Porphyrins and porphyrinogen carboxy-lase in hexachlorobenzene-induced porphyria. 1977

L C San Martín De Viale, and M D Ríos De Molina, and R W De Calmanovici, and J M Tomio

1. Qualitative and quantitative studies of the porphyrins and the porphyrinogen carboxylyase of the liver, spleen, kidney, harderian gland and erythrocytes from normal rats and from those hexachlorobenzene-induced porphyria were carried out. 2. Hexachlorobenzene has no effect on erythrocyte porphyrin content, but produces a decrease in that of Harderian gland and an increase in the porphyrin content of the kidney and spleen, and a marked increase in the liver (1 mumol/g of tissue). Octacarboxylic (isomer III) and heptacarboxylic porphyrins accumulated in kidney, spleen and liver, the former porphyrin being predominant. 3. Hexachlorobenzene has no effect on the activity of porphyrinogen carboxy-lase in erythrocytes; there is a slight decrease in enzyme activity in the Harderian gland, and a marked decrease in the liver and kidney enzyme activities. In the liver the removal of each carboxyl group from uroporphyrinogen III appears to be affected by this treatment. 4. The liver is the principal site of action of hexachlorobenzene, with the kidney next in decreasing order of effect, and erythropoietic tissue is unaffected. The marked decrease in porphyrinogen carboxy-lyase activities observed in liver and kidney could explain the high accumulation of octacarboxylic and heptacarboxylic porphyrins found in these tissues. 5. The results are discussed in relation to changes promoted by hexachlorobenzene in other enzymes of the haem pathway.

UI MeSH Term Description Entries
D011164 Porphyrias A diverse group of metabolic diseases characterized by errors in the biosynthetic pathway of HEME in the LIVER, the BONE MARROW, or both. They are classified by the deficiency of specific enzymes, the tissue site of enzyme defect, or the clinical features that include neurological (acute) or cutaneous (skin lesions). Porphyrias can be hereditary or acquired as a result of toxicity to the hepatic or erythropoietic marrow tissues. Porphyria,Porphyrin Disorder,Disorder, Porphyrin,Disorders, Porphyrin,Porphyrin Disorders
D011166 Porphyrins A group of compounds containing the porphin structure, four pyrrole rings connected by methine bridges in a cyclic configuration to which a variety of side chains are attached. The nature of the side chain is indicated by a prefix, as uroporphyrin, hematoporphyrin, etc. The porphyrins, in combination with iron, form the heme component in biologically significant compounds such as hemoglobin and myoglobin. Porphyrin
D002262 Carboxy-Lyases Enzymes that catalyze the addition of a carboxyl group to a compound (carboxylases) or the removal of a carboxyl group from a compound (decarboxylases). EC 4.1.1. Carboxy-Lyase,Decarboxylase,Decarboxylases,Carboxy Lyase,Carboxy Lyases
D002850 Chromatography, Gel Chromatography on non-ionic gels without regard to the mechanism of solute discrimination. Chromatography, Exclusion,Chromatography, Gel Permeation,Chromatography, Molecular Sieve,Gel Filtration,Gel Filtration Chromatography,Chromatography, Size Exclusion,Exclusion Chromatography,Gel Chromatography,Gel Permeation Chromatography,Molecular Sieve Chromatography,Chromatography, Gel Filtration,Exclusion Chromatography, Size,Filtration Chromatography, Gel,Filtration, Gel,Sieve Chromatography, Molecular,Size Exclusion Chromatography
D005260 Female Females
D006581 Hexachlorobenzene An agricultural fungicide and seed treatment agent. HCB
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D014018 Tissue Distribution Accumulation of a drug or chemical substance in various organs (including those not relevant to its pharmacologic or therapeutic action). This distribution depends on the blood flow or perfusion rate of the organ, the ability of the drug to penetrate organ membranes, tissue specificity, protein binding. The distribution is usually expressed as tissue to plasma ratios. Distribution, Tissue,Distributions, Tissue,Tissue Distributions
D014575 Uroporphyrinogen Decarboxylase An enzyme that catalyzes the decarboxylation of UROPORPHYRINOGEN III to coproporphyrinogen III by the conversion of four acetate groups to four methyl groups. It is the fifth enzyme in the 8-enzyme biosynthetic pathway of HEME. Several forms of cutaneous PORPHYRIAS are results of this enzyme deficiency as in PORPHYRIA CUTANEA TARDA; and HEPATOERYTHROPOIETIC PORPHYRIA. Uroporphyrinogen Carboxy-Lyase,Uroporphyrinogen III Decarboxylase,Carboxy-Lyase, Uroporphyrinogen,Decarboxylase, Uroporphyrinogen,Decarboxylase, Uroporphyrinogen III,Uroporphyrinogen Carboxy Lyase
D014577 Uroporphyrinogens Porphyrinogens which are intermediates in heme biosynthesis. They have four acetic acid and four propionic acid side chains attached to the pyrrole rings. Uroporphyrinogen I and III are formed from polypyrryl methane in the presence of uroporphyrinogen III cosynthetase and uroporphyrin I synthetase, respectively. They can yield uroporphyrins by autooxidation or coproporphyrinogens by decarboxylation. Uroporphyrinogen III

Related Publications

L C San Martín De Viale, and M D Ríos De Molina, and R W De Calmanovici, and J M Tomio
January 1986, IARC scientific publications,
L C San Martín De Viale, and M D Ríos De Molina, and R W De Calmanovici, and J M Tomio
April 1990, Biulleten' eksperimental'noi biologii i meditsiny,
L C San Martín De Viale, and M D Ríos De Molina, and R W De Calmanovici, and J M Tomio
May 1986, The Biochemical journal,
L C San Martín De Viale, and M D Ríos De Molina, and R W De Calmanovici, and J M Tomio
January 1986, IARC scientific publications,
L C San Martín De Viale, and M D Ríos De Molina, and R W De Calmanovici, and J M Tomio
January 1986, IARC scientific publications,
L C San Martín De Viale, and M D Ríos De Molina, and R W De Calmanovici, and J M Tomio
February 1978, Biochemical and biophysical research communications,
L C San Martín De Viale, and M D Ríos De Molina, and R W De Calmanovici, and J M Tomio
September 1990, Biochemical pharmacology,
L C San Martín De Viale, and M D Ríos De Molina, and R W De Calmanovici, and J M Tomio
June 1965, The Journal of investigative dermatology,
L C San Martín De Viale, and M D Ríos De Molina, and R W De Calmanovici, and J M Tomio
March 1973, The Medical journal of Australia,
L C San Martín De Viale, and M D Ríos De Molina, and R W De Calmanovici, and J M Tomio
February 1973, The Medical journal of Australia,
Copied contents to your clipboard!