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 diagnostic values of CA 19-9 and CEA were evaluated in 187 cases (including 31 gastric, 41 colorectal, 12 pancreatic, 7 hepatobiliar and 5 hepatocellular carcinomas). These tumor markers were compared to the other laboratory parameters [hemoglobin, erythrocyte sedimentation rate, serum bilirubin, ASAT (aspartate amino transferase), ALAT (alanine amino transferase) GGT (gamma glutamil transpeptidase), ALP (alkaline phosphatase)]. The specificity of CA 19-9 was 89.5%, while the sensitivity of this tumor markers was 91.7% in pancreatic carcinoma, 54.8% in gastric carcinoma and 43.9% in colorectal carcinoma. The sensitivity of CEA only in colorectal patients was higher than that of CA 19-9 (specificity 73.9%, sensitivity 64.5%). Although the CA 19-9 and CEA are not known to give any cross-reaction with each other, simultaneous measurement and evaluation of these two tumor antigens did not result in a better diagnostic sensitivity. After undergoing a gastrointestinal carcinoma operation, CA 19-9 indicated the appearance of tumor recidiva with a 62% sensitivity. Calculated together with CEA the sensitivity elevated to 88.9%. In most of the patient with benign cholostasis, the CA 19-9 and CEA values were out of the normal range (53.3% and 36.4% respectively), so these tumor markers are not suitable to differentiate between benign and malign cholostasis. According to the authors, CA 19-9 is the most useful diagnostic tool to differentiate between pancreatic carcinoma and pancreatitis chronica (both group without cholostasis), as well as for monitoring the patients after surgery of a gastrointestinal cancer.
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PMID:[Diagnostic value of CA 19-9 and CEA in gastrointestinal pathology]. 160 81

The model of biliary tract infection induced in rats given suspension of E. coli into the bile duct is described. To prevent leakage of microorganisms after the administration, a temporary ligation of the bile duct followed. Contemporary groups of sham-operated and control rats (given saline by intrabiliary injection) were compared to assess the significance of the changes. The effect of biliary infection was concentration dependent. If 0.1 ml of the concentration containing 10(2), 10(3) and 10(6) colony-forming units/ml was injected, the mortality of rats reached 8%, 57% and 65%, respectively within 24 h. Blood and bile cultures from all dead animals grew E. coli. To evaluate the effect of chronic biliary infection, the concentration of 10(2) colony-forming units/ml was used. Serum concentrations of total and conjugated bilirubin, cholesterol and creatinine, activities of S-alanine-aminotransferase, S-aspartate-aminotransferase, alkaline phosphatase, the count of leucocytes in blood, total body weight with weight of the liver were investigated on days 1, 4 and 12 after the treatment. The results showed: an increase in leucocytes (21 +/- 4.2 10(9)/l, p less than 0.02 vs control animals) on day 4, an augmentation of serum cholesterol on day 1, (2.1 +/- 0.9 mmol/l, p less than 0.02 vs control animals), the presence of E. coli in blood on day 1 and its persistence in the bile on days 1, 4 and 12. Except the bile, all of the other symptoms were reversible by day 12.
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PMID:A contribution to the model of biliary infection in rats. 161 85

In order to investigate the function of Asp-327, a bidentate ligand of one of the zinc atoms in Escherichia coli alkaline phosphatase, and the importance of this zinc atom in catalysis, site-specific mutagenesis was used to convert Asp-327 to either asparagine or alanine. The 10(7)-fold decrease in the kcat/Km ratio observed for the Asp-327----Ala enzyme compared to the wild-type enzyme indicates that the side chain of Asp-327 is important for zinc binding at the M1 site. However, only one of the two carboxyl oxygens of Asp-327 is essential for zinc binding, since the Asp-327----Asn enzyme shows approximately the same hydrolysis activity as the wild-type enzyme. The fact that the enzymatic activity of this mutant enzyme shows a dependence on zinc concentration suggests that the other carboxyl oxygen or the negative charge on the side chain of Asp-327 is important in binding of the zinc at the M1 site. However, the zinc hydroxyl must still be appropriately positioned to attack the phosphoserine in the Asp-327----Asn enzyme; therefore, the negative charge and at least one carboxyl oxygen of the side chain are not directly involved in positioning or deprotonating the zinc hydroxyl. 31P NMR studies indicate that the Asp-327----Asn enzyme exhibits transphosphorylation activity at both pH 8.0 and pH 10.0, but at a reduced level compared to the wild-type enzyme. The biphasic production of 2,4-dinitrophenylate in the pre-steady-state kinetics of the mutant enzymes at pH 5.5 suggests that the breaking of the phosphoenzyme covalent complex is rate-limiting for both mutant enzymes. These results suggest that the main function of the zinc atom at the M1 site in catalysis involves decomposition of the phosphoenzyme covalent complex and that it may be important in helping to stabilize the alcohol leaving group.
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PMID:The importance of aspartate 327 for catalysis and zinc binding in Escherichia coli alkaline phosphatase. 164 10

The influence of fluoride (F) on the transport of Pi was investigated in the osteoblast-like cell line UMR-106. Exposure of cells to F induced a dose-related stimulation of the Na-coupled Pi transport. Pi transport was significantly increased 6 h after 1 mM F incubation, with maximal response observed at 24 h (F 38.0 +/- 2.3, vehicle 19.8 +/- 1.2 pmol.micrograms DNA-1.4 min-1; P less than 0.001). Na-dependent alanine transport was not changed by F. The selective effect of F on Pi transport was not associated with changes in adenosine 3',5'-cyclic monophosphate, cell proliferation, or alkaline phosphatase activity. However, it was completely blunted by inhibiting translational processes with cycloheximide. Furthermore, F enhanced the stimulatory effect on Pi transport of various mitogens such as fetal calf serum, insulin, and insulin-like growth factor I. In conclusion, F can selectively enhance the activity of the Pi transport system present in the plasma membrane of UMR 106 osteoblast-like cells by a mechanism that probably involves newly synthetized proteins.
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PMID:Fluoride selectively stimulates Na-dependent phosphate transport in osteoblast-like cells. 164 69

In the last decade, the primary, biliary liver cirrhosis was diagnosed in 17 female patients aged between 33 and 72 years. The most frequent complaint were itching and jaundice. Hepatomegaly and itching predominated in the clinical signs Laboratory tests have shown and increase in alkaline phosphatase activity, gamma-glutamyltranspeptidase, and alanine-aminotransferase activities, accelerated ESR and decrease in blood serum albumins. Immunological abnormalities were found in 15 patients, including 12 with antimitochondrial antibodies. Liver biopsy was carried out in all patients enabling to diagnose the primary cirrhosis in 14 of them. Duration of the disease was between 1 and 9 years. Immunosuppressive treatment was carried out in 10 patients, and symptomatic treatment in the remaining 7 patients. No difference in the effect of therapy on actual health state of patients was seen.
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PMID:[Primary biliary liver cirrhosis in patients treated at Szczecin hospitals in 1978-1988]. 166 45

Nascent precursors of phosphatidylinositol-glycan (PI-G)-linked membrane proteins contain a hydrophobic COOH-terminal sequence of 15-30 residues that is eliminated during processing to yield a newly exposed COOH terminus to which the PI-G moiety is added. There is no consensus as to the primary structure of the terminal peptide but there is a specific requirement for the amino acid destined to become the COOH terminus. In nascent human placental alkaline phosphatase (PLAP), the PI-G tail is attached to Asp-484. Site-directed mutants with glycine, alanine, cysteine, serine, or asparagine (category I) at residue 484 become PI-G tailed, appear in the plasma membrane, and are enzymatically active when expressed in COS cells. Although mutants with glutamic acid, glutamine, proline, tryptophan, leucine, valine, phenylalanine, threonine, methionine, and tyrosine (category II) are expressed equally well, only small amounts appear on the plasma membrane. Furthermore, they are not PI-G tailed and have little alkaline phosphatase activity. Studies with truncated PLAP-489 rule out nonspecific conformational changes in category II mutant proteins as a reason for their failure to be processed in COS cells and point to a specific COOH-terminal processing enzyme. Direct evidence that the selectivity for category I amino acids is enzymatically determined was obtained in a cell-free translation/processing system by using rabbit reticulocyte lysate and CHO cell rough microsomal membranes. In this in vitro system, both category I and category II mutants of PLAP-513 were translated, glycosylated, and cleaved by NH2-terminal signal peptidase. However, an additional and selective cleavage at residue 484 was observed only with category I mutants.
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PMID:Selectivity at the cleavage/attachment site of phosphatidylinositol-glycan anchored membrane proteins is enzymatically determined. 170 Apr 20

Haptoglobin (Hp) phenotypes were determined by thin-layer polyacrylamide gel electrophoresis in 2071 normal Russians, Tatars, and Bashkirs. Hp phenotype distribution was found similar in these populations, making up 13.4% for Hp 1-1, 48% for Hp 1-2, 38.6% for Hp 2-2. Hp1 gene incidence (0.37) was characteristic of the European populations. Serum alkaline phosphatase and gamma-glutamyl transpeptidase activities were similar in all the three Hp phenotypes. Alanine and aspartate aminotransferases and acid phosphatase activities were higher in Hp 1-1 phenotype by 25, 15, and 15 percent, respectively.
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PMID:[Haptoglobin phenotypes and serum enzyme activity]. 171 33

Twelve blood serum parameters: sodium, potassium, chlorine, total protein, cholesterol, glucose, urea nitrogen, creatinine, bilirubin, alkaline phosphatase, alanine and aspartate aminotransferases activities were measured in 488 normal subjects (male), residents of Leningrad, by the Technicon (USA) microanalyzer. Relationships between the estimated reference values and the distribution patterns of the referent blood parameters (variability, symmetric pattern) were analyzed. The authors compare the reference values of the Leningrad population with those obtained by this microanalyzer in the USA.
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PMID:[Characteristics of the distribution and reference values of 12 biochemical indices of the blood serum]. 171 39

Serum CA 19-9 and alpha-fetoprotein (AFP) levels were determined in 211 patients with liver cirrhosis and 27 with primary hepatocellular carcinoma (HCC) associated with liver cirrhosis. This was done to determine the usefulness of CA 19-9 level with respect to AFP level in distinguishing between these two illnesses, and to assess the influence of some clinical and biochemical variables on these tests in patients with liver cirrhosis with or without primary HCC. Pathologic AFP values were found in 23 of 27 (sensitivity, 85%) patients with HCC; CA 19-9 levels increased in only 12 of 27 (sensitivity, 44%) HCC patients, the values being comparable with those of patients with liver cirrhosis. In liver cirrhosis a substantial number of false-positive values was found for both markers, although they were higher for CA 19-9 (50 of 211 versus 39 of 211). In liver cirrhosis correlations were found between AFP level and alanine amino-transferase level; and between CA 19-9 level and (1) total bilirubin value, (2) alkaline phosphatase level, and (3) pseudocholinesterase level. The authors conclude that CA 19-9 level is a poor biochemical marker, inferior to AFP level, in the detection of a carcinomatous transformation of liver cirrhosis. The finding of false-positive AFP values in liver cirrhosis seems mainly attributable to cellular proliferation and necrosis. Cholestasis seems to greatly affect serum CA 19-9 level variations, probably by reducing its liver metabolism.
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PMID:Serum CA 19-9 and alpha-fetoprotein levels in primary hepatocellular carcinoma and liver cirrhosis. 138 Dec 71

p19 is a highly conserved 19-kDa cytosolic protein that undergoes phosphorylation in mammalian cells upon activation of several distinct signal transduction pathways. Its expression is widespread but developmentally regulated. To determine the in vivo phosphorylation site(s) of p19, the protein was purified from bovine brain and resolved into the unphosphorylated form (p19) and a mixture of the two predominant phospho-forms (pp19). Proteolytic fragments of p19 and pp19 were examined by liquid chromatography/mass spectrometry (LC/MS). We detected ion masses corresponding to fragments spanning the entire amino acid sequence as deduced from the cDNA except for those predicted to contain an unmodified amino terminus. Instead, the digests revealed ions corresponding to peptides lacking the initiator methionine and containing an N-acetylated alanine at the amino terminus. The analysis of pp19, but not that of p19, revealed two sets of ions representing peptides whose m/z values differed by 80 atomic mass units, the incremental mass of a phosphate residue. These putative phosphate-bearing peptides were sensitive to alkaline phosphatase treatment. Using combined trypsin and V8 protease digestions, the phosphorylation sites were mapped to Ser-25 and Ser-38, in the peptides Leu-Ile-Leu-Ser*-Pro-Arg and Phe-Pro-Leu-Ser*-Pro-Pro-Lys, respectively. Interestingly, both phosphoserines are in a very similar sequence context, suggesting that a single proline-directed serine protein kinase, possibly p34cdc2, is responsible for phosphorylation of both sites in vivo.
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PMID:Analysis of phosphoprotein p19 by liquid chromatography/mass spectrometry. Identification of two proline-directed serine phosphorylation sites and a blocked amino terminus. 173 1


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