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:3.1.4.37 (CNPase)
539 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The properties of three phosphatases from Salmonella typhimurium have been examined. A cyclic 2',3'-nucleotide phosphodiesterase (EC 3.1.4.d) hydrolyzes cyclic 2',3'-purine and -pyrimidine nucleotides, as well as 3'-mononucleotides, and has a pH optimum of about 7.5. It requires divalent cations for activity and has a molecular weight of 67,000. Acid hexose phosphatase (EC 3.1.2.2) possesses activity towards hexose phosphates as well as other sugar phosphates. The enzyme is apparently a dimer of 37,000-dalton subunits. Nonspecific acid phosphatase (EC 3.1.3.2) hydrolyzes a variety of phosphate esters, including nucleotides and sugar phosphates. The enzyme also hydrolyzes the phosphoric anhydride bonds of pyrophosphate and nucleotides. Michaelis constants of the nonspecific acid phosphatase for several of its substrates are in the 1 to 2 mM range. Nonspecific acid phosphatase is a dimer of 27,000-dalton subunits.
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PMID:Properties of two phosphatases and a cyclic phosphodiesterase of Salmonella typhimurium. 1 82

The activity of glycerophosphorylcholine phosphodiesterases was determined in the mesencephalon, diencephalon, cerebral hemispheres, cerebellum and olfactory bulb during postnatal development from P5 to P70 of rat brain. These activities are low and gradually increase to near adult levels by the end of the first postnatal month similar to that for CNPase activity. This is in accord with glycerophosphorylcholine choline phosphate phosphodiesterase being present in the myelin membrane.
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PMID:Regional and developmental estimations of glycerophosphorylcholine phosphodiesterase activities in rat brain. 254 Sep 50

Secondary cultures of Schwann cells were transfected with a plasmid containing the SV-40 T antigen gene expressed under the control of the mouse metallothionein-I promoter. We used the calcium phosphate method for transfection and obtained a transfection efficiency of 0.01%. The colonies were cloned by limited dilution, and these cloned cell lines were carried in medium containing zinc chloride (100 microM). One cloned cell line, which has now been carried for 180 doublings, appears to have a transformed phenotype with a doubling time of 20 h. These cells express SV-40 T antigen while maintaining established Schwann cell properties (positive staining for 217c, Ran-2, A5E3, glial fibrillary acidic protein, presence of 2',3'-cyclic nucleotide phosphohydrolase [CNPase] activity, and the ability to synthesize sulfogalactosylceramide and mRNA for the myelin protein, P0). Removal of zinc chloride from the medium resulted in reduced expression of T antigen and a change in the appearance of the cells to a more bipolar shape, although they still did not exhibit contact inhibition and maintained a doubling time of 20 h. These cells now became Ran-2-negative and showed increases in CNPase activity and in their ability to synthesize sulfogalactosylceramide. The amount of P0 mRNA remained unchanged. Transfected Schwann cells, however, stopped dividing when they contacted either basal lamina or neurites and became bipolar in appearance. The Schwann cells in contact with the neurites then extended processes to wrap around bundles of neurites. Transfection with the SV-40 T antigen gene therefore provides a method for obtaining Schwann cell lines that continue to express properties associated with untransfected cells in culture and may be used to study axon-Schwann cell interaction.
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PMID:Transfection of neonatal rat Schwann cells with SV-40 large T antigen gene under control of the metallothionein promoter. 282 29

Primary cultures of cerebral glia derived from neonatal rat brain were utilized to determine 1) the developmental changes of dolichol-linked oligosaccharide and N-linked glycoprotein biosyntheses, 2) the enzymatic correlates of these developmental changes, and 3) the temporal relations between the biosyntheses of dolichol-oligosaccharide and N-linked glycoproteins and the biochemical expression of astrocytic and oligodendroglial differentiation. Marked, parallel developmental increases in the rates of incorporation of [3H]glucosamine into both dolichol-oligosaccharide and glycoprotein were observed, with maximal rates achieved after 9-10 days in culture and little change occurring over the next 10 days in culture. Concerning the enzymatic correlates, dolichol kinase exhibited a moderate developmental increase with a maximum at 5 days in culture, whereas the activities of the three critical enzymes that utilize dolichyl phosphate in the synthesis of the dolichol-linked oligosaccharide, i.e., N-acetylglucosaminylphosphotransferase (GlcNAc-1-P transferase), mannosylphosphoryldolichol (Man-P-Dol) synthase, and glucosylphosphoryldolichol (Glc-P-Dol) synthase, reached maxima after 6-9 days in culture. Both the activity of Man-P-Dol synthase in vitro and the rate of formation of its product, Man-P-Dol, in intact cells were shown to correlate closely with the rates of oligosaccharide and glycoprotein biosyntheses. An important regulatory role for Man-P-Dol synthase and its product, Man-P-Dol, was suggested further by the demonstration of a maturation-dependent activation by Man-P-Dol of GlcNAc-1-P transferase, the first committed step in the pathway. Two enzymatic markers of astrocytic (glutamine synthetase) and oligodendroglial (2',3'-cyclic nucleotide 3'-phosphohydrolase) differentiation exhibited marked developmental increases in activity with onset at the time of attainment of peak rates of dolichol-oligosaccharide and glycoprotein biosyntheses. Importance of the latter processes for glial differentiation is suggested.
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PMID:Dolichol-linked oligosaccharide and glycoprotein biosyntheses in glial cells in primary culture: development and enzymatic correlates. 284 60

The activity of 2', 3'-cyclic nucleotide 3'-phosphohydrolase (CNP, EC 3.1.4.37), a myelin-associated enzyme, was monitored in brain, spinal cord, and sciatic nerve homogenates from tri-o-tolyl phosphate (TOTP) and tri-m-tolyl phosphate (TMTP) treated hens. Atropinized adult White Leghorn hens were orally dosed with TOTP (200 mg/kg) or with TMTP (200 mg/kg). The treated birds were monitored daily for development of delayed neurotoxicity, and CNP activity was measured via spectrophotometry at the time of maximal locomotor impairment (27-35 days post dosing). The TOTP-treated birds manifested locomotor deficit by 15 days postdosing and exhibited T2-T4 ataxia at maximal locomotor impairment. The hens administered TMTP exhibited no signs of delayed neurotoxicity. CNP activity of sciatic nerve preparations from TOTP-dosed hens was significantly inhibited (p less than 0.05) at the time of maximal locomotor impairment. There was also a significant correlation between decreased CNP activity and the degree of ataxia at the time of maximal locomotor impairment. This decrease in sciatic nerve CNP activity was most likely associated with nerve fiber degeneration. The level of CNP activity in spinal cord and brain homogenates from TOTP-dosed birds was not markedly altered. TMTP-treated birds exhibited no change in neural tissue CNP activity. The results suggest that the criterion of decreased CNP activity may serve as a useful biochemical adjunct to established clinical, biochemical, and morphological methods in the assessment of chemically-induced neuropathies.
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PMID:Effect of acute tri-o-tolyl phosphate exposure on 2', 3'-cyclic nucleotide 3'-phosphohydrolase activity in hen neural tissues. 284 76

A commercial cresyl diphenyl phosphate preparation was analyzed to contain approximately 35% of triphenyl phosphate, 45% of cresyl diphenyl phosphates, 18% of dicresyl phenyl phosphates and 2% of tricresyl phosphates. The product was almost free of the o-cresyl isomers as revealed by the analysis of its alkaline hydrolysis products. A single intraperitoneal injection (150 or 300 mg/kg) caused an induction of microsomal cytochrome P-450 in the liver of Wistar rats with a concomitant increase in the activities of mixed function monooxygenases and proliferation of smooth endoplasmic reticulum 24 h after the treatment. These effects were not detected in the kidneys. The morphological changes in hepatocytes included the enlargement of nuclei and mitochondria with increased cristae. The hepatic morphology returned to normal 2 weeks after the treatment. The activity of pseudocholine esterase in blood was inhibited 4 h and 24 h after the injection but the effect levelled off. The concentration of the organophosphates in blood and liver decreased rapidly with only traces detected in blood after 24 h. No effects on the activities of cerebral and muscle acetylcholine esterase were observed. The treatment (300 mg/kg) inhibited the brain--2',3'-cyclic nucleotide 3'-phosphohydrolase through the 2-week observation period associated with demyelination in peripheral nerves.
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PMID:Acute biological effects of commercial cresyl diphenyl phosphate in rats. 356 47

Synaptosomes were prepared from rat cortex by subjecting a washed crude mitochondrial pellet to centrifugation first on discontinuous Ficoll-isotonic sucrose gradients and then on discontinuous sucrose gradients. The synaptosome fraction, collected from the 7.5-14% Ficoll band (II), was further separated into two additional fractions, designated IIA and IIB, which bank at the 0.32-1.05 M and at the 1.05-1.6 M sucrose interfaces, respectively. Electron microscopic analysis showed that fraction IIB contained synaptosomes and extra terminal mitochondria and was essentially free of membrane fragments. Further characterization showed that IIB contained 69% of the protein and 83% of the lactic dehydrogenase activity of fraction II and had a specific activity of a 2',3'-cyclic nucleotide 3'-phosphohydrolase approximately 1% of that obtained with myelin. Fraction IIA had approximately 50% the specific activity of the 2',3'-cyclic nucleotide 3'-phosphohydrolase found in myelin. Synaptic plasma membranes were prepared by lysing fraction IIB in 1 mM sodium phosphate, 0.1 mM EDTA at pH 8.5 and subjecting this preparation to centrifugation on a discontinuous sucrose density gradient. Enzymatic analysis indicated that membranes banding at the 0.6-0.8 M sucrose interface had high specific activities of plasma membrane enzymes (e.g. acetylcholinesterase, ATPase, 5'-nucleotidase). The specific activity of the (Na+ + K+)-ATPase in the purified membrane preparation was 8-fold higher than that in the original homogenate. Specific activities of various marker enzymes indicated that the composition of these membrane preparations for the most part was synaptic plasma membranes, approximately 7% mitochondrial outer membranes and 3% a membrane containing 2',3'-cyclic nucleotide 3'-phosphohydrolase activity. The polypeptide compositions of three possible contaminating membranes and of synaptic membranes were compared by electrophoresis in 6-20% gradient polyacrylamide gels in the presence of sodium dodecyl sulfate. Whereas mitochondrial and myelin membranes had distinct compositions, the compositions of the microsomal and synaptosomal plasma membranes were similar. Synaptic plasma membranes contained at least 27 polypeptides; the three major polypeptides had molecular weights of 103,000; 54,000; and 50,000. The major polypeptides of soluble synaptosomal proteins had molecular weights of 54,000 and 42,000.
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PMID:An improved method of preparing rat brain synaptic membranes. Elimination of a contaminating membrane containing 2',3'-cyclic nucleotide 3'-phosphohydrolase activity. 624 53

L-3,5,3'-Triiodothyronine (T3) has been shown to influence the synthesis of myelin-associated lipids in cultures of cells dissociated from brains of embryonic mice (Bhat, N. R., Sarlieve, L., Subba Rao, G., and Pieringer, R. A. (1979) J. Biol. Chem. 254, 9342-9344). This culture system was used in the present study to gain additional information on the regulation of the synthesis of myelin lipids by thyroid hormone. The rate of synthesis of the myelin associated sulfolipids remained drastically diminished throughout a 70-day developmental period when cells were grown in the presence of hypothyroid calf serum (T3 < 25 ng/100 ml; thyroxine (T4), 1.2 microgram/ml). However, the activity could be restored to normal levels after 72 h of exposure to deficient medium supplemented with exogenous T3. Half-maximal effects were obtained with 2 X 10(-9) M T3 and 6.25 X 10(-7) M T4. T3 does not alter the synthesis of sulfated mucopolysaccharides, which share adenosine 3'-phosphate, 5'-phosphosulfate (PAPS), as a common precursor, with sulfolipids. This observation argues against the hormone altering the entry of sulfate or the synthesis of PAPS. Rather, T3 acts by changing the activity of the glycolipid:PAPS sulfotransferase(s) in direct proportion to the concentration of T3 in the growth medium. The activity of 2',3'-cyclic nucleotide 3'-phosphohydrolase, another myelin marker was also found to be T3 dependent. The response of sulfolipid synthesis to varying amounts of T3 was also observed in a serum-free medium, which suggests that T3 can function independently of other hormones and serum factors in exerting a relatively specific effect on the regulation of myelination.
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PMID:Investigations on myelination in vitro. Regulation of sulfolipid synthesis by thyroid hormone in cultures of dissociated brain cells from embryonic mice. 625 88

2',3'-Cyclic nucleotide 3'-phosphohydrolase (nucleoside-2':3'-cyclic-phosphate 2'-nucleotidohydrolase, EC 3.1.4.37) activity has been demonstrated in rat liver mitochondria. The enzyme was localized in both the outer and inner mitochondrial membranes but was absent from the intermembrane space and matrix. The mitochondrial (cyclic nucleotide) phosphohydrolase was activated by freezing and thawing and by treatment with digitonin or detergents. It is suggested that (cyclic nucleotide) phosphohydrolase is an integral membrane protein which is buried to a significant degree within the membrane. Atractyloside was found to be a noncompetitive inhibitor of the enzyme both in intact mitochondria and in preparations of the mitochondrial membranes. The enzyme substrate, 2',3'-cyclic adenosine monophosphate, had no effect on the oxidation of exogenous beta-hydroxybutyrate or succinate by intact mitochondria. These findings suggest that 2',3'-cyclic nucleotide 3'phosphohydrolase is more widely distributed than was previously thought and that the enzyme may play a fundamental role in membranes, independent of their specialized structure or functions.
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PMID:2',3'-cyclic nucleotide 3'-phosphohydrolase in rat liver mitochondrial membranes. 626 Jan 66

Chronic ethanol ingestion induced a 47% increase in the specific activity of 2',3'-cyclic nucleotide 3'-phosphohydrolase (nucleoside-2':3'-cyclic-phosphate 2'-nucleotidohydrolase, EC 3.1.4.37) in whole mitochondria. Both inner and outer mitochondrial membranes showed increased (cyclic nucleotide)phosphohydrolase activity, but the inner was increased 94% compared to 67% for the outer. Techniques which disrupt membrane structure increased (cyclic nucleotide)phosphohydrolase activity. After these treatments, whole mitochondria from ethanol-treated animals still showed a 50% increase in activity. This increase may be related either to an inherent increase in the resistance of (cyclic nucleotide)phosphohydrolase to protein degradation or turnover, or to ethanol-induced membrane changes. An increase in (cyclic nucleotide)phosphohydrolase reaction medium pH was observed when freshly isolated, highly-coupled mitochondria were used. The total increase in pH was about 2-fold greater in the controls compared to the ethanol-treated mitochondria. It is suggested that the smaller initial increase in pH and the greater activity of (cyclic nucleotide)phosphohydrolase in the mitochondria from the ethanol-treated animals relate to previously observed changes in the lipid and protein composition of the mitochondrial membranes. In addition, (cyclic nucleotide)phosphohydrolase may represent an excellent marker for membrane integrity.
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PMID:Effects of chronic ethanol ingestion on the activity of rat liver mitochondrial 2',3'-cyclic nucleotide 3'-phosphohydrolase. 626 Jan 67


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