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 histochemical distribution of 14 enzymes in the human amnion at term are described. Adenosine triphosphatase, 5'-nucleotidase, acid phosphatase and nonspecific esterase show continuous gradations of enzyme activity. Cells with intense activity are prominent in acid phosphatase and nonspecific esterase preparations. A distinct subpopulation of amniotic cells can be defined by their alkaline phosphatase activity. The possible correlations with morphological studies are discussed.
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PMID:Enzyme histochemical patterns in the normal human amnion: amniotic histochemical patterns. 4 99

The biochemical effects of the nonsteroidal compound Centchroman were observed in healthy, adult, female rhesus monkeys. The compound was administered at the antifertility dose (.625 mg/kg) for 22 days in a cycle. No marked weight changes were seen in the Fallopian tube, ovary, adrenal or pituitary as a result of treatment. Uterine weight increased significantly, however (p less than .01). In the Fallopian tube, levels of glycogen and protein increased significantly (p less than .01), lactic acid decreased significantly (p less than .01), and nonprotein nitrogen was unchanged as a result of treatment. Similar changes were observed in the uterus, and in addition, total total phospholipid concentration rose significantly (p less than .01) in the uterus. The activities of beta-glucuronidase, acid and alkaline phosphatases and glucose-6-phosphate dehydrogenase (G-6-PD) in the Fallopian tube were unchanged due to treatment. Adenosine triphosphatase (ATPase) and malic dehydrogenase activities were significantly stimulated (p less than .01) and lactic dehydrogenase activity was significantly depressed (p less than .01). In the uterus, beta-glucuronidase and acid and alkaline phosphatase activity were unaltered, however, the activities of ATPase and the dehydrogenases of glucose-6-phosphate, lactate and malate were markedly increased (p less than .01). It is suggested that the antifertility effect of Centchroman may be due principally to the ability of the compound to elicit estrogen-like responses in the Fallopian tube and uterus.
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PMID:Effect of 3,4-trans-2,2-dimethyl-3-phenyl-4-P-(beta-pyrrolidinoethoxy) phenyl -7-methoxy chroman (centchroman) on the biochemistry of the fallopian tube and uterus of rhesus monkeys (Macaca mulatta). 12 88

Three parts were distinguished by electron microscopy and by enzyme histochemistry at the boundary zone between the white and red pulp of the human spleen. The first was the inner layer of the perifollicular region, composed of medium-sized lymphocytes with abundant free ribosomes in their cytoplasm. A small number of reticulum cells intervened among these lymphocytes. This inner layer was considered to correspond to the "Follikelaussenzone" (Strasser). The second was the outer layer of the perifollicular region, composed of a meshwork of reticulum cells with reticular fibers, and sheathed and non-sheathed arteries. Small and medium-sized lymphocytes, granulocytes, erythrocytes, platelets, and a small number of plasma cells were observed in the mesh spaces. This outer layer was considered to correspond to the "marginal zone" (Snook). At the outermost part of this layer, the venous sinus appeared. There was no distinct border between this layer and the red pulp. The third was the neighboring region of the periarterial lymphoid sheath, showeing similar structure and cellular components to the outer layer of the perifollicular region. It was characteristic feature for the lymphocytes and some of the reticulum cells of this region to have a strong activity for alkaline phosphatase reaction, while the lymphocytes of the outer layer showed only a weak activity. Adenosine triphosphatase and 5'-nucleotidase activities were demonstrated on the lymphocytes of these three parts of the boundary zone as well as the lymph follicle. Different activities for these enzyme reactions may indicate the functional properties of the B-cell system.
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PMID:An electron microscopic and enzyme histochemical study of the boundary zone between the white and red pulp of the human spleen. 14 41

Seven well differentiated chondrosarcomas of bone have been analyzed by electron microscopy, and the fine structural localization of adenosine triphosphatase and nonspecific alkaline phosphatase has been elucidated. On the basis of the fine structural appearance, two distinct cell types were shown to constitute the tumor tissue: chondrocyte-like cells and large "mitochondria-rich cells". Large, multinucleated cells in the tumor did not seem to correspond to osteoclasts but rather were likely to represent true neoplastic cells. Some chondrocyte-like cells appeared to be binucleated by virtue of deep, groove-like nuclear indentations. Adenosine triphosphatase and alkaline phosphatase were associated with the plasma membrane of both chondrocyte-like and mitochondria-rich cells suggesting that they might be of common origin. Normal chondroblasts and chondrocytes lack histochemically demonstrable adenosine triphosphatase on their plasma membrane. Presence of this enzyme in the tumor cells may indicate that they are histogenetically related to immature non-chondroid matrix forming cells (known to carry the enzymes).
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PMID:Contribution to the knowledge of the fine structure of chondrosarcoma of bone. With a note on the localization of alkaline phosphatase and "ATPase". 15 79

Adenosine contracts pregnant and nonpregnant guinea pig myometrial smooth muscle (MSM). We have 1) described dissociation of A1-adenosine receptors from adenylate cyclase inhibition in nonpregnant MSM (M. A. Smith, J. L. Silverstein, D. P. Westfall, and I. L. O. Buxton, Cell. Signal. 1: 357-365, 1989); 2) described appearance of such inhibitory coupling in pregnant MSM [W. P. Schiemann, D. P. Westfall, and I. L. O. Buxton, Am. J. Physiol. 261 (Endocrinol. Metab. 24): E141-E150, 1991]; and 3) demonstrated a role for myometrial A1 receptors in the rapid formation of D-myo-inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] in nonpregnant MSM and the cyclooxygenase dependence of this effect (W. P. Schiemann, K. O. Doggwiller, and I. L. O. Buxton. J. Pharmacol. Exp. Ther. 258: 429-437, 1991). To further characterize adenosine action in pregnant tissue, we explored A1 coupling to increased phosphoinositide hydrolysis in near-term pregnant MSM. The A1-receptor agonist (+)-N6-(2-phenylisopropyl)adenosine stimulates the rapid dose-dependent formation of Ins(1,4,5)P3 and stimulates rapid degradation of uterine inositol monophosphates (InsP) in a manner paralleling increases in inositol polyphosphates. Both A1-mediated responses were blocked by the A1 antagonist 8-(p-sulfophenyl)theophylline, and, unlike the effect observed in nonpregnant MSM, treatment of pregnant MSM with either meclofenamate or indomethacin failed to block A1-mediated increases in Ins(1,4,5)P3. Pretreatment of MSM with either Li+ or pertussis toxin failed to alter either Ins(1,4,5)P3 formation or InsP degradation. Furthermore, assay of inositol phosphomonoesterase (InsPase) activity in the presence or absence of Li+ confirmed the existence of an MSM Li(+)-insensitive InsPase enzyme.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Adenosine A1-receptor coupling to phosphoinositide metabolism in pregnant guinea pig myometrium. 165 16

Previous results demonstrated that the adenosine that accumulates in human fat cell suspensions is derived from extracellular sources (Kather, H. (1988) J. Biol. Chem. 263, 8803-8809). To get insight into the mechanisms responsible for the lack of adenosine release, extracellular adenine nucleotide catabolism was minimized by 10 mmol/liter beta-glycerophosphate and 10 mumol/liter alpha,beta-methyleneadenosine 5'-diphosphate. Intracellular adenine nucleotide catabolism resulted in a release of inosine and hypoxanthine under these conditions that was increased markedly by isoproterenol. Experiments with inhibitors of adenosine deaminase and adenosine kinase indicated that the production of inosine and hypoxanthine proceeded via AMP deamination. Consistently, IMP levels were increased transiently in the presence of isoproterenol. In addition, the cells possessed a nucleotide phosphomonoesterase that was resistant to the inhibitory actions of ATP and alpha,beta-methyleneadenosine 5'-diphosphate and showed preference for IMP over AMP. Adenosine (approximately 1 nmol/10(6) cells/h) was also produced inside the cells. However, adenosine production was unrelated to ATP turnover via adenylate cyclase, and any adenosine formed was immediately reconverted to adenine nucleotides in the absence and presence of isoproterenol. It was concluded that adenosine is not released by intact human adipocytes, because the alternative routes of intracellular AMP catabolism are compartmentalized (at least in functional terms), and adenosine kinase is not saturated with substrate in the absence and presence of isoproterenol.
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PMID:Pathways of purine metabolism in human adipocytes. Further evidence against a role of adenosine as an endogenous regulator of human fat cell function. 229 25

Elevated concentrations of alkaline phosphatase occur in a variety of diseases. The effect of alkaline phosphatase on platelet aggregation was tested. Adenosine diphosphate-induced aggregation was inhibited at the highest concentrations of alkaline phosphatase employed. Similar results were observed when epinephrine, collagen and arachidonic acid were used as aggregating agents. A dose-dependent inhibition of ristocetin-induced aggregation by alkaline phosphatase was observed. These results were confirmed using plasma from patients with cholestatic disease and elevated concentrations of alkaline phosphatase similar to those used in the in vitro studies. These data indicate that patients with significantly elevated levels of alkaline phosphatase may be predisposed to a thrombocytopathy.
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PMID:The effect of alkaline phosphatase on platelet aggregation. 274 39

Adenosine [gamma-(S)-16O,17O,18O]triphosphate was used as substrate in the phosphokinase reaction catalyzed by 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase. The product D-fructose 2,6-[2-16O,17O,18O]bisphosphate was then used as substrate in the alkaline phosphatase-mediated transfer of the phospho groups to (S)-butane-1,3-diol, where the configuration at phosphorus has been determined. Although there was approximately equal transfer by alkaline phosphatase of the labeled 2- and the unlabeled 6-phospho groups, the subsequent assignment of configuration of the chiral phospho group from the 2-position was unambiguous. It was found that 6-phosphofructo-2-kinase proceeds by a pathway that results in net inversion of the configuration at phosphorus. The simplest interpretation of this result is that the phospho group is transferred directly between substrates in a ternary complex by an "in-line" mechanism not involving a phosphoenzyme intermediate. This conclusion is consistent with the fact that the enzyme cannot be labeled by [gamma-32P]ATP and with steady-state kinetic data that suggest an ordered sequential mechanism. This finding also indicates that the adenine nucleotide and sugar phosphate isotope exchange reactions catalyzed by the enzyme are not relevant to the normal catalytic pathway of the kinase.
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PMID:The stereochemical course of phospho group transfer catalyzed by rat liver 6-phosphofructo-2-kinase. 297 3

A screening method using high-performance liquid chromatography (HPLC) for the simultaneous detection of deficiencies of adenine phosphoribosyltransferase (APRT) and hypoxanthine phosphoribosyltransferase (HPRT) activities in human erythrocytes is described. Both enzyme reactions of APRT and HPRT in lysates treated with a charcoal-dextran were simultaneously carried out in the same reaction tube and the enzyme activities were determined by measuring the increases in absorbance at 260 nm of adenosine and inosine converted from adenosine-5'-monophosphate and inosine-5'-monophosphate with alkaline phosphatase. Adenosine and inosine were separated from adenine and hypoxanthine by a reversed-phase column. The method could detect 1% of normal APRT activity and 0.3% of normal HPRT activity. The within-run coefficients of variation for APRT and HPRT activities were 3.2 and 3.4%, respectively.
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PMID:Screening for adenine and hypoxanthine phosphoribosyltransferase deficiencies in human erythrocytes by high-performance liquid chromatography. 343 62

1. A method for the preparation of brush border from rabbit kidneys is described. Contamination by other organelles was checked by electron microscopy and by the assay of marker enzymes and was low. 2. Seven enzymes, all hydrolases, were substantially enriched in the brush-border preparation and are considered to be primarily located in this structure. They are: alkaline phosphatase, maltase, trehalase, aminopeptidase A, aminopeptidase M, gamma-glutamyl transpeptidase and a neutral peptidase assayed by its ability to hydrolyse [(125)I]iodoinsulin B chain. 3. Adenosine triphosphatases were also present in the preparation, but showed lower enrichments. 4. Alkaline phosphatase was the most active phosphatase present in the preparation. The weak hydrolysis of AMP may well have been due to this enzyme rather than a specific 5'-nucleotidase. 5. The two disaccharidases in brush border were distinguished by the relative heat-stability of trehalase compared with that of maltase. 6. The individuality of the four peptidases was established by several means. The neutral peptidase and aminopeptidase M, both of which can attack insulin B chain, differed not only in response to inhibitors and activators but also in the inhibitory effect of a guinea-pig antiserum raised to rabbit aminopeptidase M. This antiserum inhibited both the purified and the brush-border activities of aminopeptidase M. The neutral peptidase and gamma-glutamyl transpeptidase were unaffected but aminopeptidase A was weakly inhibited. The characteristic responses to Ca(2+) and serine with borate served to distinguish aminopeptidase A and gamma-glutamyl transpeptidase from other peptidases. 7. No dipeptidases, tripeptidases or carboxypeptidases were identified as brush-border enzymes. 8. Incubation of brush border with papain released almost all the aminopeptidase M activity but only about half the activities of maltase, gamma-glutamyl transpeptidase and aminopeptidase A. No release of alkaline phosphatase, trehalase or the neutral peptidase was observed.
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PMID:Studies on the enzymology of purified preparations of brush border from rabbit kidney. 414 72


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