Disease relevance of Urod

• Females developed a massive porphyria, due to depression of uroporphyrinogen decarboxylase activity, whereas males did not [1].
• The quantitative analysis of the metabolites of 2-deoxy-D-galactose demonstrated the predominance of the monophosphate and the negligible formation of UPD derivatives of this sugar analog in AS-30D hepatoma cells [2].
• Uroporphyrinogen decarboxylase deficiency in experimental chronic hepatic porphyria [3].

High impact information on Urod

• We have cloned and identified a DNA sequence complementary to the mRNA of uroporphyrinogen decarboxylase ( UroDCase ) from rat [4].
• Differential gene expressions of selenoprotein W and uroporphyrinogen decarboxylase, which can be involved in oxidative stress, were also observed [5].
• Studies on porphyrin metabolism in the kidney. Effects of trace metals and glutathione on renal uroporphyrinogen decarboxylase [6].
• Inhibition of the haem biosynthesis enzyme uroporphyrinogen decarboxylase (UD) only occurred in the liver of females treated with HCB or DEN/HCB [7].
• 6. Rats treated with cycloheximide for 10h showed no decrease in uroporphyrinogen decarboxylase activity/mg of protein, suggesting a relatively slow turnover of the enzyme [8].

Chemical compound and disease context of Urod

• Hexachlorobenzene (HCB) induces a porphyria characterized by a diminished activity of the enzyme uroporphyrinogen decarboxylase (URO-D), presumably due to inactivation by reactive metabolites of HCB [9].
• Activation of uroporphyrinogen decarboxylase by ferrous iron in porphyria cutanea tarda [10].
• The decrease in uroporphyrinogen decarboxylase activity induced by ethanol predisposes rats to the development of porphyria and accelerates xenobiotic-triggered porphyria, regardless of hepatic damage [11].

Biological context of Urod

• Decarboxylation of porphyrinogens by rat liver uroporphyrinogen decarboxylase [12].
• Individual phospholipid content, [32P] incorporation, total lipid content, lipid peroxidation, uroporphyrinogen decarboxylase activity, its inhibitor generation and porphyrin content, were the parameters measured in the liver of treated rats [13].
• Enzyme kinetics indicate that uroporphyrinogen decarboxylase reversibly binds ferrous iron, with a binding constant of approximately 5 x 10(4) mol-1 [10].

Anatomical context of Urod

• Level of immunoreactive UROD in cytosol of porphyric rats was not modified by HCB [14].
• Comparison between crab hepatopancreas and rat liver uroporphyrinogen decarboxylase [15].

Associations of Urod with chemical compounds

• Increased inhibition of hepatic uroporphyrinogen decarboxylase by hexachlorobenzene in male rats given the oestrogenic drugs diethylstilboestrol and chlorotrianisene [16].
• During this time the allosteric activator, UDP-N-acetylglucosamine, lost its effect whereas the inhibitor UPD showed greater inhibitory properties, thus counteracting the activation [17].
• Combined treatment with ethinyl estradiol plus iron partially corrected the reduction of BSIF and restored the activity of ALA-S and URO-D to control levels [18].
• The effects of ethanol, estrogen, and hexachlorobenzene on the activities of hepatic delta-aminolevulinate synthetase, delta-aminolevulinate dehydratase, and uroporphyrinogen decarboxylase in male rats [19].
• Chlorophenolic and sulfur-containing metabolites of HCB incubated with GSH-free rat liver cytosolic protein drastically diminished the UROD activity [20].

Other interactions of Urod

• We investigated the effects of ethinyl estradiol (5 mg/kg body wt daily for 5 days, orally) and/or iron sorbitol (50 mg/kg body wt daily for 5 days, i.m.) on bile flow, bile salt independent fraction (BSIF), hepatic delta-aminolevulinate synthase (ALA-S) and uroporphyrinogen decarboxylase (URO-D) in female rats [18].

Analytical, diagnostic and therapeutic context of Urod

• The determination of uroporphyrinogen decarboxylase in tissues by high-performance liquid chromatography coupled to fluorescence detection [21].
• It is proposed that the effect of phlebotomy on patients with porphyria cutanea tarda is to mobilze storage iron in the liver to the active ferrous form, which activates hepatic uroporphyrinogen decarboxylase, the enzyme which is defective in this syndrome, with resultant clinical and biochemical remission [10].

References