H A Sancovich

Buenos Aires Ciudad, Buenos Aires, Buenos Aires F.D., Argentina

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Publications (39)75.6 Total impact

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    ABSTRACT: These studies try to elucidate why isocoproporphyrin appears in hexachlorobenzene-poisoned rats' feces. Chronic exposure of hexachlorobenzene to rats produces an experimental model for human porphyria cutanea tarda. After 8 weeks of treatment, rats showed high porphyrin excreta and 50% inhibition of liver uroporphyrinogen decarboxylase activity. Uroporphyrin plus heptacarboxylic porphyrin exceeded coproporphyrin in urine, whereas in feces, isocoproporphyrin, from abnormal pentacarboxylic porphyrinogen III oxidative decarboxylation by liver coproporphyrinogen oxidase, became the main porphyrin. Trypsin-treated mitochondria showed that the outer and inner membrane permeability barrier was highly conserved after hexachlorobenzene intoxication. In digitonin-treated hexachlorobenzene mitochondria, coproporphyrinogen oxidase was free in the mitochondrial intermembrane space, whereas in normal mitochondria, 30% to 50% remained anchored to the inner membrane. Hexachlorobenzene led to a decrease in respiratory control and ADP/O ratios (uncoupled mitochondria). Albumin restored oxidative phosphorylation, indicating no irreversible inner membrane damage. Normal and hexachlorobenzene mitochondria oscillatory studies exhibited similar damping factor values, showing that hexachlorobenzene had no significant effect on membrane fluidity and elasticity. Mitochondrial uncoupling could explain the free state of the enzyme within the intermembrane space. The free state of the enzyme makes it more flexible and would allow pentacarboxylic porphyrinogen III, whose levels are increased, to compete with coproporphyrinogen III and being transformed into dehydroisocoproporphyrinogen, the liver forerunner of fecal isocoproporphyrin.
    No preview · Article · Dec 2008 · International Journal of Toxicology

  • No preview · Article · Mar 2007
  • A M Ferramola de Sancovich · H A Sancovich

    No preview · Article · Jun 2006
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    ABSTRACT: ALA-D (EC is the first cytosolic enzyme in the haem metabolic pathway. Some metals compete with its major cofactor Zn(2+), modifying both enzyme structure and function. Our purpose was to contribute to the understanding of the biochemical role of metals such as Pb(2+), Cd(2+), Cu(2+), Mg(2+), Zn(2+), Na(+), K(+) and Li(+) on ALA-D, using chicken embryos as experimental model. Mg(2+) and Zn(2+) showed enzyme activation in yolk sac membrane (YSM) (113% at 10(-5) M Mg(2+) and from 10(-4) M Zn(2+)), and slight inactivation in liver. Cd(2+) and Cu(2+) caused a non allosteric inhibition in both tissues (100% from 10(-4) M). Surprisingly Pb(2+) was not such a strong inhibitor. Interference of cations during the Schiff base formation in enzymatic catalysis process is explained considering their Lewis acid-base capacity, coordination geometry and electron configuration of valence. Interactions among monovalent cations and biochemical substances are governed chiefly by its electrostatic potential. 0.1 M K(+) and 0.4 M Na(+) produced 30% of enzymatic inhibition by the interference on interactions among the functional subunits. Li(+) activated the YSM enzyme (130% at 10(-5) M) due to a more specific interaction. This study may contribute to elucidate for the first time the possible structural differences between the YSM and liver enzymes from chicken embryo.
    No preview · Article · Mar 2005 · Journal of Inorganic Biochemistry
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    ABSTRACT: The chick embryo has been used as a screening system to study porphyrin metabolism, and the toxicological and teratogenic effects of many chemical substances. The aim of this study is to evaluate Cd 2+, Pb 2+, and Cu 2+ teratogenicity; and in vivo effects on chick embryo of d-aminolevulinic acid dehydratase (ALA-D) and porphobilinogen deaminase (PBG-D) activities. On day 12 of incubation, White Leghorn eggs were injected in the yolk with cadmium acetate, lead acetate, or copper sulfate in two different doses. The yolk sac membrane and liver were removed 12 and 60 hours later and ALA-D and PBG-D activities assayed. The in vivo Cd 2+ administration in chick embryo induced higher mortality rate and teratogenic effects than Pb 2+ and Cu 2+. The different effects observed on the enzyme activities can be better explained by both (a) differences in metals' capacity to cross the vitelline membrane, and (b) a secondary effect of alterations in general mineral metabolism, more than as a result of direct action on the enzymes themselves. Our results are the first to show that yolk sac membrane enzymes are more sensible than liver enzymes to the action of the metals used in our studies. These findings indicate that the yolk sac membrane is the preferential tissue to be used for metal biomarker toxicity assays.
    No preview · Article · Jul 2004 · Revista Argentina de Dermatologia
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    ABSTRACT: In the present study, the effects of hexachlorobenzene (HCB) on epidermal growth factor receptor (EGFR) content of liver microsomes and plasma membrane, and on EGFR-tyrosine kinase activity in the microsomal fraction were investigated. In addition, we studied the parameters of the tyrosine kinase signalling pathway such as protein tyrosine kinase (PTK) activity and phosphotyrosine content in microsomal and cytosolic protein. To determine whether the observed alterations were correlated with a manifestation of overt toxicity, a single very low dose of HCB (1mg/kg body wt) and two much higher doses (100 and 1000 mg/kg body wt), the highest being toxicologically significant in that it reduced serum thyroxine (T(4)) and inhibited uroporphyrinogen decarboxylase (URO-D) (EC activity, were tested. Our results demonstrated that liver microsomes of rats treated with HCB had higher levels of EGFR than untreated rats; treated rats also had less EGFR present in hepatocyte plasma membrane fractions than did untreated rats. HCB altered the phosphotyrosine content and protein phosphorylation of some microsomal and cytosolic proteins in a biphasic dose-response relationship. At the low dose, phosphorylation and phosphotyrosine content of several microsomal proteins were increased; however, these effects were diminished or reversed at the higher doses. Our results suggest that chronic HCB treatment produces a down-regulation of the EGFR and a dose-dependent increase in EGFR-tyrosine kinase activity in the microsomal fraction. This effect may contribute to the alteration of membrane and cytosolic protein tyrosine phosphorylation. The level of sensitivity encountered in our studies is extraordinary, occurring at 1/10 to 1/1000 the doses of HCB known to cause other toxicological lesions.
    No preview · Article · Jun 2003 · Biochemical Pharmacology
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    ABSTRACT: 1. Chick embryos of 7, 9, 11, 12, 13, 14, 15, 17 and 19 d of embryonic development were examined to determine the activities of 5-aminolevulinic dehydratase (ALA-D, EC and porphobilinogen deaminase (PBG-D, EC 2. Liver and yolk sac membrane ALA-D specific activities showed a maximum between 12 and 13 d of embryonic development, yolk sac membrane PBG-ase activity a maximum at 9 d and at 7 d in liver. Total activities of ALA-D and PBG-D were not constant during the course of embryonic development but probably related to the changes of intensity of haem synthesis. 3. ALA-D and PBG-ase activities were higher in yolk sac membrane than in liver, showing the importance of the yolk sac membrane as erythropoietic tissue. PBG-D catalysed the rate-limiting reaction of the cytosolic steps in the biosynthetic pathway in both tissues.
    No preview · Article · Jun 2002 · British Poultry Science
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    ABSTRACT: One of the main sites of haem synthesis and erythropoiesis in the bird embryo is the yolk sac membrane (YSM), which appears on the fifth day of development. A further site of haem production is the liver. Delta Aminolevulinic acid dehydratase (ALA-D) specific activity was determined both in the liver and in the YSM, and a maximun at 12 days of development (ED), was found. Lower enzyme activity was detected in the liver than in the YSM under the same conditions. In the liver, total enzyme activity, total protein content and the organ weight varied accordingly to the rate of growth and to changes in the general metabolism. In the YSM total enzyme activity showed a maximun between the 12th and 13th ED, decreasing during the last week. Total protein content remains almost constant along the period studied. An increase of the wet mass of the YSM was registered with embryo development, perhaps due to the structural changes in the YSM walls and to the growing amounts of adherent yolk materials which makes it more difficult to remove the yolk. The dry mass presented similar variations, though it can be clearly noticed that there is an important loss of dry mass from the 17th ED to the 19th ED, which is due to its retraction into the embryo's body while it looses functionality near the end of development. ALA-D optimum pH was 6,8 for both tissues, but they presented differences in thermoestability. YSM ALA-D resulted more thermostable than the liver enzyme, as can be seen from their activation energy values. This property of YSM enzyme was enhanced by protecting the active site or by maintaining sulphydrilic groups reduced. Kinetics studies showed ALA-D like a Michaelis-Menten enzyme. YSM ALA-D presented higher affinity for the substrate than liver enzyme. All these studies will be useful in correlating data with porphyrinogenic drugs between chick embryo and rat liver. In turn, these results will be useful in mediating porphyrinogenic effects of drugs in human liver.
    No preview · Article · Apr 2001 · Revista Argentina de Dermatologia
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    ABSTRACT: Hexachlorobenzene (HCB) is a dioxin-type chemical that acts mainly through the aryl hydrocarbon receptor. Chronic exposure of rats to HCB increases the activity of malic enzyme (ME). In this report, we show that this increase is correlated with an induction of ME messenger RNA (mRNA) levels, with the maximal HCB effect achieved after 9 days of intoxication. This effect is specific for ME, as other liver enzymes, such as glyceraldehyde-3-phosphate dehydrogenase, phosphoenol pyruvate carboxykinase, and mitochondrial alpha-glycerol-3-phosphate dehydrogenase, are not affected by HCB. The induction of ME mRNA levels is accompanied by an increase in ME promoter activity, as demonstrated by transient transfection experiments performed in rat hepatoma H35 cells. In an attempt to identify the cis-regulatory elements responsible for the HCB effect, different promoter deletions and mutations were used. The results obtained localize the responsive region between positions -315 and -177. This region does not contain either consensus xenobiotic response or activating protein-1 elements, the two main mediators of dioxin compounds described to date. In contrast, a thyroid hormone response element (TRE) is located between -281 to -261. Deletions and mutations of the TRE element do not respond to HCB, demonstrating that this element mediates the response of this dioxin-type compound. As ME gene expression is regulated mainly by thyroid hormones, we next investigated the role of T3 receptor (T3R) in the ME gene transcriptional induction mediated by HCB. Using Scatchard analysis, we show that neither T3R binding features for its ligand nor alpha1 or beta1T3R mRNA levels are changed with the toxic. In gel shift assays, however, we observed that protein/DNA complexes formed on TRE from the ME promoter were induced by HCB. Using an oligonucleotide with a mutation that eliminates the TRE function, we demonstrate a loss of the induced protein/DNA complexes. Together, these data suggest that the dioxin-type compound HCB increases ME gene transcription by modulating the levels of still unidentified nuclear proteins that bind to the TRE element of the ME promoter.
    Preview · Article · Oct 1999 · Endocrinology
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    ABSTRACT: The time and dose-dependent effects of the in vivo administration of hexachlorobenzene (HCB), on hepatic microsomal membrane functions, were studied in female Wistar rats. Administration of HCB (100 mg/100 g b.w.) resulted in time-dependent decreases in the activity of two membrane-bound enzymes: 5'nucleotidase and Na+/K+ ATPase. HCB was found to cause a significant rise in protein tyrosine kinase (PTK) activity during the early stages of intoxication (day 2), followed by a significant decrease at 10 days, returning to control levels after 20 days of treatment. A stimulatory effect of HCB on in vitro endogenous microsomal protein phosphorylation was observed from 2 days of intoxication up to 30 days of treatment, with an important stimulation of phosphorylation at 5 days. Administration of HCB (100 mg/100 g b.w.) for 10 days caused a 50% reduction in epidermal growth factor receptor (EGF-R) ligand binding. The effects of known specific inhibitors of protein phosphatases on endogenous protein phosphorylation were studied. HCB affected the labelling of several bands, as well as the 5'nucleotidase and PTK activities, in a dose-dependent manner. In conclusion, this study indicated that the in vivo administration of HCB results in a significant alteration of membrane function.
    No preview · Article · Mar 1998 · Toxicology
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    ABSTRACT: Hexachlorobenzene (HCB) is a widespread environmental pollutant. Chronic exposure of laboratory animals to HCB triggers porphyria, induction of liver microsomal enzymes, low levels of T4 reproductive dysfunction's, liver and thyroid tumors. Previous findings from our laboratory have shown that HCB increased the activity of the liver thyroid-responsive enzymes: malic enzyme (ME), glucose-6-phosphate dehydrogenase (G6PD) without any change in the mytochondrial alpha-glycerophosphate dehydrogenase (alpha-GPD). In this study we have demonstrated that HCB treatment increased ME mRNA. We also have investigated if HCB affected: a) the thyroid hormone receptor (TR) concentration and binding affinity for its ligands, b) specifically the ME gene expression, or other thyroid hormone responsive enzymes were affected as well, c) Protein/DNA complex formed on the thyroid responsive element (TRE). Livers from female Wistar rats intoxicated with HCB (100 mg/100 g b.w.), for 9 and 15 days, were analyzed. Northern blot hybridization analysis, have demonstrated that ME mRNA levels increased 4 times and 2 times after 9 and 15 days intoxication respectively, without any alterations in the mRNA levels of other thyroid hormone responsive enzymes such as glyceraldheyde 3- phosphate dehydrogenase, phosphoenolpyruvatecarboxikinase and alpha-GPD. These results suggest that HCB affects specifically, ME gene expression. Hepatic T3 and T4 levels evaluated by RIA were not affected by HCB. Scatchard analyses showed that TR affinity and number of sites were not altered after 9 and 15 days of HCB treatment (control, Ka: 1.9 nM, Bmax 3.9 f/mol 100 micrograms DNA: HCD 9 days Ka: 2.1 nM, Bmax 4.5 fmol/100 micrograms DNA: HCB 15 days Ka 1.9 nM. Bmax 5.1 fmol/100 micrograms DNA intoxication, neither at 9 nor at 15 days. Electrophoresis mobility shift assay showed that HCB did not modify nuclear protein extract affinity for the TREs sequence. Our results suggest that TR itself was not directly involved in the induction of ME gene expression by HCB. Nevertheless TR could interact with other transcription factors in the overexpression of ME gene.
    No preview · Article · Feb 1998 · Acta physiologica, pharmacologica et therapeutica latinoamericana: órgano de la Asociación Latinoamericana de Ciencias Fisiológicas y [de] la Asociación Latinoamericana de Farmacología
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    ABSTRACT: 5-Aminolevulinic acid dehydratase catalyses the self condensation between two molecules of 5-aminolevulinic acid, via a Schiff base, in which a lysine residue at its active site is proposed to be involved. The aim of the work was to further clarify the mechanism of this step in porphobilinogen biosynthesis. 5-Aminolevulinic acid dehydratase was purified 230-fold from pig liver, ε-Aminolysil residues were identified by treating the enzyme with pyridoxal 5-phosphate. Schiff bases formed between either the substrate or pyridoxal 5-phosphate and the enzyme were stabilized by NaBH4 reduction. Levulinate and pyruvate acted as competitive enzyme inhibitors. Pyridoxal 5-phosphate but not pyridoxamine 5-phosphate reversibly inhibited the enzyme activity, in a competitive fashion (Ki = 0.12 mM). After NaBH4 treatment this inhibition became irreversible. The amount of labelled substrate bound to the enzyme after NaBH4 reduction decreased in the presence of either pyridoxal 5-phosphate, levulinate or pyruvate. Enzyme elution profiles from Sephacryl S-300 showed that NaBH4 treatment (1) in absence of substrate, did not induce any change on the enzyme, eluting as a typical 5-aminolevulinic acid dehydratase single peak (Mw 280,000), which overlapped with that of the enzyme activity; and (2) in the presence of labelled 5-aminolevulinate, had an additional peak eluting with a Mw of 140,000, without enzyme activity. This peak coincides in shape and elution volume with the radioactive one. These data suggest that pyruvate regulates pig liver 5-aminolevulinic acid dehydratase activity in vivo and that during catalysis, a tetrameric structure forms the enzyme-substrate complex. The results support the involvement of a critical ε-aminolysil group at the active site of the enzyme.
    No preview · Article · Jan 1996 · The International Journal of Biochemistry & Cell Biology
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    ABSTRACT: The functional thyroid status of hexachlorobenzene (HCB)-treated rats was studied. HCB caused a depletion of serum thyroxine (T4), but did not change L-3,5,3'-triiodothyronine (T3) levels in serum of rats. The activities of the thyroid regulated mitochondrial enzyme L-glycerolphosphate dehydrogenase (LGPD) and cytosolic enzymes, malic enzyme (ME), glucose-6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6PGD) were assayed in livers of normal and HCB (100 mg/100 g bw) treated Wistar rats. Mitochondrial LGPD activity did not change significantly, however ME, 6GPD and G6PD were induced by HCB only in non-thyroidectomized animals. The absence of cytosolic enzymes induction in thyroidectomized rats treated with HCB indicates that HCB is not intrinsically thyromimetic. The induction of hepatic ME, G6PD and 6PGD activities in HCB thyroidectomized rats was dependent on the presence of thyroid hormone. The unchanged activity of mitochondrial LGPD in contrast to the increased activities of the cytosolic enzymes ME, G6PD and 6PGD is not consistent with a shift in functional thyroid status following HCB treatment.
    No preview · Article · May 1995 · Journal of endocrinological investigation
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    ABSTRACT: The role of thyroid status in hexachlorobenzene (HBC) induced porphyria was studied in normal, thyroidectomized and thyroxine (T4) treated rats. Female Wistar rats were treated with HCB for different periods of time. Serum T4 levels were depressed after 8 days of HCB administration whereas levels of triiodothyronine (T3) were not altered. T4 administered simultaneously with HCB resulted in hyperthyroxinemia. The time course of porphyrinogen carboxy-lyase (PCL) activity in the three HBC treated groups was studied. A rapid and significant decrease of PCL activity was found after 8 days of HCB treatment in T4 treated rats with respect to untreated animals. In contrast, HCB treatment of normal and thyroidectomized rats elicited a significant decrease of PCL activity after 21 and 30 days, respectively. This study shows that thyroid hormone plays an important role in the early establishment of HCB induced porphyria.
    No preview · Article · Jun 1994 · Journal of endocrinological investigation
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    ABSTRACT: In the rat liver, the microsomal content of cytochrome P-450 decreased by 50% after triiodothyronine (T3) administration. The molecular basis for the decreased cytochrome P-450 levels was investigated. The activities of the enzymes involved in heme synthesis or degradation were not altered by thyroid hormone administration. The incorporation of 3H-delta-aminolaevulinate into the liver microsomal heme was markedly reduced in T3-treated rats. The latter appeared not to reflect a lowered binding affinity of the apoprotein moiety of cytochrome P-450 for heme. The sodium dodecyl sulfate gel electrophoresis of the microsomal preparation showed a decrease in apocytochrome P-450. It is suggested that the amount of the apocytochrome may be the primary event affected in the formation of cytochrome P-450, by triiodothyronine treatment of thyroidectomized rats.
    No preview · Article · Jun 1991 · Biochimica et Biophysica Acta
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    ABSTRACT: Photoxidation with methylene blue and rose bengal and chemical modification by diethylpryrocarbonate of pig liver 5-aminolevulinic acid dehydratase produced strong inactivation of the enzyme which was concentration dependent. Loss of enzyme activity by both photoxidation and ethoxyformylation was pH and time-dependent and protected by the presence of the substate and competitive inhibitors. The rate of inactivation was directly related to the state of protonation of histidyl groups, the unprotonated from being modified at a much faster rate than the protonated form. Plots of the pseudo-first order rate constants for 5-aminolevulinic acid dehydratase inactivation against pH resulted in typical titration curves showing inflection points at about pH 6.4 for methylene blue and rose bengal and 6.8 for diethylprocarbonate providing further and unequivocal evidence for the existence of critical histidyl groups at the active centre of the enzyme.
    No preview · Article · Feb 1990 · Journal of enzyme inhibition
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    ABSTRACT: The effect of hexachlorobenzene (HCB) (1 g/kg bw) administration for 4 weeks, on thyroxine (T4) and triiodothyronine (T3) metabolism was studied in Wistar rats. The effect on serum binding of T4 has also been studied. Animals were injected with a tracer dose of either labeled hormone and by examining serum L-125I-T4 and L-125-I-T3, kinetics of radiolabeled hormones metabolism were calculated. The T4 metabolic clearance (MCI) as well as the distribution space, were increased by 6 fold. Decreased serum T4 levels result from an increase both in deiodinative and fecal disposal in HCB-treated rats. 125I-T3 metabolism was slightly affected. The enhanced peripheral disposition of thyroxine appears to lead to increased thyroid function, as measured by augmented TSH serum levels and 125I-thyroidal uptake. Serum binding of T4 was not affected.
    No preview · Article · Jan 1990 · Journal of endocrinological investigation
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    ABSTRACT: A purple pigment, phyriaviolin, and a blue pigment, phyriaazulin, have been found in relatively large amounts in the urine of patients suffering from two diverse pathological conditions, porphyria cutanea tarda and Crohn's disease. The two pigments have been characterised by chemical, spectroscopic, and chromatographic studies and identified to be indirubin and indigo (indigotin). Possible reasons for their formation are discussed.
    No preview · Article · Apr 1988 · Clinica Chimica Acta
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    ABSTRACT: Triiodothyronine administration to thyroidectomized animals, decreased cytochrome P-450 content by 50%. Haem oxygenase was not modified by triiodothyronine treatment, either alone or with a suboptimal dose of CoCl2. Under the same conditions hepatic delta-amino-laevulinic acid synthase activity was not affected. Triiodothyronine caused a two fold increase in tryptophan pyrrolase activity. Both the hole and total enzyme were increased to the same degree. Porphobilinogen deaminase-Uroporphyrinogen III Co-synthase activity was induced by 67% over thyroidectomized values, in triiodothyronine treated rats, and only 32% above the sham operated controls. Our results suggest that under triiodothyronine stimulation, the decrease in cytochrome P-450 content is not due to an enhanced rate of degradation of the haem moiety, but it rather dissociates to increase the cellular haem pool, and saturates in part the newly synthesized apotryptophan pyrrolase.
    No preview · Article · Feb 1988 · Acta physiologica et pharmacologica latinoamericana: organo de la Asociación Latinoamericana de Ciencias Fisiológicas y de la Asociación Latinoamericana de Farmacología
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    ABSTRACT: Four heptacarboxylic, six hexacarboxylic, and four pentacarboxylic porphyrins related to uroporphyrin-III by decarboxylation of one, two, or three of the acetic acid side chains have been synthesised as their methyl esters by application of the MacDonald or b-oxobilane methods, as appropriate. Comparison (mixed mp, “mixed” nmr spectra, and hplc) of the synthetic materials with the methyl esters of hepta-, hexa-, and pentacarboxylic porphyrins isolated from natural sources showed that the structures of the latter corresponded to the D-ring methyl, the DA-dimethyl, and the DAB-trimethyl analogs of uroporphyrin-III. Because the naturally occurring porphyrins arise by oxidation of intermediate porphyrinogens, we conclude that the enzymic decarboxylation of uroporphyrinogen-III to coproporphyrinogen-III takes place in a preferred sequential clockwise fashion (both in normal and abnormal metabolism) starting with the acetic acid moiety on the D-ring and followed by those on the A, B, and C rings.
    No preview · Article · Mar 1980 · Bioorganic Chemistry

Publication Stats

367 Citations
75.60 Total Impact Points


  • 2007
    • Buenos Aires Ciudad
      Buenos Aires, Buenos Aires F.D., Argentina
  • 1967-2006
    • University of Buenos Aires
      • • Biological Chemistry Department
      • • Faculty of Exact and Natural Sciences
      Buenos Aires, Buenos Aires F.D., Argentina
  • 1995
    • Universidad Nacional Lomas de Zamora
      Buenos Aires, Buenos Aires F.D., Argentina
  • 1976-1980
    • Cardiff University
      • School of Chemistry
      Cardiff, WLS, United Kingdom