Disease relevance of Gulo

• In this study we isolated the L-gulono-gamma-lactone oxidase gene of the rat and the homologue of this gene of the guinea pig by screening rat and guinea pig genomic DNA libraries in lambda phage vectors, respectively, using a rat L-gulono-gamma-lactone oxidase cDNA as a probe [1].
• Catalytically-active enzyme was expressed in silkworm cells by a recombinant baculovirus encoding rat L-gulono-gamma-lactone oxidase [2].
• Groups of 10 male and 10 female Sprague-Dawley rats were administered dermally coal coprocessing products (light gas oil, LGO; heavy gas oil I, HGOI; heavy gas oil II, HGOII) at 1 g/kg body weight/d for 14 d [3].
• Significant increases of ascorbic acid levels and L-gulonolactone oxidase was observed with malathion toxicity [4].
• The effect of riboflavin deficiency on the activity of L-gulonolactone oxidase [L-gulono-gamma-lactone: oxygen 2-oxidoreductase, EC 1.1.3.8] and on vitamin C status was studied [5].

High impact information on Gulo

• Cloning and chromosomal mapping of the human nonfunctional gene for L-gulono-gamma-lactone oxidase, the enzyme for L-ascorbic acid biosynthesis missing in man [6].
• Sequencing analysis indicated that the isolated segment represented a 3'-part of the gene, where the regions corresponding to exons VII, IX, X, and XII of the rat L-gulono-gamma-lactone oxidase gene remain with probable deletion of the regions corresponding to exons VIII and XI [6].
• In the present study, we isolated a segment of the nonfunctional L-gulono-gamma-lactone oxidase gene from a human genomic library, and mapped it on chromosome 8p21.1 by spot blot hybridization using flow-sorted human chromosomes and fluorescence in situ hybridization [6].
• Thus it is clear that the guinea pig homologue of the L-gulono-gamma-lactone oxidase gene exists as a pseudogene that randomly accumulated a large number of mutations without functional constraint since the gene ceased to be active during evolution [1].
• To test the effect of this mutation on the expression of L-gulono-gamma-lactone oxidase, we inserted a region of the cDNAs coding for normal and mutant L-gulono-gamma-lactone oxidases into an expression vector, pSVL, and transfected COS-1 cells with such vectors [7].

Chemical compound and disease context of Gulo

• Production by a baculovirus expression system of the APO-protein of L-gulono-gamma-lactone oxidase, a flavoenzyme possessing a covalently-bound FAD [2].

Biological context of Gulo

• On the other hand, regions corresponding to exons I and V were not identified in the guinea pig L-gulono-gamma-lactone oxidase gene homologue [1].
• Sequence analysis study indicated that the human L-gulono-gamma-lactone oxidase gene has accumulated a large number of mutations since it stopped being active and that it now exists as a pseudogene in the human genome [8].
• A missense mutation of L-gulono-gamma-lactone oxidase causes the inability of scurvy-prone osteogenic disorder rats to synthesize L-ascorbic acid [7].
• The expression plasmid pSVL-GLO, carrying rat liver L-gulono-gamma-lactone oxidase cDNA, was microinjected into the cytoplasm of fertilized eggs during the one-cell stage [9].
• Four male F0 fish having the transgene in their germ cells came to maturity, and F1 progeny derived from one of the F0 fish possessed L-gulono-gamma-lactone oxidase activity, indicating that the transgene was functionally expressed in the fish [9].

Anatomical context of Gulo

• Purification and characterization of L-gulonolactone oxidase from chicken kidney microsomes [10].
• Ascorbate synthesizing activity in the follicle was demonstrated by detecting the enzyme L-gulono-gamma-lactone oxidase in microsomes prepared from granulosa cells [11].
• The present results suggest that the reaction mechanism of this enzyme is different from that of L-gulono-gamma-lactone oxidase (EC 1.1.3.8) isolated from rat liver microsomes [12].
• The influences of chronic deficiency of L-ascorbic acid (AsA) on the differentiation of osteo-chondrogenic cells and the process of endochondral ossification were examined in the mandibular condyle and the tibial epiphysis and metaphysis by using Osteogenic Disorder Shionogi (ODS) rats that bear an inborn deficiency of L-gulonolactone oxidase [13].
• Firstly, the existence of GLO mRNA was examined in the liver, kidney, lung, small intestine, spleen, testis, and prostate from a male rat; and GLO mRNA was found to be present only in the liver, in which GLO activity was also detected [14].

Associations of Gulo with chemical compounds

• Isolation and sequence analysis of a complementary DNA encoding rat liver L-gulono-gamma-lactone oxidase, a key enzyme for L-ascorbic acid biosynthesis [15].
• L-gulono-gamma-lactone oxidase is the enzyme responsible for the production of methylguanidine in the rat liver [16].
• Detection of L-gulono-gamma-lactone oxidase on SDS-polyacrylamide gels by the fluorescence of its covalently bound flavin [17].
• The dietary addition of 200 ppm PCB, 500 ppm DDT, 2,000 ppm pentobarbital or 3,000 ppm chloretone caused a significant increase in the activity of hepatic UDPglucose dehydrogenase, but did not affect the activity of hepatic L-gulonolactone oxidase [18].
• As with man, monkey and the guinea pig, this rat lacks L-gulonolactone oxidase necessary for the synthesis of AA from glucose [19].

Analytical, diagnostic and therapeutic context of Gulo

• Northern blot hybridization using this cDNA as a probe demonstrated that guinea pigs lack mRNA for L-gulono-gamma-lactone oxidase [20].
• Castration caused a decrease in the activities of such biosynthetic enzymes as L-gulono-gamma-lactone oxidase and D-glucuronolactone-delta-hydrolase with no significant alteration in the activity of L-gulono-gamma-lactone hydrolase in the rat prostate [21].

References