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 ability of three diets to produce nephrocalcinosis in female rats has been compared after 30, 60 and 90 days of feeding. Severe nephrocalcinosis with associated tubular damage was induced with a standard laboratory maintenance low-protein diet and with a diet containing a single-cell protein (Pruteen) but not with a casein-containing diet. Both the Pruteen and casein diets were high-protein diets. The development of the lesion was equally rapid following feeding of either the laboratory maintenance diet or the Pruteen diet. Nephrocalcinosis was present, with body kidneys similarly affected, at each 30-day interval with either diet. A severe degree of nephrocalcinosis was associated with widespread renal damage although signs of tubular regeneration and repair were evident at 30 days. Nephrocalcinosis induced by the Pruteen diet was accompanied by enlargement of the kidney. Renal function was assessed at each time by the measurement of urine volume, specific gravity and protein content, inulin clearance, and the excretion of the urinary enzymes N-acetyl-beta-glucosaminidase and alkaline phosphatase. Despite extensive calcification and some tubular damage, renal function was unimpaired, reflecting the capacity of the functional reserve of the kidney.
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PMID:The pathogenesis and effect on renal function of nephrocalcinosis induced by different diets in female rats. 653 63

A series of marker enzymes for brush borders, basolateral membrane, and lysosomes were assayed in mucosal biopsy specimens from patients with untreated and treated coeliac disease and from controls. The brush border enzymes lactase, sucrase, neutral alpha-glucosidase, alkaline phosphatase, and leucyl-beta-naphthylamidase showed reduced activities in the untreated state and complete or partial normalization during treatment. The lysosomal marker enzyme acid phosphatase increased in activity in untreated coeliac disease and was normalized by treatment. The brush border enzyme gamma-glutamyl transferase was nearly normal in untreated patients and slightly increased in treated patients. The basolateral membrane marker, 5'-nucleotidase, was reduced both in untreated and treated patients, whereas the lysosomal marker N-acetyl-beta-glucosaminidase was normal in the untreated state and decreased during treatment. The possible pathogenetic role of the three latter enzymes in coeliac disease is discussed. The patterns of the other enzymes are suggested to be attributable to the morphologic changes in the mucosa.
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PMID:Jejunal mucosal enzymes in untreated and treated coeliac disease. 667 55

Rectal biopsy specimens from control subjects, patients with either active or quiescent ulcerative colitis, and patients with Crohn's colitis were examined histologically and assayed for marker enzymes associated with tissue organelles. They were catalase (peroxisome); neutral alpha-glucosidase (endoplasmic reticulum); alkaline phosphatase (plasma membrane); malate dehydrogenase (mitochondria); lactate dehydrogenase (cytosol). There was no significant change in these enzyme activities in patient samples compared with controls. Activities of three acid hydrolases (lysosomal enzymes), beta-glucuronidase, acid phosphatase, and N-acetyl-beta-glucosaminidase, were also assayed in the biopsy samples. Decreased activities of all three enzymes were noted in ulcerative colitis, particularly in active disease. Normal values were obtained in Crohn's colitis. Measurement of lysosomal integrity by assays of latent N-acetyl-beta-glucosaminidase activity revealed similar results in control and colitic subjects. It is suggested that the lysosomal changes reflect a specific tissue release of enzyme and may be implicated in the pathogenesis of the tissue damage.
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PMID:Organelle pathology in ulcerative and Crohn's colitis with special reference to the lysosomal alterations. 671 88

A low-speed supernatant from dog liver was prepared and subjected to analytical subcellular fractionation using either preformed Percoll or reorientating sucrose density gradient centrifugation. In Percoll the following organelles, with marker enzymes and modal densities between brackets, were characterised: plasma membrane (alkaline phosphatase, 5' nucleotidase, gamma-glutamyl transferase, 1.039); endoplasmic reticulum (neutral alpha-glucosidase, 1.039); lysosomes (N-acetyl-beta-glucosaminidase, 1.087; alpha-mannosidase, 1.081) peroxisomes (catalase, 1.045) and mitochondria (succinate dehydrogenase, 1.081). In sucrose alkaline phosphatase had a bimodal particulate distribution (1.120, 1.187) distinct from that of 5' nucleotidase (1.160) and of gamma-glutamyl transferase (1.173). Other modal densities were: endoplasmic reticulum (1.187), lysosomes (1.227, 1.200), peroxisomes (1.213) and mitochondria (1.187). Further resolution was achieved by homogenisation in digitonin which disrupted lysosomes and, in sucrose, selectively increased the densities of the plasma membrane components. Both procedures therefore achieved distinct but quite different resolutions of organelles and should prove valuable for investigating subcellular pathology.
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PMID:Evaluation of preformed Percoll and reorientating sucrose density gradient centrifugation for the analytical subcellular fractionation of dog liver. 687 78

The intestine of lambs killed immediately after birth and at intervals after the first feed was studied by electron microscope cytochemistry. Ferritin, incorporated into this feed, was found within 2 h of feeding within vesicles throughout the cytoplasm of enterocytes lining the proximal and mid-intestine. Some of these vesicles had fused with the lateral and basal membranes of the enterocytes. Histochemical reaction products for alkaline phosphatase and a series of lysosomal enzymes were localized within the vesicles; the distribution of acid hydrolases, however, was not uniform within each cell. Biochemical estimations of the activity of these enzymes showed greatest activity in the distal intestine of the newborn lamb. The activity of only one of these enzymes, N-acetyl-beta-glucosaminidase, was maximal in the mid-intestine. These observations indicate that cytoplasmic vesicles, translocating proteins across the enterocyte, probably carry intestinal alkaline phosphatase activity in their limiting membrane. Lysosomal enzymes, particularly glucosaminidase, are introduced into these vesicles as they traverse the enterocytes of the mid-intestine. A less specialized complement of lysosomal enzymes is probably introduced into vesicles in the distal intestine where ingested protein may be digested, rather than transported across the cell.
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PMID:Enzymes involved in protein transmission by the intestine of the newborn lamb. 712 59

Polymorphonuclear leukocytes were isolated from the peripheral blood of rabbits by Ficoll-Hypaque centrifugation followed by dextran sedimentation. The granulocytes were homogenized in isotonic sucrose and subjected to analytical subcellular fractionation by sucrose density gradient centrifugation. Leucine aminopeptidase, when assayed with L-leucine-7-amido-4-methyl-coumarin as substrate, showed a similar distribution to N-acetyl-beta-glucosaminidase and thus is localized to the tertiary granules. There was no leucine aminopeptidase associated with the plasma membrane of these cells. Further experiments with purified plasma membranes and inhibitor studies using diazotized sulphanilic acid further confirmed that leucine aminopeptidase had a purely intracellular localization. Vitamin B-12 binding protein showed a similar localization to alkaline phosphatase indicating that, as in human polymorphonuclear leukocytes, vitamin B-12 binding protein is located to the specific granules.
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PMID:Localization of leucine aminopeptidase and vitamin B-12 binding protein in rabbit peripheral blood polymorphonuclear leukocytes. 715 Jun 59

Lysosomes and brush border membranes from diseased ileal mucosa of a patient with Crohn's disease were separated by rate zonal density gradient centrifugation. The organelles were located and characterized in the density gradient of assay of marker enzymes, and their enzyme content compared to that of similar organelles from normal tissue. The activity and latency of lysosomal enzymes (N-acetyl-beta-glucosaminidase and acid phosphatase) was significantly increased, whereas the activity of brush border alkaline phosphatase was rather decreased. The possible relevance of these findings to the pathophysiology of Crohn's disease is discussed.
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PMID:Subcellular fractionation of human intestinal mucosa by large-scale zonal centrifugation. Characteristics of lysosomes and brush border membranes in the distal ileum of a patient with Crohn's disease. 720 80

Using a modified model of Masugi's nephritis of rats, various enzymatic activities in urine, serum and renal tissue (glomeruli or cortex) were determined at appropriate intervals after the administration of anti-kidney serum and compared with the urinary protein content and the kidney weight. In the urine, alkaline phosphatase (Al-Phosase), acid phosphatase (Ac-Phosase) and N-acetyl-beta-glucosaminidase (NA-beta-Gase) activities remarkably increased after the induction of nephritis, reached their peaks on the 10th day and reverted to almost the normal levels on the 30th day. The patterns of time course of these enzymatic activities were similar to patterns seen in the urinary protein content and the kidney weight. In the serum, the Al-Phosase activity decreased slightly, while NA-beta-Gase activity increased slightly. The Ac-Phosase activity in serum remained at normal levels during the experimental periods. In the glomeruli, the bound activities of these three enzymes decreased with nephritis, showing a negative correlation with results in the urine. On the other hand, fibrinolytic activities in the urine (plasmin-like enzyme) and renal cortex (plasminogen activator) also paralleled the urinary protein content and the kidney weight in the course of the disease. These results suggest that the Al-Phosase, Ac-Phosase and NA-beta-Gase excreted into urine in cases of nephritis may be mostly derived from damaged renal cells and one part of Al-Phosase may also come from the plasma. Moreover, the increase of plasmin-like enzyme in urine is considered to be due to the increase of plasminogen activator in the renal cortex. Thus, the determination of these enzymatic activities in the urine should be useful for evaluating effects of drugs for the treatment of nephritis.
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PMID:Pharmacological studies on experimental nephritic rats (9). Changes in activities of urinary enzymes in the modified type of Masugi's nephritis and their sources. 720 60

Anti-rat glomerular basement membrane (GBM) rabbit serum was produced by immunizing rabbits with the supernatant substance of trypsin-digested rat GBM. Nephritis was induced in rats by a single intravenous administration of 0.25 ml of anti-serum and changes in pathohistological and biochemical parameters during the process of the disease were investigated in comparison with those of Masugi nephritis and the modified type of Masugi nephritis previously reported. In light microscopic studies, histological changes seen in the kidneys closely resembled those of typical human glomerulonephritis. Changes such as hypercellularity, adhesion between capillary wall and Bowman's capsule, crescent formation and hyalinization in glomeruli and interstitial infiltration were the most pronounced on the 30th day after the anti-serum injection. In immunofluorescent studies, a linear fixation of rabbit IgG was observed along the GBM from the 1st day and the staining of a certain intensity was preserved throughout the experimental periods. A linear staining with anti-rat IgG serum was recognized from the 10th day. The fixation of fibrinogen was also seen in not only the glomerular capillary walls, but also in Bowman's space after the 10th day. Proteinuria significantly increased from the 1st day, reached a peak of 12 times the control level, and thereafter gradually decreased. The patterns of progress of urinary alkaline phosphatase and N-acetyl-beta-glucosaminidase activities were much the same as those seen in cases of proteinuria and the levels at their peak times were about 10 and 3 times control levels, respectively. Plasma urea nitrogen level transiently increased on the 5th day and then reverted to the control level by the 30th day. Plasma cholesterol levels were significantly high from the 5th to the 20th days. It is concluded that glomerular damages in this model are more severe, so-called, "nephritic type" and continue for longer periods than in cases of Masugi nephritis, however, do not differ in degree and duration from findings in the modified type of Masugi nephritis.
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PMID:[Pharmacological studies on experimental nephritic rats (11). Changes in pathohistological and biochemical parameters in anti-rat GBM rabbit serum-induced nephritis (author's transl)]. 728 45

Proximal tubules were isolated in highly pure form from rabbit cortices by a mechanical procedure that is known to preserve the structural and metabolic aspects of the tubular cells. Postnuclear supernates prepared from the isolated tubules were subjects to isopycnic centrifugation in linear sucrose gradients. The enzyme activities associated with the plasma membrane (gamma-glutamyl transpeptidase, amino-peptidase M, alkaline phosphatase, Na-K-ATPase, and phosphodiesterase I) exhibited sharp unimodal frequency-density profiles with a median density near 1.16 g/ml, which shifted to a heavier density when treated with digitonin. The lysosomal enzymes, N-acetyl-beta-glucosaminidase, alpha-mannosidase, and cathepsin B, and the peroxisomal enzyme catalase exhibited particle-associated activity near a density of 1.22 g/ml. Disruption of these particles by freezing and thawing resulted in these activities appearing in the rho = 1.10 g/ml region of the gradient where the soluble cytosolic enzyme, phosphoglucomutase, exhibited activity. Cytochrome oxidase activity typical of mitochondria gave a sharp unimodal profile at rho = 1.18 g/ml. Microsomal glucose-6-phosphatase and NADPH: cytochrome c reductase activities gave median densities near 1.16 g/ml, which did not change after incubation with digitonin. Galactosyl transferase activity gave a skewed profile at rho = 1.16 g/ml and showed a slight shift to heavier density after digitonin. This study of the enzymatic activities and density gradient distribution of the components of the proximal tubule cells provides the methodology for the further study of the cellular processing of endogenous and exogenous substances by this vital cell type.
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PMID:Analytical cell fractionation of isolated rabbit renal proximal tubules. 730 Jan 16


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