Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The dorsal surface of the rabbit ear was found to be a suitable place for the production of long-lasting lymphoedema. Its major tissues (skin and sub cutaneous) are those to which secondary lymphoedema is confined in clinical situations. After 32 weeks of partial lymphatic blockade total tissue activity levels of neutral proteinase and beta-glucuronidase were depressed while alkaline phosphatase was elevated. Subsequent complete lymphatic blockade for a further 5 weeks resulted in severe fibrosis of the s.c. tissues. The total tissue activity levels of 3 characteristic lysosomal macrophage hydrolases--acid protease, beta-glucuronidase and acid phosphatase--were significantly increased. There were strong correlations between the activity levels of these enzymes and the extent of fibrosis, increased fibrosis being characterized by higher activity levels. This, together with other evidence, suggested--as fibrosis became more severe--the total number of macrophages increased, but a high proportion of these were non-stimulated. Since these cells (when stimulated) are normally responsible for the lysis of collagen and removal of fibrotic tissue the impairment of their function as occurs in chronic lymphoedema results in further fibrosis and the continuation of the vicious circle.
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PMID:Lymphoedema of the rabbit ear following partial and complete lymphatic blockade; its effects on fibrotic development, enzyme types and their activity levels. 67 48

The possible role of the eosinophil and its cytotoxic granule proteins in the vascular lesions seen in temporal arteritis was elucidated. Sixteen sections of biopsy specimens from arteria temporalis showing giant cell arteritis were stained for eosinophil cationic protein (ECP) by polyclonal antibodies and the immunoperoxidase method. Activated eosinophils were identified by monoclonal antibodies linked to alkaline phosphatase. Activated eosinophils and secreted ECP were seen in all layers of the inflamed vessels and were most evident in necrotic lesions and thrombi. Only a small number of granulocytes seen in the adventitia were immunoreactive for cathepsin G, and no extracellular deposits of this neutrophil granule protein were seen. A few immunoreactive eosinophils were found in the adventitia in two of five negative temporal artery biopsy specimens from patients with polymyalgia rheumatica. All eight coronary artery biopsy specimens with atherosclerotic lesions showed no activated eosinophils or secreted ECP. These findings indicate that eosinophils are involved in the vascular lesion in temporal arteritis and suggest that cytotoxic eosinophil granule proteins may contribute to the necrotic lesions and the development of thrombi.
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PMID:Deposition of eosinophil cationic protein in vascular lesions in temporal arteritis. 176 67

The human septal cartilage is of ectodermal origin and contributes to midfacial growth and development. Acromegaly is an endocrine disease due to growth hormone (Gh) excess originating from a somatotrophic adenoma of the pituitary gland. Excessive Gh levels lead to high insulin-like growth factor I (IGF I) concentrations, which are known to stimulate cartilage growth in vivo and in vitro. One of the salient clinical pictures is coarsening of the midface and enlargement of the septal cartilage. Septal cartilage was obtained from 8 acromegalic patients during transnasal hypophysectomy and from 10 healthy adults during septoplasty to analyse the following aspects of cartilage biochemistry, metabolism and growth. 1. Intracellular glycogen, the major source of energy of chondrocytes, was determined enzymatically and found to be drastically reduced in acromegaly. 2. Several intracellular enzymes, related to biomatrix degradation, showed a strict local pattern of distribution. Cathepsin B activity, a neutral proteinase degrading both the helical and nonhelical region of the collagen molecule was significantly increased in acromegaly, whereas alkaline phosphatase activity, an enzyme related to mineralization of the cartilage at the chondroosseous junction was depressed in acromegaly. 3. The cell density in some areas of the septal cartilage was increased in acromegaly, whereas the clonal proliferation rate of its chondrocytes in response to serum and growth factors was decreased. Chondrocytes both of healthy adults and acromegalic patients could be effectively stimulated by insulin-like growth factor I and II and to a lesser extent by epidermal growth factor.
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PMID:Human nasal septal cartilage: analysis of intracellular enzyme activities, glycogen content, cell density and clonal proliferation of septal chondrocytes of healthy adults and acromegalic patients. 252 4

Rat neutrophils added to 3H-labelled glomerular basement membrane (GBM) treated with rabbit anti-rat GBM antiserum degraded the GBM as judged by the release of 3H-labelled peptides. Cells from female animals promoted a more marked degradation than cells from males. This correlated with measurements of higher levels of elastase in granule fractions from the cells. The subcellular distributions of granule marker enzymes was found not to differ between the sexes. Levels of myeloperoxidase, lysozyme, cathepsin G, alkaline phosphatase, gamma-glutamyltranspeptidase and N-acetyl-beta-glucosaminidase showed no sex-based differences. No alpha-mannosidase could be detected in the cells.
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PMID:Biochemical studies of neutrophils from male and female rats: a differential response to basement membrane treated with nephrotoxic antiserum. 284 4

The degradation of phosphorylated and dephosphorylated neurofilament proteins by the Ca2+-activated neutral proteinase calpain was studied. Neurofilaments were isolated from bovine spinal cord, dephosphorylated by alkaline phosphatase (from Escherichia coli) and radioiodinated with [125I]-Bolton-Hunter reagent. The radioiodinated neurofilament proteins (untreated and dephosphorylated) were incubated in the presence and absence of calpain from rabbit skeletal muscle, and the degradation rates of large (NF-H), mid-sized (NF-M) and small (NF-L) neurofilament polypeptides were analysed by SDS/polyacrylamide-gel electrophoresis and autoradiography. The degradation of dephosphorylated neurofilament proteins occurred at a higher rate, and to a greater extent, than did that of the phosphorylated (untreated) neurofilament proteins. The dephosphorylated high-molecular-mass neurofilament (NF-HD) was proteolyzed 6 times more quickly than the untreated NF-H. The degradation rate of the NF-M and NF-L neurofilament proteins was also enhanced after dephosphorylation, but less than that of NF-H. This indicates that the dephosphorylation of neurofilament proteins can increase their sensitivity to calpain degradation.
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PMID:Dephosphorylation of neurofilament proteins enhances their susceptibility to degradation by calpain. 285 97

1. The control of exo-beta-N-acetylglucosaminidase (EC 3.2.1.30) production by Bacillus subtilis B growing on a chemically defined medium was studied. 2. The enzyme was repressed during exponential growth by those carbon sources that enter the glycolytic pathway above the level of phosphoenolpyruvate. When exponential growth ceased as a result of low concentrations of the nitrogen, carbon or metal ion components of the medium, the enzyme was formed and its amount could be increased by the addition of cell-wall fragments as inducer. 3. The enzyme was de-repressed and could be induced during exponential growth on non-glycolytic compounds metabolized directly into pyruvate, acetyl-CoA or tricarboxylic acid cycle intermediates. 4. The major difference in the metabolism of the organism utilizing these two groups of compound was the existence of high activities of phosphoenolpyruvate carboxylase required for gluconeogenesis. 5. It is concluded that the de-repression of glucosaminidase occurs when the only principal change detected in the intermediary metabolism of the organism was the presence of high activities of phosphoenolpyruvate carboxylase. 6. When the organism was grown on media containing repressing compounds, the enzyme was only de-repressed on entry of the cells into the initial stages of sporulation, where phosphoenolpyruvate carboxylase activity, even in the presence of excess of glucose, increased in parallel with glucosaminidase, neutral proteinase and alkaline phosphatase activities. 7. These results suggest a strong link, at the level of the tricarboxylic acid cycle, between the control of phosphoenolpyruvate carboxylase and the control of the de-repression of glucosaminidase and sporulation.
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PMID:Control of the production of exo-beta-N-acetylglucosaminidase by Bacillus subtilis B. 419 60

Casein micelles of mouse milk consist of alpha-, beta-, gamma-, and kappa-caseins. By digestion with alkaline phosphatase, they were separated as an independent band by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE). The compositions of alpha-, beta-, gamma-, and kappa-caseins were 24.3, 25.1, 9.4, and 41.2% in colostrum, and 36.8, 15.6, 11.9, and 35.7% in mature milk, respectively. Zero-day-old pups were allowed to access either colostrum or mature milk, and the aggregated milk in the stomach was analyzed by SDS-PAGE. Caseins in colostrum were digested more rapidly and efficiently than those in mature milk. Among the seven peptides present in the aggregated caseins, four peptides were colostrum-specific and derived from alpha- and gamma-caseins. It was expected that colostrum-specific and soluble peptides were generated from alpha- and gamma-caseins through gastric proteinase digestion. Amino acid sequence analysis and the pH of the aggregated milk suggested that caseins in the stomach were digested by a chymotrypsin-like proteinase. Caseins in colostrum were different from those in mature milk, with respects to the casein composition as well as the gastric proteinase sensitivity. It is concluded that the lactating mice on the day of parturition supply particular caseins to their young.
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PMID:Gastric proteinase digestion of caseins in newborn pups of the mouse. 1151 10