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

---

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

The effects of total superior mesenteric and coeliac ganglionectomy on the thickness of the mucosa, the cell composition of the epithelium and the enzyme activity of the absorptive cells was studied in 10 Hanford mini pigs 3 weeks and 6 months after ganglionectomy. The mucosal thickness increased after ganglionectomy by 10-33% (P less than 0.02) mainly due to increase in the villus height. Differential cell counts showed a postganglionectomy decrease in percentage of goblet cells of 20-40%. Absorptive cell counts increased significantly (P less than 0.05). Enterochromaffin cells (stained with the Masson-Fontana method) and 5-hydroxytryptamine (5-HT)-immunoreactive cells did not change significantly in the small intestine. The activity of L-leucine-amino-peptidase, non-specific alkaline phosphatase, adenosintriphosphatase, non-specific acid phosphatase, non-specific esterase and succinate dehydrogenase, as assessed by absorption photometry, increased by 2-18% (P less than 0.01) after ganglionectomy. Total ganglionectomy thus results in a rise in villus height and in an increase in the number of absorptive cells which, by their enzymatic activity, appear to be fully mature.
...
PMID:Effects of superior mesenteric and coeliac ganglionectomy on the small intestinal mucosa in the Hanford mini pig. I. Histological and enzyme-histochemical study. 265 30

To study the origin of increased serum placental-like alkaline phosphatase (PLAP-like) activity in smokers, heat stable alkaline phosphatase activity was assayed from serum and bronchoalveolar lavage (BAL) fluid in 83 smoking and non-smoking patients. PLAP-like activity was increased in about 80% of the smokers, independently of the underlying lung disease. Isoenzyme activities in BAL fluid correlated (r = 0.631, p less than 0.001) with serum values. When adjusted for the albumin concentration, mean PLAP-like activity in BAL fluid was almost 1000-fold higher than that in serum, suggesting local synthesis of PLAP-like isoenzymes in the lungs. Although a direct dose-response effect was not observed, the values in serum and in BAL fluid tended to be higher in patients smoking over 10 cigarettes daily as compared to patients smoking less. In ex-smokers the results indicated that PLAP-like activity decreased to the level observed in non-smokers within 5 years after cessation of smoking. PLAP activity was L-leucine sensitive compatible with the Nagao-variant type of PLAP in almost all cases. In three patients the activity was due to the L-leucine resistant (true placental) isoenzyme.
...
PMID:Increased serum placental-like alkaline phosphatase activity in smokers originates from the lungs. 367 17

In order to characterize newly established human urinary bladder carcinoma cell lines (JTC-29, JTC-30, JTC-31, JTC-32, JTC-33 and JTC-34) by Kakuya et al. [In Vitro, 19, 591-599 (1983)], we investigated alkaline phosphatase in these cell lines. Relatively high alkaline phosphatase activity was found in JTC-29 and JTC-32 cells, but the enzyme activity in the other cell lines was very low. Prednisolone induced alkaline phosphatase activity even at 0.005 micrograms/ml (14 nM) and the effect was maximal at 0.05 micrograms/ml. NaCl also induced alkaline phosphatase activity at 50 mM. A further increase in the activity was observed at 0.1 M NaCl, but at 0.2 M all cells came off from plastic culture dishes without an increase in the enzyme activity during the incubation for 24 h at 37 degrees C. Both actinomycin D and cycloheximide abolished the increases in the enzyme activity with prednisolone or NaCl. The Lineweaver-Burk plot showed that the increases in the enzyme activity are due to the increases in Vmax, but not in Km. Alkaline phosphatase in JTC-32 cells and prednisolone-treated JTC-32 cells was heat stable and 100% of the initial enzyme activity remained after 30 min of incubation at 56 degrees C. However, the enzyme in JTC-29 cells was heat labile and its activity was reduced to less than 50% after 20 min of incubation at 56 degrees C. L-Phenylalanine was the strongest inhibitor for the enzyme reactions in JTC-32 cell homogenates among L-phenylalanine, L-leucine and L-homoarginine, whereas L-homoarginine was the strongest for the enzyme reactions in JTC-29 cell homogenates.(ABSTRACT TRUNCATED AT 250 WORDS)
...
PMID:Characterization of alkaline phosphatase in human urinary bladder carcinoma cell lines and enzyme regulation with prednisolone or sodium chloride. 393 23

Thermostability of the purified alkaline phosphatase derived from human uterine muscle and myoma was established before and after desialization. Both enzymes were inhibited by sucrose, glucose and maltose in proportion to the carbohydrate concentration. L-Homoarginine inhibits the myoma enzyme in 90%, L-leucine, L-histidine and L-tryptophan in about 60%, and L-phenylalanine in less than 15%. The type of inhibition and Ki values were determined. Muscle and myoma enzymes cross-reacted with antisera against human liver and placental isoenzymes. Molecular and kinetic properties of the enzyme were compared with known human isoenzymes of alkaline phosphatase.
...
PMID:Alkaline phosphatase from human uterine myoma. II. Kinetic and immunological properties. 398 59

The effects of low and high doses of 17 beta-estradiol and progesterone for 2 weeks on intestinal digestive and absorptive functions have been investigated in ovariectomized rats. The uptake of glucose was significantly enhanced following ovariectomy and administration of hormones restored the level of glucose uptake to that observed in sham-operated animals. Neither, the uptake of L-leucine nor calcium was affected after ovariectomy and treatment with the hormones. The activity of alkaline phosphatase (AP) of ileum was significantly elevated with the low and high doses of 17 beta-estradiol but in jejunum only at high doses. Progesterone alone did not alter AP activity but the combination of this hormone and 17 beta-estradiol significantly enhanced the jejunal and ileal AP activities. It seems that activity of AP is mainly under the control of 17 beta-estradiol. The activity of ileal disaccharidases and leucine aminopeptidase were enhanced at high doses of 17 beta-estradiol alone or in combination with progesterone whereas in the jejunum only AP activity was increased significantly. The present study indicates that 17 beta-estradiol plays an important role in regulating the activities of intestinal digestive enzymes and it is the ileal enzymes which are more prone to its action.
...
PMID:Effects of 17 beta-estradiol and progesterone on intestinal digestive and absorptive functions in ovariectomized rats. 401 72

The influence of two new 1-desoxynojirimycin derivatives, BAY m 1099 and BAY o 1248, on rat small intestinal disaccharidases (sucrase, maltase, isomaltase, glucoamylase, lactase, trehalase) and alkaline phosphatase activity has been investigated in vitro. Both compounds are very potent alpha-glucosidase inhibitors. Tested in the range of 0.1-5.0 micrograms/ml, inhibition is strongest on sucrase (up to 97.1%) and glucoamylase (up to 96.7%). BAY m 1099 also reduced (up to 56.4%) beta-galactosidase (lactase) activity. For both inhibitors a competitive type of sucrase inhibition was demonstrated (Lineweaver-Burk plot). Affinity versus sucrase was unusually tight. The Ki of BAY m 1099 versus sucrase amounted to 1.14 x 10(-7) M and of BAY o 1248 to 6.92 X 10(-8) M (Dixon plot). Both inhibitors did not impair active transport of L-leucine or methyl-alpha-D-glucoside into everted rings of rat jejunum in vitro.
...
PMID:Effect of 1-desoxynojirimycin derivatives on small intestinal disaccharidase activities and on active transport in vitro. 403 92

Duodena from 20-day-old chick embryos can be maintained in large scale organ culture on specially designed stainless-steel grids in contact with serum-free medium for 48 h with excellent preservation of mucosal structure at both the light and electron microscope levels. Although mitotic rate was subnormal, several other factors attest to the essential viability of the cultured intestine: L-leucine incorporation into protein, as well as the synthesis of a specific vitamin D(3)-induced calcium-binding protein (CaBP), increased over a 48-h culture period, and the electropotential gradient across the intestine was maintained throughout the culture period as was a concentration gradient for calcium. The tissue responded to vitamin D(3) in the medium by synthesizing the calcium-binding protein within 6 h and by exhibiting enhanced (45)Ca uptake within 12-24 h. Concentrations of vitamin D(3), or its 25-hydroxylated derivative, higher than necessary for CaBP induction, also increased the activity of alkaline phosphatase. The 1,25-dihydroxylated derivative of vitamin D(3), at a level extremely potent in CaBP induction, did not stimulate alkaline phosphatase. Mucosal to serosal transport of (45)Ca could also be measured in everted duodenal sacs, subsequent to culture under similar conditions, and was also increased by vitamin D(3) in the medium. Other embryonic organs, esophagus, stomach, liver, pancreas, lung, skin, and muscle, did not produce CaBP in response to vitamin D(3) in the culture medium. However, CaBP-synthesizing capacity was present in the entire intestinal tract, exclusive of the rectum. (59)Fe and (32)P uptake by cultured duodenum were also stimulated by vitamin D(3). The system has proven quite useful in the study of the vitamin D-mediated calcium absorptive mechanism but should be applicable to the study of the absorption of other nutrients, drugs, hormones, etc., as well as other studies of intestinal function.
...
PMID:Embryonic chick intestine in organ culture. A unique system for the study of the intestinal calcium absorptive mechanism. 435 39

The effects of variation in dietary protein content on small intestinal brush border and cytosol peptide hydrolase activities have been investigated. One group of rats was fed a high protein diet (55% casein) and another group was fed a low protein diet (10% casein). After 1 wk, brush border peptide hydrolase activity (L-leucyl-beta-naphthylamide as substrate) and cytosol peptide hydrolase activity (L-prolyl-L-leucine as substrate) were determined in mucosae taken from the proximal, middle, and distal small intestine. As judged by several parameters, brush border peptide hydrolase activity was significantly greater in rats fed the high protein diet when data for corresponding segments were compared. In contrast, no significant difference was seen in cytosol peptide hydrolase activity. IN A SECOND STUDY, BRUSH BORDER AND CYTOSOL PEPTIDE HYDROLASE ACTIVITIES WERE DETERMINED IN THE PROXIMAL INTESTINE BY UTILIZING AN ADDITIONAL THREE PEPTIDE SUBSTRATES: L-leucyl-L-alanine, L-phenylalanylglycine, and glycyl-L-phenylalanine. Sucrase, maltase, and alkaline phosphatase activities were also determined. As before, brush border peptide hydrolase activities were significantly greater in rats fed the high protein diet. However, activities of the nonproteolytic brush border enzymes did not vary significantly with diet. In contrast to the results obtained with L-prolyl-L-leucine as substrate for the cytosol enzymes, cytosol activity against the three additional peptide substrates was greater in rats fed the high protein diet. It is suggested that the brush border peptide hydrolase response to variation in dietary protein content represents a functional adaptation analogous to the regulation of intestinal disaccharidases by dietary carbohydrates. The implication of the differential responses of the cytosol peptide hydrolases is uncertain, since little is known of the functional role of these nonorgan-specific enzymes.
...
PMID:The responses of rat intestinal brush border and cytosol peptide hydrolase activities to variation in dietary protein content: dietary regulation of intestinal peptide hydrolases. 443 Jul 19

In model experiments using human erythrocytes, glycochenodeoxycholate caused extensive membrane damage (as judged by release of membrane phospholipid and acetylcholinesterase and by cell lysis) at approximately 10-fold lower concentrations than glycocholate. Chenodeoxycholate feeding had no effect upon the total protein, bile salt or phospholipid concentration of rat bile, although evidence is presented to suggest an expansion of the bile salt pool occurred. Rats fed chenodeoxycholate showed a dose-dependent enrichment of this bile acid in bile; this occurred mainly at the expense of cholate. Chenodeoxycholate feeding resulted in an increased biliary output of the plasma membrane enzymes alkaline phosphatase and 5'-nucleotidase; the hepatic activities of these enzymes were also increased. In contrast, the biliary output and hepatic activities of two other plasma membrane enzymes, alkaline phosphodiesterase I and L-leucine-beta-naphthylamidase, were unaffected by chenodeoxycholate feeding. A greater proportion of all four plasma membrane enzymes studied existed in bile of chenodeoxycholate-fed rats in a "soluble" form (as judged by their remaining in the supernatant on centrifugation of bile). These results are discussed in relation to the origin of plasma membrane enzymes in bile and to the potential toxicity of chenodeoxycholate and its conjugates to the membranes of the hepatobiliary system.
...
PMID:Effect of chenodeoxycholate feeding upon the biliary output of plasma membrane enzymes in the rat. 608 20

We report on a new alkaline phosphatase isoenzyme abnormality occurring as an incidental finding in a male infant aged 4 months. Isoenzyme electrophoresis on cellulose acetate showed a prominent, diffuse alkaline phosphatase staining band in the alpha 1-globulin position together with a second band in the alpha 2/beta region and minor 'trailing' in the intermediate alpha 2 region. Normal liver and bone alkaline phosphatase were absent and intestinal phosphatase was not detected. On acrylamide gel electrophoresis a marked origin band was detectable suggesting the presence of high molecular weight enzyme. In addition, a series of compact bands in the alpha 2/beta position was present cathodal to the usual liver and bone isoenzymes. Total alkaline phosphatase activity was marginally elevated and was heat labile, L-phenylalanine resistant and partially L-homoarginine and L-leucine sensitive.
...
PMID:A new alkaline phosphatase isoenzyme abnormality. 615 Jun 78


<< Previous 1 2 3 4 5 6 Next >>

---