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 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

To examine the effect of bile acids on the activity of intestinal aminopeptidase in vivo, we measured the activity of aminopeptidase in the intestinal mucosa from rats fed the diet containing cholestyramine which sequesters luminal bile acids (experiment 1) and from bile diverted rats (experiment 2). After 32 h fasting, rats were refed for 16 h either of a standard diet (25% casein diets), the same diet containing cholestyramine, or the fat-free diet in experiment 1. In the intestinal washing, the content of total bile acids was markedly decreased with feeding cholestyramine and activities of trypsin and chymotrypsin were also lowered with cholestyramine. Cholestyramine feeding decreased the specific activity of aminopeptidase in the homogenate of intestinal mucosa but increased the specific activities of sucrase and alkaline phosphatase. All these parameters were not modified by the fat-free diet. In experiment 2, bile diverted and sham operated rats were refed the standard diet for 16 h with prior 32 h fasting. Bile diversion, like cholestyramine feeding, lowered the content of total bile acids, the activities of pancreatic hydrolases in the intestinal washings, and the specific activity of aminopeptidase in the intestinal mucosa. The specific activity of sucrase in the intestinal mucosa was higher in bile diverted rats but the activity of alkaline phosphatase was not changed. These data indicate that the decreased abundance of intraluminal bile acid affects the activity of intestinal aminopeptidase not through the decreased absorption of dietary lipid.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Cholestyramine and bile diversion lower the aminopeptidase activity in the intestinal brush border membrane of rats. 800 18

The effects of gentamicin and G418 on the cellular function of LLC-PK1 epithelial pig kidney cells were investigated. Exposing the cells for 2 days to these aminoglycoside antibiotics inhibited the increase in cell-associated apical membrane enzyme activity (alkaline phosphatase, aminopeptidase, and gamma-glutamyltransferase). Kinetic analysis revealed that the maximal activity of alkaline phosphatase was reduced by these aminoglycosides. Both aminoglycosides inhibited [3H]leucine incorporation into microsomes prepared from LLC-PK1 cells. The LLC-PK1 cells transfected with DNA encoding aminoglycoside 3'-phosphotransferase II, designated T2000B, were resistant to G418 as assessed by colony formation assay and the number of floating dead cells and by assay of apical enzyme activity. After a 4-hr exposure to G418, [3H]leucine incorporation in the host LLC-PK1 cells was inhibited, whereas that in T2000B cells was relatively unaffected. Gentamicin inhibited [3H]leucine incorporation similarly in both cells. The inhibition of protein synthesis by aminoglycosides occurred earlier than that of apical enzyme activity. These findings suggest that the inhibition of protein synthesis by aminoglycoside antibiotics is a possible cause of the reduction in cell viability as well as the apical enzymes in LLC-PK1 cells.
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PMID:Cellular toxicity of aminoglycoside antibiotics in G418-sensitive and -resistant LLC-PK1 cells. 805 26

Endopeptidase 24.11 (enkephalinase), an enzyme known to be present in plasma and liver, is capable of metabolizing a substantial number of bioactive peptides. We measured plasma endopeptidase 24.11 activity in normal subjects and in patients with chronic hepatocellular disease or chronic cholestatic liver disease. The mean level of plasma endopeptidase 24.11 activity was 13 times higher in cholestatic patients than in controls or patients with hepatocellular disease (p < 0.01). Plasma endopeptidase 24.11 activity in patients correlated closely with traditional serum markers of cholestasis, including levels of alkaline phosphatase, gamma-glutamyltranspeptidase and aminopeptidase (p < 0.01 for all). However, plasma endopeptidase 24.11 activity correlated poorly with serum ALT aminotransferase level (p = NS), indicating that it is not a marker of hepatocellular disease. The lack of overlap between plasma endopeptidase 24.11 activity in cholestatic patients and noncholestatic liver disease controls suggests that this enzyme activity is a useful biochemical marker of cholestasis. In addition, because of the broad spectrum of peptides metabolized by endopeptidase 24.11, increased plasma endopeptidase 24.11 activity may contribute to the pathophysiology of the syndrome of cholestasis.
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PMID:Plasma endopeptidase 24.11 (enkephalinase) activity is markedly increased in cholestatic liver disease. 810 33

Intestinal mucosa of rats was prepared by squeezing the frozen and thawed intestine. The method was much easier compared to the conventional method in which intestine was cut longitudinally or everted and mucosa was scraped. Jejunal mucosal weight prepared by the two methods was not different, but ileal mucosal weight prepared by squeezing was significantly heavier than that by scraped. No significant difference was observed between activity of some brush border enzymes (arylamidase, aminopeptidase, alkaline phosphatase, and sucrase) in mucosa prepared by squeezing and that by conventional scraping method in jejunum. Activity of brush border aminopeptidase and sucrase in ileal mucosa prepared by squeezing was significantly higher than that prepared by scraping.
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PMID:Facile preparation of rat intestinal mucosa for assay of mucosal enzyme activity. 828 18

A chimeric precursor interlinked by an arginine residue between the full-length signal sequence of alkaline phosphatase and the eukaryotic cytoplasmic cytochrome b5 was constructed. Expression of the chimeric precursor protein in Escherichia coli resulted in efficient export of spectrally authentic cytochrome b5 into the periplasm [Karim, Harding, Evans, Kaderbhai and Kaderbhai (1993) Bio/Technology 11, 612-618]. On sequencing, the apparent absence of arginine at the N-terminus of the secreted cytochrome b5 implied that the chimera was either miscleaved by signal peptidase or further processed following signal excision by an uncharacterized peptidase. The influence of the N-terminal region of cytochrome b5 on the unusual processing of the chimeric precursor was investigated by engineering a number of variant forms in which the region between Arg+1 and the mature portion of cytochrome b5 was extended and varied. Observations of the in vivo processed patterns of these variant cytochrome b5 forms exported into the periplasm revealed that the absence of arginine was due to neither miscleavage of the translocated precursor by the signal peptidase nor the nature of the early region of cytochrome b5. In fact, the selective excision of the arginine residue occurred subsequent to signal sequence deletion by an aminopeptidase which was sensitive to the metal chelator o-phenanthroline. We show that this aminopeptidase also participates in the trimming of the N-terminal arginine residue of the bacterial alkaline phosphatase to generate the three isoenzymes in the periplasm.
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PMID:Processing of chimeric mammalian cytochrome b5 precursors in Escherichia coli: reaction specificity of signal peptidase and identification of an aminopeptidase in post-translocational processing. 835 42

An epidemiologic study of Pasteurella haemolytica serovar 1 (Ph1) in market-stressed feeder calves from 7 farms in eastern Tennessee was conducted. The nasal mucus of each calf was cultured sequentially at the farm of origin (day 0), at an auction market (day 133), and at a feedyard in Texas (days 141, 148, 155, and 169). Of the 103 calves tested, 77 were culture-positive, including 1 on day 0, 1 on day 133, 20 on day 141, 57 on day 148, 50 on day 155, and 14 on day 169. From the 143 Ph1 isolates, 20 enzyme profiles were determined by use of a commercial enzyme system that detects 19 enzymatic reactions; 4 antimicrobial susceptibility profiles were obtained, using the disk-diffusion method, which evaluated susceptibility to 11 antibacterial drugs. All isolates were positive for acid phosphatase and alkaline phosphatase, but were negative for alpha-galactosidase, alpha-mannosidase, beta-glucosidase, beta-glucuronidase, cystine aminopeptidase, N-acetyl-beta-glucosaminidase, and trypsin. Other positive enzyme reactions included: leucine aminopeptidase, 140 Ph1 isolates; phosphohydrolase, 90 isolates; alpha-fucosidase, 63 isolates; esterase (C4), 59 isolates; valine aminopeptidase, 30 isolates; esterase lipase (C8), 24 isolates; beta-galactosidase, 2 isolates; and alpha-glucosidase, chymotrypsin and lipase (C14), 1 isolate each. Thirty-four Ph1 profiles were identified, using combined enzyme and antimicrobial susceptibility profiles. The data indicate that the strains isolated during the feedyard period may have been determined more by farm of origin (P < or = 0.001) than by habitation with calves from other farms while in the feedyard.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Identification of Pasteurella haemolytica A1 isolates from market-stressed feeder calves by use of enzyme and antimicrobial susceptibility profiles. 842 78

Endoscopic diagnosis completed by biopsy achieved remarkable accuracy. New trends--endoscopy with the use of ultrasound orange red porphyrin fluorescence elicited by blue light e. g. krypton laser and strip biopsy not only greater accuracy of endoscopic methods but also open up new therapeutic possibilities. Histochemical and histoenzymatic methods allow to classify histological findings of the norm (presence of pepsinogen and neutral glycoprotein) of atrophic gastritis with intestinal metaplasia (acid glycoprotein, activity of sucrose, alkaline phosphatase-AP, leucin-aminopeptidase-LAP) and of dysplasia (presence of sulfomucin, decrease of AF, LAP, sucrose and trehalase activity) and to divide them into well defined groups. We are able to distinguish which mucosal changes are suspect, we know that malignant transformation can after a certain period of time be expected approximately 2-14% yet we still do not know whether the period from dysplastic change to malignant transformation is not longer than malignant change in resected stomach. Epidemiologic and experimental data gives us enough reasons for dietary and chemopreventive measures (apart of other treatment) especially in risk groups patients.
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PMID:[Early diagnosis of gastric cancer]. 850 56

The mechanism by which yeast dipeptidyl aminopeptidase (DPAP) A, type II integral membrane protein, is retained in the late Golgi apparatus has been investigated. Prior work demonstrated that the 118-amino acid cytoplasmic domain is both necessary and sufficient for Golgi retention and that mutant or overexpressed DPAP A no longer retained in the Golgi was delivered directly to the vacuolar membrane (Roberts, C. J., S. F. Nothwehr, and T. H. Stevens. 1992. J. Cell Biol. 119:69-83). Replacement of the DPAP A transmembrane domain with a synthetic hydrophobic sequence did not affect either Golgi retention of DPAP A or vacuolar delivery of the retention-defective form of DPAP A. These results indicate that the DPAP A transmembrane domain is not involved in either Golgi retention or targeting of this membrane protein. A detailed mutational analysis of the cytoplasmic domain of DPAP A indicated that the most important elements for retention were within the eight residue stretch 85-92. A 10-amino acid region from DPAP A (81-90) was sufficient for Golgi retention of alkaline phosphatase, a type II vacuolar membrane protein. Detailed mutational analysis within this 10-amino acid sufficient region demonstrated that a Phe-X-Phe-X-Asp motif was absolutely required for efficient retention. The efficiency of Golgi retention via the DPAP A signal could be diminished by overexpression of wild type but not retention-defective versions of Kex2p, another late Golgi membrane protein, suggesting that multiple Golgi membrane proteins may be retained by a common machinery. These results imply a role for a cytoplasmic signal involving aromatic residues in retention of late Golgi membrane proteins in the yeast Saccharomyces cerevisiae.
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PMID:Membrane protein retention in the yeast Golgi apparatus: dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues. 850 44

The histological change of the biliary mucosa in clonorchiasis is characterized as adenomatous hyperplasia, and cross-sectioned mucosa looks like intestinal mucosa. In addition to the glandular hyperplasia, the metaplasia of mucin secreting cells is also known. The present study investigated the presence of intestinal secretion from the biliary mucosal cells of rabbits and rats with Clonorchis sinensis infection. The rabbit was infected with 300 and the rat was infected with 100 metacercariae of C. sinensis. A part of the animals were followed up after praziquantel treatment. The rabbit livers were prepared for histochemistry to observe any endocrine secretion and the bile duct mucosa of the mice was processed for the activity of brush border membrane (BBM)-bound enzymes of the small intestine. Immunohistochemistry with the polyclonal antibodies and biotin-streptavidin-peroxidase staining kit showed no positive cells for gastrin and secretin, but a few cells were positive for serotonin. The proliferated biliary mucosa of the mice revealed no activity of disaccharidases and aminopeptidase. Only alkaline phosphatase activity was found both in the control and the infected. The hyperplastic biliary mucosal cells showed no gastrointestinal secretory functions. The serotonin secreting cells may be one of the inflammatory cells.
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PMID:Secretions of the biliary mucosa in experimental clonorchiasis. 851 95


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