Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Several species of protozoan parasites of the family Trypanosomatidae have a surface membrane-associated enzyme which is capable of hydrolyzing extracellular 3'-nucleotides and nucleic acids, thereby aiding in the acquisition of nutritionally required purines and Pi from their hosts. In Crithidia luciliae, this 3'-nucleotidase/nuclease previously has been shown to be highly regulated as purine and/or Pi starvation of this trypanosomatid leads to as much as a 1000-fold increase in enzyme activity. We have purified the enzyme to apparent homogeneity from detergent extracts of purine-starved C. luciliae by heparin-agarose chromatography followed by Mono Q and Mono S fast protein liquid chromatography. The enzyme had an apparent molecular weight of 43,000 and a pI of approximately 5.8. The enzyme displayed broad pH optima, with peaks at 8.0, for both nucleotidase and nuclease activities. The pH optima shifted to lower values when the activity was assayed in the presence of sulfhydryl reagents. The enzyme was most active with 3'-AMP and poly(A) in nucleotidase and nuclease assays, respectively. As a nuclease the enzyme hydrolyzed RNA at a faster rate than single-stranded DNA with no detectable hydrolysis of double-stranded DNA. The loss of enzyme activity which occurred upon storage at acid pH was prevented by the inclusion of Zn2+ in storage buffers. The physicochemical and kinetic properties of this trypanosomatid enzyme suggest that it is similar to the class I nucleases found in fungi and in germinating seedlings of higher plants.
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PMID:An inducible 3'-nucleotidase/nuclease from the trypanosomatid Crithidia luciliae. Purification and characterization. 215 95

The rates of glycolysis and glycogenolysis an the rate of lactate formation from glucoso-6-phosphate (G-6-Ph) in the liver were reduced during stress (starvation). On the contrary, these activities in the adrenals were increased. The rates of lactate formation from fructose diphosphate remained unchanged in both organs. The results obtained attest to the inhibition in the liver and activation in the adrenals of phosphorylase, hexokinase and phosphofructokinase. The degree of hexokinase inhibition in the liver depended on the presence of cAMP, ATP and MgCl2 in the incubation medium and was a consequence of enzymatic phosphorylation. Unlike 2', 3'-AMP, the inhibitory effect of CAMP was highly specific. The protein inhibitor of protein kinase completely reversed the inhibitory effect of cAMP on hexokinase. In the adrenals, cAMP slightly increased the rates of glycolysis and lactate formation from G-6-Ph because of allosteric effects of cAMP. The activation rather than inhibition of glycolysis in the adrenals during stress is probably caused by the absence in this tissue of cAMP-dependent protein kinase which phosphorylates hexokinase.
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PMID:[Effect of cAMP of glycolysis and glycogenolysis in the liver and adrenals of white rats]. 627 Dec 95