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

1. The total content of neutral sugars in skin of the weanling albino rats kept on the protein-deficient diet was increased by about 40%; this was mainly due to the increased concentration of galactose. The content of sialic acid was increased by about 20%. The collagen nitrogen was decreased significantly, with a concomitant increase of non-collagen nitrogen. At the same time, the content of sulphated glycosaminoglycans in skin was significantly decreased and that of non-sulphated glycosaminoglycans was increased. 2. Protein-deficient diet enhanced the activities of the protein-bound carbohydrate-degrading lysosomal hydrolases, viz. cathepsin D (EC 3.4.4.23), N-acetyl-beta-D-glucosaminidase (EC 3.2.1.30) and beta-D-glucuronidase (EC 3.2.1.31) both in liver and skin. The activity of liver hyaluronidase (EC 3.2.1.35) was also increased upon limitation of protein supply. 3. The changes observed in skin were accompanied by increased concentration of the protein-bound hexoses, hexosamines and sialic acids in serum, and of hexosamine and uronic acid in urine. The serum fucose remained unchanged.
Acta Biochim Pol 1979
PMID:Effect of protein deficiency on the metabolism of glycoproteins and glycosaminoglycans in albino rat skin. 54 53

It was found that streptozotocin-induced diabetes is accompanied by increased proteolytic activity and decreased collagen biosynthesis in rat skin wounds. External application of cathepsin D inhibitor from potatoes normalized the proteolytic activity and restored collagen biosynthesis in wounded skin of these animals.
Acta Biochim Pol 1991
PMID:Cathepsin D inhibitor from potato reverses inhibition of collagen biosynthesis in wounded skin of rats with experimental diabetes. 179 92

The influence was studied of different diets on the activity of cathepsin D (PSCatD), pepstatin (PIA) and leupeptin (LIA) insensitive acid autolytic activity (AAA), RNA, DNA and protein in skeletal leg muscle (LM) and liver of 37 mice. The diets affected the weight of the liver and content of protein in the liver and LM. The protein:DNA ratio was lowest on high carbohydrate (HC) and commercial (C) diets in both tissues and about 3 times higher in LM than in the liver. The RNA:protein ratio was highest in the high protein-fat (HPF) and recommended (R) diet fed groups. The RNA:DNA ratio was lowest on HC and C diets. In the liver, PSCatD, AAA, LIA were lowest on HPF, and highest on HC diets, but for PIA on high fat-protein (HFP) and C diets, respectively. The highest activities were correlated with the lowest percentage of protein and fat in the diets (low energy diets). For LM, the highest activities were found on a C diet and lowest for PSCatD on HEP but for AAA, PIA, LIA on HC diets. Cathepsin D accounted for about 70% of hemoglobin degradation in the liver and 66% in LM. In AAA, cathepsin D participates in 58.5% and 50.5% in the liver and LM inhibition, respectively, but leupeptin accounted for about 15% and 27% (in the presence of Mg++) of inhibition.
Acta Physiol Pol
PMID:Changes in cathepsin D, acid autolytic activity, RNA, DNA in skeletal muscle and liver of mouse kept on high protein, carbohydrate and lipid diets. 248 68

The effects of acute exhaustive exercise, training and hypokinesia on cathepsin D activity were studied in the superficial ("white") layer of the vastus lateralis, in the deepest ("red") layer of the same muscle, in the soleus, in the heart muscle and in the liver of rats. In was found that acute exercise increased the enzyme activity in both portions of the quadriceps and in the liver. Training increased cathepsin D activity in the "red" quadriceps and in the soleus. In hypokinetic rats cathepsin D activity was markedly increased in each muscle investigated.
Acta Physiol Pol
PMID:Effect of motor activity on cathepsin D activity in rat muscles. 718 51

Cathepsin D expression was determined by immunohistochemistry in 445 formalin fixed, paraffin embedded primary invasive breast carcinomas. We found: 1. a relationship between cathepsin D expression and histological type of tumour, 2. a negative correlation between cathepsin D expression and histological grade, 3. a negative correlation between cathepsin D expression and tumour diameter, 4. a relationship between the morphology of cathepsin D granules and histological type of the tumour.
Pol J Pathol 1995
PMID:Cathepsin D in invasive ductal NOS, medullary, lobular and mucinous breast carcinoma. An immunohistochemical study. 778 Jun 91

Intoxication of rats with methanol (1.5 and 3.0 g/kg body weight) led to a significant, time- and dose-dependent decrease in the activities of cathepsins A, B and C, while the activity of cathepsin D was unaffected. The decrease was associated with a different partial release of individual cathepsins to the post-lysosomal fraction.
Acta Biochim Pol 1997
PMID:Activity of liver proteases in experimental methanol intoxication. 936 Jul 24

In the present paper we analyzed cathepsin D activity in digestive tract cancers. Cathepsin D activity was estimated in 10% homogenates of oesophageal cancer, gastric cancer and colon cancer tissues and in the blood serum and expressed as the amount of liberated tyrosine which was assayed acc. to Folin-Ciocalteau. Mean cathepsin D activities in neoplastic tissues and normal counterparts were as follows: oesophaged cancer (218.5 mM Tyr/1/2 h vs 145.0 mM Tyr/1/2 h), gastric cancer (285.4 mM Tyr/1/2 h vs 142.3 mM Tyr/1/2 h) and colon cancer (233.7 mM Tyr/1/2 h vs 159.5 mM Tyr/1/2 h). In all examined neoplastic tissues cathepsin D activity was almost too-fold higher than in the normal counterparts. Cathepsin D activity in the sera of cancer patients was too a lesser degree higher than in the sera of normal subjects. The data indicate that estimating of cathepsin D activity in the neoplastic tissues homogenates and in the blood serum may be of diagnostic value and may constitute an information which is complementary to the analysis of other tumor markers and histopathologic examination.
Pol Merkur Lekarski 1997 May
PMID:[Activity of cathepsin D in some neoplasms of the gastrointestinal tract]. 937 76

The presence of cathepsin D was assessed in epithelial and stromal cells of the gastric mucosa in patients with ulcer disease depending on the course of ulcer healing, accompanying Helicobacter pylori infection, mode of treatment, location of ulceration, the presence of relapses, intestinal metaplasia, ulcer diameter, age and gender of the patients. The presence of cathepsin D was assessed by immunohistochemistry using an immunoenzymatic method StreptABC. Immunohistochemistry was performed on formalin-fixed paraffin sections obtained from 54 selected patients (20 men and 34 women, aged from 23 to 75 years), in whom endoscopy of the upper alimentary tract revealed ulcerations within the stomach, and then ulcer healing was monitored by endoscopy and histopathology. Before immunohistochemistry each specimen was routinely stained with hematoxylin and eosin, and histopathological study was performed to confirm a nonneoplastic character of ulcers, followed by staining with Giemsa method for the presence of Helicobacter pylori. The presence of cathepsin D was analyzed using image analysis. Student's t-test and a correlation coefficient were used to study the relationship between the expression of cathepsin D and selected parameters. The following significant relationships were observed: 1. between the expression of cathepsin D in epithelial cells and the course of peptic ulcer healing after antiulcerative treatment; 2. between the expression of cathepsin D in stromal cells after antiulcerative treatment and the course of ulcer healing.
Pol J Pathol 1998
PMID:Immunocytochemical evaluation of gastric mucosal cathepsin D in peptic ulcer. 979 10

EPH-gestosis is accompanied by an extensive remodelling of the extracellular matrix of the umbilical cord arteries, vein and Wharton's jelly. For better understanding of processes proceeding in it we decided to determine proteolytic activity in acidic pH range. Presented results suggest that cathepsin D is one of the main proteolytic enzymes of umbilical cord.
Ginekol Pol 2000 Aug
PMID:[Selected aspects of proteolytic activity of umbilical cord and its alterations in EPH-gestosis]. 1108 20

Effect of three epsilon-aminocaproylaminoacids with significant antifibrinolytic activity on chymotrypsin, trypsin, cathepsin B, cathepsin C and cathepsin D activities was examined. Slight inhibition of trypsin and chymotrypsin activity was observed only at high concentrations of these compounds. All tested dipeptides did not influence activities of cathepsin B, cathepsin C and cathepsin D.
Acta Pol Pharm
PMID:Effect of epsilon-aminocaproylaminoacids on the activity of proteolytic enzymes. 1150 92


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