis. In contrast to renin-like activity, cathepsin D measured in the same animals increased in all organs, except for the plasma. Similar changes of renin-like activity were observed in salt-loaded animals with 1.7% sodium chloride solution ad libitum for 35 days. In the infarcted myocardial ventricular muscle of the rats and rabbits, the tissue isorenin showed a tendency to decrease, associated with a significant increase in cathepsin D activity. Like in aorta, isorenin seems to be a different enzymatic entity of cathepsin D in the myocardial tissue. The measurement of isorenin content of the vascular endothelium and cardiac muscle fibers seems to reveal much higher amounts in the coronary vascular endothelium than in the myocardial fibres. The activation of the enzymatic angiotensin forming mechanisms in the coronary vascular bed could be one of the risk factors in myocardial infarction.
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PMID:A comparative study of the renin-like activity in the heart and vascular system under various experimental conditions. 642 49

WNK kinase is a serine/threonine kinase that plays an important role in electrolyte homeostasis. WNK4 significantly inhibits the surface expression of the sodium chloride co-transporter (NCC) by enhancing the degradation of NCC through a lysosomal pathway, but the mechanisms underlying this trafficking are unknown. Here, we investigated the effect of the lysosomal targeting receptor sortilin on NCC expression and degradation. In Cos-7 cells, we observed that the presence of WNK4 reduced the steady-state amount of NCC by approximately half. Co-transfection with truncated sortilin (a dominant negative mutant) prevented this WNK4-induced reduction in NCC. NCC immunoprecipitated with both wild-type sortilin and, to a lesser extent, truncated sortilin. Immunostaining revealed that WNK4 increased the co-localization of NCC with the lysosomal marker cathepsin D, and NCC co-localized with wild-type sortilin, truncated sortilin, and WNK4 in the perinuclear region. These findings suggest that WNK4 promotes NCC targeting to the lysosome for degradation via a mechanism involving sortilin.
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PMID:WNK4 enhances the degradation of NCC through a sortilin-mediated lysosomal pathway. 1995 8