Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The release of plasma-membrane-bound enzymes by phosphatidylinositol-specific phospholipase C obtained from Bacillus thuringiensis was investigated. Among the ectoenzymes of plasma membrane tested, alkaline phosphodiesterase I was released markedly from rat kidney cortex slices, in addition to alkaline phosphatase and 5'-nucleotidase. Other membrane-bound enzymes; alanine aminopeptidase, leucine aminopeptidase, dipeptidyl peptidase, leucine aminopeptidase, dipeptidyl peptidase IV, esterase and gamma-glutamyl transpeptidase could not be liberated from the treated slices. Alkaline phosphodiesterase I was released linearly from rat kidney slices with the concentration of phosphatidylinositol-specific phospholipase C, but little enzyme was released from rat liver slices. Alkaline phosphodiesterase I separated from kidney tissue with n-butanol still retained phosphatidylinositol and was transformed into a lower molecular weight form by phosphatidylinositol-specific phospholipase C. This suggests an important function for phosphatidylinositol in the binding of alkaline phosphodiesterase I to the plasma membrane of rat kidney cells. The alkaline phosphodiesterase I released from rat kidney had a molecular weight of about 240,000 and an isoelectric point (pI) of 5.4. The enzyme hydrolyzed the phosphodiester linkage of p-nitrophenyl-thymidine 5'-monophosphate at pH 8.9 and had a Km value of 0.3 mM. The enzyme was activated by Mg2+ and Ca2+, but was inhibited by EDTA. Strong inhibition took place on the addition of adenosine 5'-phosphosulfate or the nucleotide pyrophosphates, i.e., UDP-galactose and alpha, beta-methylene ATP.
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PMID:Release of alkaline phosphodiesterase I from rat kidney plasma membrane produced by the phosphatidylinositol-specific phospholipase C of Bacillus thuringiensis. 609 28

Microscopical studies showed that initial differentiation of the guinea-pig small intestine occurs between days 35 and 55 of foetal development. Changes observed at this time include formation of villi (by day 42), elaboration of submucosal duodenal Brunner's glands (by day 49) and the appearance of a well-developed microvillus membrane (by day 56). Different microvillus membrane-associated hydrolases appear at different stages of foetal and postnatal development. The 'early' enzymes such as aminopeptidase, alkaline phosphatase and sucrase show a sharp increase and reach their maximal levels between days 35 and 50, whereas the late enzymes such as dipeptidyl peptidase IV and lactase increase gradually between days 35 and 50, and reach maximal activity between days 50 and 60. A combination of techniques involving precipitation with Mg2+ followed by fractionation on sucrose density gradients has enabled us to prepare, for the first time, a 21-fold enriched microvillus membrane fraction from the foetal intestine. Polypeptide analysis of this membrane fraction by sodium dodecyl sulphate/polyacrylamide gel electrophoresis showed the presence of developmentally specific polypeptides at different stages of foetal and postnatal development. Three polypeptides of molecular weights 205 000, 80 000 and 47 000 are major microvillus membrane components at the 40-day foetal stage. Two other polypeptides of molecular weights 60 000 and 131 000 are major microvillar components at 56-day and older foetal stages as well as at the 3-day neonatal stage. The adult microvillus membrane contained 112 000 and 122 000 Mr polypeptides as major components. The above results were confirmed using two-dimensional isoelectric focussing-sodium dodecyl sulphate/polyacrylamide gel electrophoretic techniques.
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PMID:Structural and biochemical differentiation of the mammalian small intestine during foetal development. 653 51

A microvillar fraction was prepared from human kidney cortex. This fraction was seven to 10 times enriched in aminopeptidases N and A, gamma-glutamyltransferase, dipeptidyl peptidase IV, neutral endopeptidase and alkaline phosphatase. Dipeptidyl peptidase IV activity of human renal microvilli could be inhibited by di-isopropylphosphorofluoridate and neutral endopeptidase activity by phosphoramidon. Nearly all the activity of aminopeptidases A and N could be removed from the membrane by treatment with papain, but only 19% and 33% of dipeptidyl peptidase IV and gamma-glutamyltransferase activities were released under the same conditions. Neutral endopeptidase and alkaline phosphatase were not solubilized by papain. Treatment with elastase gave results similar to papain, except that gamma-glutamyltransferase was not released. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis under reducing conditions of microvilli revealed 36 polypeptide bands, 12 of which contained carbohydrate. A band of apparent Mr 130 000 was labelled with [3H]di-isopropylphosphorofluoridate and hence identified as dipeptidyl peptidase IV. Antibodies raised to human kidney microvilli produced 11 precipitates with detergent solubilized proteins and six with papain released proteins. Several of the precipitates were identified histochemically. Microvilli prepared from human kidney are very similar to microvilli from pig and rabbit kidney with respect to enzymology, response to papain treatment, sodium dodecyl sulphate-polyacrylamide gel patterns and immunochemistry.
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PMID:Proteins of the kidney microvillar membrane; analysis by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and crossed immunoelectrophoresis. 661 1

The amount and type of dietary fibre ingested influences colonic luminal characteristics, especially the concentration of carbohydrate fermentation products such as butyrate. This study aimed to assess whether diets supplemented with fibres of differing fermentability (delivering different amounts of butyrate to the colon) influence mucosal activities of urokinase and brush border hydrolases, and epithelial turnover. Groups of five rats were fed one of four diets containing low (2%), highly fermented (guar 10% or oat bran 10%) or slowly fermented fibre (wheat bran 10%) for 4 weeks. Activities of urokinase, alkaline phosphatase, dipeptidyl peptidase IV and maltase were measured in mucosal homogenates of proximal and distal colon and from rectum. Proliferative kinetics were assessed in distal and proximal colon by the metaphase arrest technique. Hydrolase activities were similar across all four dietary groups but a significant difference was found for urokinase (P = 0.014). This was due to a reduction in urokinase activities of > 30% at the three sites in the wheat bran group compared with the other groups. Of proliferative indices, only crypt column height differed across the groups (P = 0.038) and was highest in rats fed wheat bran and lowest in those fed the low fibre diet (P = 0.047). The proportion of mitoses in the top one-fifth of the crypt also differed across groups (P = 0.038) due to the high values in the distal colon of the low fibre group. Thus, addition of a slowly fermented (but not highly fermented) fibre to the diet of rats reduces net urokinase activity in large bowel mucosa and increases the life span of colonic epithelial cells without changing activities of brush border hydrolases.
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PMID:Dietary modulation of colonic mucosal urokinase activity in rats. 754 11

A method for analysing microgram amounts of microvillar membranes by two-dimensional electrophoresis (protein mapping) is described, and has been used to characterize the microvillar proteins of the small intestine of German shepherd, corgi, and beagle dogs. Detergent-solubilized microvillar membranes were radiolabelled with 14C and separated by isoelectric focussing followed by SDS-PAGE. Proteins were detected fluorographically and glycoproteins by lectin-affinity staining. The microvillar hydrolases alkaline phosphatase and dipeptidyl aminopeptidase IV were identified by active-site labelling and aminopeptidase N by immunoprecipitation. Changes following pancreatic duct diversion were consistent with accumulation of pro-sucrase-isomaltase and diminished expression of the sucrase and isomaltase subunits. Cytoskeletal proteins were concentrated in the core fraction remaining after extraction of microvillar membranes with Triton X-100. There were no consistent differences between dogs of different breed, and the canine protein maps were similar to the human.
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PMID:Characterization of microvillar membrane proteins of dog small intestine by two-dimensional electrophoresis. 758 24

The distribution and relative catalytic activities of five plasma membrane enzymes (alkaline phosphatase, dipeptidyl peptidase IV, gamma-glutamyl transpeptidase, microsomal alanyl aminopeptidase and glutamyl aminopeptidase) were examined in human and pig oesophagus. In both species, alkaline phosphatase activity occurred in basal and suprabasal cells of the epithelium and in capillaries. Stromal cells in the human submucosa were particularly reactive. Dipeptidyl peptidase IV was present in blood vessels and capillaries in man and pig and in submucous glands in the pig. The enzyme was also present in both species in the lamina propria cells immediately adjacent to the epithelial basal lamina. In the human, gamma-glutamyl transpeptidase occurred in the epithelial basal cells and in isolated basal and lower prickle cells in the pig. Stromal cells in the human submucosa were strongly reactive and capillaries in the muscularis propria in both species moderately active. Microsomal alanyl aminopeptidase was detected in lamina propria cells adjacent to the epithelial basal cell layer in man and pig and at the apices of mucous cells in pig submucous glands. Weak glutamyl aminopeptidase activity was confined to capillaries in both species. The findings of this study, along with the ready availability of pig oesophagus, suggest that the pig may be a suitable model for studies of the gullet in man.
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PMID:A comparison of membrane enzymes of human and pig oesophagus; the pig oesophagus is a good model for studies of the gullet in man. 779 26

A number of transmembrane digestive enzymes of the porcine small intestinal brush border membrane were found to be partially Triton X-100-insoluble at 0 degree C and colocalized in gradient centrifugation experiments with the GPI-anchored alkaline phosphatase in low-density, detergent-insoluble complexes commonly known as glycolipid "rafts". Thus, aminopeptidase N (EC 3.4.11.2), aminopeptidase A (EC 3.4.11.7), dipeptidyl peptidase IV (EC 3.4.14.5), and sucrase-isomaltase (EC 3.2.1.48-10) were 34-48% detergent-insoluble. Maltase-glucoamylase (EC 3.2.1.20) was markedly less detergent-insoluble (20%), and lactase-phlorizin hydrolase (EC 3.2.1.23-62) was essentially fully soluble in detergent. In radioactively labeled, mucosal explants, the newly synthesized brush border enzymes began to associate with detergent-insoluble complexes while still in their transient, high mannose-glycosylated form, and their insolubility increased to that of the steady-state level soon after they achieved their mature, complex glycosylation, i.e., after passage through the Golgi complex. Detergent-insoluble complexes isolated by density gradient centrifugation were highly enriched in brush border enzymes, and the enrichment was apparent after only 1 h of labeling, where aminopeptidase N, sucrase-isomaltase, and alkaline phosphatase together comprised 25-30% of the total labeled, detergent-insoluble proteins, showing that sorting of newly made brush border membrane proteins into the glycolipid "rafts" does take place intracellularly. I therefore propose that, in the enterocyte, the brush border enzymes are targeted directly from the trans-Golgi network toward the apical cell surface.
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PMID:Involvement of detergent-insoluble complexes in the intracellular transport of intestinal brush border enzymes. 784 19

Epidemiological and in vivo and in vitro experimental studies have suggested that fermented milks may interfere with the emergence and/or the development of colon cancer. The results, however, remain inconclusive. This prompted us to develop a new approach based on the use of HT-29, a cultured human colon cancer cell line, to study at the cellular level the effect of fermented milks on colon cancer cell growth and differentiation characteristics. Undifferentiated HT-29 cells have been grown in the continuous presence of milks fermented by one of the following bacterial populations: Lactobacillus helveticus, Bifidobacterium, L.acidophilus or a mix of Streptococcus thermophilus and L. bulgaricus. Penicillin G was added to the cell culture medium, resulting in a complete blockade of bacterial growth without significant effect on bacterial viability. One out of the four bacteria species studied, namely L.acidophilus, was without effect on both cell growth and differentiation. The three other bacterial strains induced a significant, although variable, reduction in the growth rate of HT-29 cells, which resulted in a 10-50% decrease in the cell number at steady-state (i.e. at cell confluency). The most efficient strains in lowering the HT-29 growth rate were L. helveticus and Bifidobacterium. Concomitantly, the specific activities of dipeptidyl peptidase IV (DPP IV), a sensitive and specific marker of HT-29 cell differentiation, and that of three other brush border enzymes (sucrase, aminopeptidase N and alkaline phosphatase) were significantly increased, thus suggesting that these cells may have entered a differentiation process. Altogether, these results indicate that the use of cultured colon cancer cells may be a useful tool to further study the effect of fermented milks on colon cancer and that bacterial strains may exert a different and specific effect on cancer cell growth and differentiation when used in fermented milk products.
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PMID:Use of HT-29, a cultured human colon cancer cell line, to study the effect of fermented milks on colon cancer cell growth and differentiation. 785 55

The specific activities of aminopeptidase A (APA), aminopeptidase M (APM), and dipeptidyl-aminopeptidase IV (DP IV) were determined in isolated brain microvessels and in brain homogenate of rats with different ages (between 1 and 8 weeks old). In addition, the blood-brain barrier (BBB)-specific enzymes gamma-glutamyltranspeptidase (gamma-GT) and alkaline phosphatase (ALP) were measured. As similarly described by others, gamma-GT activity increased during this time period by fourfold, whereas ALP increased between weeks 1 and 2 and declined thereafter. DP IV activity increased fivefold during the first 8 weeks after birth and APM activity increased by twofold. A decrease of APA activity was found between weeks 1 and 2 after birth followed by an increase thereafter. The development of aminopeptidase activities responsible for the processing of specific neuropeptides acting on brain microvessels may be important in the development of regulation processes for cerebral blood flow and BBB permeability in the maturing animal.
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PMID:Developmental changes of enzymes involved in peptide degradation in isolated rat brain microvessels. 799 52

1. To evaluate tubular damage in diabetic patients, we measured the 24 h urinary excretion of five enzymes (N-acetyl-beta-D-glucosaminidase, gamma-glutamyl transpeptidase, dipeptidyl aminopeptidase IV, alanine aminopeptidase and alkaline phosphatase) that originate in renal proximal tubular cells. 2. Studies were performed on 118 non-insulin-dependent diabetic patients, 59 non-diabetic patients with chronic renal disease and 47 normal control subjects. First, the correlation between renal function, glycaemic control and urinary enzyme excretion was investigated. Secondly, the subjects were treated by controlled diet therapy to assess the effects of better glycaemic control on urinary enzyme excretion. 3. Regardless of a diabetic or non-diabetic cause of renal dysfunction, all of the five enzymes showed abnormal urinary excretion in patients with renal insufficiency (serum creatinine concentration > 2.0 mg/dl). In diabetic patients, however, an increase in N-acetyl-beta-D-glucosaminidase excretion and a decrease in gamma-glutamyl transpeptidase excretion were noted even in those who had no signs of renal dysfunction, including microalbuminuria. Moreover, the excretion of these two enzymes had a higher degree of correlation with glycaemic control and renal function than did that of the other three enzymes. Multiple regression analysis revealed that excretion of N-acetyl-beta-D-glucosaminidase is best correlated with urinary protein (r2 = 0.35), whereas excretion of gamma-glutamyl transpeptidase is closely associated with glomerular filtration rate (r2 = 0.33). 4. In diabetic patients, diet therapy improved glycaemic control but had no effects on renal function, microalbumin excretion and beta 2-microglobulin excretion.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Enzymuria in non-insulin-dependent diabetic patients: signs of tubular cell dysfunction. 809 85


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