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PubMed2002

Cloning and expression of the gene for soybean hydroxyisourate hydrolase. Localization and implications for function and mechanism.

The gene encoding hydroxyisourate hydrolase, a novel ureide-metabolizing enzyme, has been cloned from soybean (Glycine max). The gene encodes a protein that is 560 amino acids in length and contains a 31-amino acid signal sequence at the N terminus that is not present in the mature protein. The presence of two SKL motifs near the C terminus suggests that the protein resides in the peroxisome. This expectation is borne out by results from immunogold electron microscopy, which revealed that hydroxyisourate hydrolase was localized in the peroxisomes of uninfected root nodules. The gene encoding hydroxyisourate hydrolase was expressed in Escherichia coli, and soluble, catalytically active enzyme was purified to homogeneity. Sequence analysis revealed considerable homology with members of the beta-glucosidase family of enzymes. Two glutamate residues, E199 and E408, align with the conserved glutamates that play catalytic roles in the beta-glucosidases. However, the other residues that have been identified by crystallography to interact directly with the substrates in beta-glucosidases are not conserved in hydroxyisourate hydrolase. The E199A and E408A hydroxyisourate hydrolase mutants were devoid of detectable catalytic activity. Analysis of transcripts for hydroxyisourate hydrolase demonstrated that its level of expression was highest in the nodule; mRNA was detectable 12 d after infection and increased until 21 d postinfection, then declined. In a similar manner, immunodetection of hydroxyisourate hydrolase indicated preferential localization in the nodule; the amount of protein detected was maximal at 21 d postinfection. The pattern of expression of hydroxyisourate hydrolase matched that of urate oxidase, and supports the hypothesis that hydroxyisourate hydrolase plays a role in ureide metabolism.

Amidohydrolases↗

PubMed1985

Intraparticulate localization and some properties of a clofibrate-induced peroxisomal aldehyde dehydrogenase from rat liver.

A study was made of the effect of chronic administration of the hypolipidemic drug clofibrate on the activity and intracellular localization of rat liver aldehyde dehydrogenase. The enzyme was assayed using several aliphatic and aromatic aldehydes. Clofibrate treatment caused a 1.5 to 2.3-fold increase in the liver specific aldehyde dehydrogenase activity. The induced enzyme has a high Km for acetaldehyde and was found to be located in peroxisomes and microsomes. Clofibrate did not alter the enzyme activity in the cytoplasmic fraction. The total peroxisomal aldehyde dehydrogenase activity increased 3 to 4-fold under the action of clofibrate. Disruption of the purified peroxisomes by the hypotonic treatment or in the alkaline conditions resulted in the release of catalase from the broken organelles, while aldehyde dehydrogenase as well as nucleoid-bound urate oxidase and the peroxisomal membrane marker NADH:cytochrome c reductase remained in the peroxisomal 'ghosts'. At the same time, treatment by Triton X-100 led to solubilization of the membrane-bound NADH:cytochrome c reductase and aldehyde dehydrogenase from intact peroxisomes and their 'ghosts'. These results indicate that aldehyde dehydrogenase is located in the peroxisomal membrane. The peroxisomal aldehyde dehydrogenase is active with different aliphatic and aromatic aldehydes, except for formaldehyde and glyceraldehyde. The enzyme Km values lie in the millimolar range for acetaldehyde, propionaldehyde, benzaldehyde and phenylacetaldehyde and in the micromolar range for nonanal. Both NAD and NADP serve as coenzymes for the enzyme. Aldehyde dehydrogenase was inhibited by disulfiram, N-ethylmaleimide and 5,5'-dithiobis(2-nitrobenzoic)acid. According to its basic kinetic properties peroxisomal aldehyde dehydrogenase seems to be similar to a clofibrate-induced microsomal enzyme. The functional role of both enzymes in the liver cells is discussed.

Aldehyde Dehydrogenase↗

PubMed1990

Effects of prolonged treatment with phthalate ester on rat liver.

Rats were fed a diet containing 2%, 0.2% or 0.02% di(2-ethylhexyl)phthalate (DEHP) for a period of 102 weeks. Only the 2% diet caused a substantial decrease in body weight. Both peroxisomal palmitoyl-CoA dehydrogenase and mitochondrial carnitine acetyltransferase activities were greatly induced by exposure to the highest dose of phthalate ester, reaching maximal plateau values after about 20 weeks of treatment. The diet containing 0.2% DEHP increased both activities slowly, but continuously, and at the end of the two-year period these increases were almost comparable to those obtained with the highest dose. Even the lowest dose gave a slowly increase in these activities. Both microsomal NADPH-cytochrome c reductase activity and the level of cytochrome P-450 were increased initially by exposure to 2% DEHP, but returned almost or completely to the control level after about 30 weeks of exposure. Depending on the dose of DEHP in the diet, peroxisomal catalase activity was elevated above the control level during the first year of treatment but was about the same as in the control animals during the second year. A substantial decrease in peroxisomal urate oxidase activity was observed throughout the entire experimental period. When treatment was ceased after one year, all activities returned to the control values within 2-3 weeks. These results demonstrate the complex nature of the effects caused by prolonged treatment with DEHP with cumulative increases at low doses.

Animals↗

PubMed2005

Intensive chemotherapy in patients with lymphoma. Management of the risk of hyperuricemia.

Intensive chemotherapy with stem cell autograft is a well-established salvage treatment for relapsed/refractory lymphoma patients aged less than 65 years and it is also an effective treatment option for high-risk patients at diagnosis. Clinical applicability of autograft has been greatly amplified by the use of peripheral blood progenitor cells (PBPC), whose administration is simple and feasible, and results in lower toxicity. In addition, the development of several prophylactic measures preventing extrahemopoietic toxicities has markedly improved the feasibility and tolerability of the approach. In particular, the risk of nephrotoxicity is no more a major problem in the autograft setting since the use of proper treatments for the management of hyperuricemia, including forced hydration along with urinary alkalinization and the administration of the recombinant urate oxidase drug rasburicase. The high-dose sequential (HDS) chemotherapy program is a typical example of an intensive chemotherapy with PBPC autograft. A 15-year experience with the HDS approach in 240 lymphoma patients is reported here. The results demonstrate the clinical efficacy of HDS, with prolonged survival both in relapsed/refractory patients (54% alive) and in those treated frontline (72% alive). In addition, a very low incidence of extrahemopoietic toxicities was observed. In particular, nephrotoxicity was almost abolished, with 2 patients displaying only mild and transient renal dysfunction. In conclusion, the reported results demonstrate the therapeutic efficacy of HDS in the treatment strategy for lymphoma and emphasize the importance of delivering intensive chemotherapy with all the prophylactic measures able to minimize nephrotoxicity and other potential extrahemopoietic toxicities.

Adolescent↗

PubMed2005

Pharmacological treatment of acute and chronic hyperuricemia in kidney diseased patients.

Several trials argued the possibility that hyperuricemia may have a direct effect on cardiovascular and renal disease. It has been shown that an elevated serum uric acid concentration is a predictor of cardiovascular events such as myocardial infarction. It also predicts the development of hypertension and in hypertensive patients, hyperuricemia is associated with increased cardiovascular morbidity and mortality. Hyperuricemia is a complication often seen in patients with chronic and acute renal disease. The relationship between serum uric acid level and the appearance or progression of renal dysfunction has been debated in the last years. During chemotherapy for hematological malignancies or more rarely for solid tumors, acute renal failure, secondary to a sudden marked increase in uric acid, is not such a rare complication. The therapeutic intervention includes hyper hydration, urinary alkalinization, and the use of uric acid decreasing agents such as allopurinol and rasburicase, a recent recombinant-urate oxidase. In our personal experience, patients with acute renal failure due to hyperuricemia, showed a better renal prognosis with rasburicase than allopurinol. Chronic hyperuricemia is also associated with chronic tubulo-interstitial disease with glomerular sclerosis, and renal dysfunction. Experimental trials showed that uric acid can affect kidneys through different mechanisms at glomerular, tubulo-interstitial and vascular level. Although allopurinol is often the drug of choice, caution must be used to avoid serious side effects. New therapeutic options, for treating hyperuricemia are needed in patients with renal dysfunction for slowing the progression to end stage kidney disease.

Acute Disease↗

PubMed1986

Phytol and peroxisome proliferation.

Infantile Refsum's disease is characterized by high levels of phytanic acid and the absence of normal hepatic peroxisomes. We investigated the in vivo influence of phytol, a precursor of phytanic acid, on peroxisomes by both biochemical and morphological methods. Enhanced supply of phytol in the diet of adult mice causes proliferation of hepatic peroxisomes. The peroxisomal beta-oxidizing capacity as well as exchanges of acyl moieties between peroxisomes and mitochondria are raised around 5- and 2-fold, respectively. In parallel a 1.5-fold increase of total catalase and mitochondrial butyryl-CoA dehydrogenase activities occurs, whereas peroxisomal urate oxidase and glycolate oxidase remain normally active. Serum triglyceride levels are decreased after 3 wk of phytol feeding; serum cholesterol levels remain unaffected. Phytol feeding also induces peroxisome proliferation in duodenal epithelium, in myocardium and in skin sebaceous glands, but not in kidney.

Animals↗

PubMed1982

Hyperuricemic effects of cholinergic agents in rats.

The hyperuricemic effect of cholinergic agents was studied in rats given potassium oxonate which inhibits urate oxidase and in functionally hepatectomized rats. Acetylcholine slightly increased plasma uric acid in the oxonate-treated animals, and the effect was markedly enhanced by pretreatment with physostigmine. Carbachol alone showed the hyperuricemic effect at a smaller dose than acetylcholine. The hyperuricemic effects of physostigmine plus acetylcholine and carbachol alone were also observed in eviscerated rats with nonfunctioning livers. Nephrectomy markedly potentiated cholinergic agent-induced hyperuricemia, and methylatropine but not hexamethonium apparently abolished the induction of hyperuricemia both in potassium oxonate-treated rats and in eviscerated rats with nonfunctioning livers and without kidneys. However, carbachol-induced hyperuricemia was not found in rats given allopurinol whose plasma levels of uric acid were maintained by exogenously administered uric acid. These results supported the ideas that the hyperuricemic effect of cholinergic agents is due to the stimulated production of uric acid and that uric acid production in tissues other than the liver and the gastrointestinal viscera is closely related to the induction mechanisms of hyperuricemia.

Acetylcholine↗

PubMed1983

Rat liver peroxisomes, II. Stimulation of peroxisomal fatty-acid beta-oxidation by thyroid hormones.

From liver homogenates of control and thyroxine-treated rats the light mitochondrial fractions were prepared by differential centrifugation. Mitochondria and peroxisomes of these fractions were further separated by isopycnic sucrose density gradient centrifugation. Analysis of the activities of the peroxisomal marker enzymes catalase and urate oxidase throughout the gradient exhibited completely corresponding distributions with that of peroxisomal palmitoyl-CoA oxidation. Thyroxine treatment did not change the proportion of mitochondria and peroxisomes present in the differential fractions of the homogenate. Consequently, the activities of peroxisomal beta-oxidation in the light mitochondrial fractions of control and thyroxine-treated animals were directly comparable with each other. A 2.5-fold increase in peroxisomal palmitoyl-CoA oxidation raising the activity from 0.089 to 0.220 U/g as estimated in the light mitochondrial fractions was found following treatment of male rats with daily doses of 25 micrograms L-thyroxine (s.c.) over a period of 10 days. Total hepatic peroxisomal fatty-acyl-CoA oxidation was calculated based on estimations in the light mitochondrial fractions. The difficulties encountered herein are discussed. The present result replenishes the broad spectrum of cellular effects exerted by thyroid hormones and indicates that both the mitochondrial and the peroxisomal system contribute to the well known hormone effects such as increase in fatty-acid oxidation, O2 consumption and heat production.

Acyl Coenzyme A↗

PubMed2006

Pathophysiology, clinical presentation and treatment of gout.

Gout is a common form of inflammatory arthritis that has been managed primarily in general medical practices for centuries. It appears that there has been an increasing prevalence of gout over the past decades, implying a growing public health burden. Accurate diagnosis and recognition of the various stages and manifestations of gout enable realistic goal setting for management. Recent evidence suggests new risk factors and potentially refutes others. Management of gout requires characterising and modifying risk factors and associated disorders, and commonly initiating drug therapy. Pharmacotherapy of gout includes the management of acute flares with anti-inflammatory agents such as NSAIDs and glucocorticoids and long-term treatment with urate-lowering drugs. Although pharmacotherapy is generally safe and effective, there are caveats and limitations to all gout therapies. Patient non-adherence and errors with the use of drugs for gout treatment are important factors leading to medical failures. With early intervention, careful monitoring and patient education, gout is a condition that can be managed very effectively. The advent of new drugs (such as febuxostat and urate oxidase [uricase]) and enhanced understanding of the pathogenesis of gout continue to improve our therapeutic options, particularly in a subset of patients with refractory disease and those who are intolerant to currently available medications.

Acute Disease↗

PubMed1999

Identification of peroxisomal proteins by using M13 phage protein VI phage display: molecular evidence that mammalian peroxisomes contain a 2,4-dienoyl-CoA reductase.

To elucidate unknown mammalian peroxisomal enzymes and functions, we subjected M13 phage expressing fusions between the gene encoding protein VI and a rat liver cDNA library to an immunoaffinity selection process in vitro (biopanning) with the use of antibodies raised against peroxisomal subfractions. In an initial series of biopanning experiments, four different cDNA clones were obtained. These cDNA species encoded two previously identified peroxisomal enzymes, catalase and urate oxidase, and two novel proteins that contained a C-terminal peroxisomal targeting signal (PTS1). A primary structure analysis of these novel proteins revealed that one, ending in the tripeptide AKL, is homologous to the yeast peroxisomal 2,4-dienoyl-CoA reductase (EC 1.3.1.34; DCR), an enzyme required for the degradation of unsaturated fatty acids, and that the other, ending in the tripeptide SRL, is a putative member of the short-chain dehydrogenase/reductase (SDR) family, with three isoforms. Green fluorescent protein (GFP) fusions encoding GFP-DCR-AKL, GFP-DCR, GFP-SDR-SRL and GFP-SDR were expressed in mammalian cells. The analysis of the subcellular location of the recombinant fusion proteins confirmed the peroxisomal localization of GFP-DCR-AKL and GFP-SDR-SRL, as well as the functionality of the PTS1. That the AKL protein is indeed an NADPH-dependent DCR was demonstrated by showing DCR activity of the bacterially expressed protein. These results demonstrate at the molecular level that mammalian peroxisomes do indeed contain a DCR. In addition, the results presented here indicate that the protein VI display system is suitable for the isolation of rare cDNA clones from cDNA libraries and that this technology facilitates the identification of novel peroxisomal proteins.

Alcohol Dehydrogenase↗

PubMedDate not supplied

[Role of uric acid in hypertension and in the progression of chronic renal disease].

In humans, uric acid (UA) is the main urinary metabolite of purines, whereas in other species (avians) it is the chief nitrogen compound excreted in the urine. The absence of uricase, due to nonsense or splice mutations occurring during the evolution of primates, results in blood urate levels much higher in humans than in other mammalians. This could have favorable implications, including protection from oxidative damage, as well as possibly allowing better blood pressure (BP) control in settings of low dietary Na+ intake. UA is a stimulus of the renin-angiotensin system (RAS). Moreover, blood UA levels are a major marker of proximal tubular function and overall volume status. On the other hand, hyperuricemia is a co-factor in Na+ -sensitive arterial hypertension, a marker and perhaps itself responsible for microvascular and systemic damage through RAS stimulation, inhibitory effects on endothelial cells, and the proliferation of perivascular smooth muscle cells. Recent studies in rats rendered hyperuricemic through administration of oxonic acid demonstrate the induction of hypertension and severe microvascular damage when associated with subtotal nephrectomy or chronic cyclosporine treatment. The opportunity to pharmacologically manipulate blood UA levels through inhibitors of synthesis (allopurinol), uricosuric agents (benziodarone), or recombinant urate oxidase (rasburicase) provides a relevant therapeutic potential in UA metabolism disorders, tumor lysis syndrome, and possibly in essential hypertension, as well as chronic progressive renal disease.

Animals↗

PubMed2006

Treatment of oncologic emergencies.

Most oncologic emergencies can be classified as metabolic, hematologic, structural, or side effects from chemotherapy agents. Tumor lysis syndrome is a metabolic emergency that presents as severe electrolyte abnormalities. The condition is treated with allopurinol or urate oxidase to lower uric acid levels. Hypercalcemia of malignancy is treated with aggressive rehydration, furosemide, and intravenous bisphosphonates. Syndrome of inappropriate antidiuretic hormone should be suspected if a patient with cancer presents with normovolemic hyponatremia. This metabolic condition usually is treated with fluid restriction and furosemide. Febrile neutropenia is a hematologic emergency that usually requires inpatient therapy with broad-spectrum antibiotics, although outpatient therapy may be appropriate for low-risk patients. Hyperviscosity syndrome usually is associated with Waldenström's macroglobulinemia, which is treated with plasmapheresis and chemotherapy. Structural oncologic emergencies are caused by direct compression of nontumor structures or by metastatic disease. Superior vena cava syndrome presents as neck or facial swelling and development of collateral venous circulation. Treatment options include chemotherapy, radiation, and intravenous stenting. Epidural spinal cord compression can be treated with dexamethasone, radiation, or surgery. Malignant pericardial effusion, which often is undiagnosed in cancer patients, can be treated with pericardiocentesis or a pericardial window procedure.

Antineoplastic Agents↗

PubMed1990

Transdifferentiation of ductular cells into hepatocytes in regenerating hamster pancreas.

The transdifferentiation of regenerating pancreatic cells into hepatocytes in the Syrian golden hamster and Fischer rat is an example of the surprising plasticity of cells in the adult animal. While earlier experiments suggested that these might be derived from acinar cells, unequivocal evidence of this in both models has not been forthcoming. In this paper, we document that pancreatic ductular epithelium in the hamster is the cell of origin and that presumptive hepatocytes can be identified morphologically as early as the 3rd day after the induction of regeneration. The patterns of development of various organelles as characterized by their acquisition of liver-specific protein markers parallels those that have been reported by others during the differentiation of embryonic and postnatal hepatocytes. Colloidal gold-labeled antibody staining of carbamoyl phosphate synthetase, a liver-specific mitochondrial enzyme, and catalase, a peroxisomal enzyme, first appeared 60 hours and 4.5 days postregeneration, respectively. At these times, the morphologic features of the hepatocyte phenotype in the pancreas were ambiguous. Morphometric analysis showed that for both enzymes, the number of gold particles/organelle increased to a maximum by the 9th week. In contrast, urate oxidase, a liver-specific peroxisomal enzyme, was not identified by ultrastructural immunochemistry until the 14th day after regeneration and remained at low levels through the 9th week.

Animals↗

PubMed1988

Selective induction of peroxisomal enzymes by the hypolipidemic drug bezafibrate. Detection of modulations by automatic image analysis in conjunction with immunoelectron microscopy and immunoblotting.

Quantitative immunoelectron microscopy in conjunction with quantitative analysis of immunoblots have been used to study the effects of bezafibrate (BF), a peroxisome-proliferating hypolipidemic drug, upon six different enzyme proteins in rat liver peroxisomes (Po). Antibodies against following peroxisomal enzymes: catalase, urate oxidase, alpha-hydroxy acid oxidase, acyl-CoA oxidase, bifunctional enzyme (hydratase-dehydrogenase) and thiolase, were raised in rabbits, and their monospecificities were confirmed by immunoblotting. Female Sprague-Dawley rats were treated for 7 days with 250 mg/kg/day bezafibrate and liver sections were incubated with the appropriate antibodies followed by the protein A-gold complex. The labeling density for each enzyme was estimated by automatic image analysis. In parallel experiments immunoblots prepared from highly purified peroxisome fractions of normal and BF-treated rats were incubated with the same antibodies. The antigens were visualized by an improved protein A-gold method including an anti-protein A step and silver amplification. The immunoblots were also quantitated by an image analyzer. The results revealed a selective induction of beta-oxidation enzymes by bezafibrate with thiolase showing the most increase followed by bifunctional protein and acyl-CoA oxidase. The labeling density for catalase and alpha-hydroxy acid oxidase was reduced, confirming fully the quantitative analysis of immunoblots which in addition revealed reduction of uricase. These observations demonstrate that hypolipidemic drugs induce selectively the beta-oxidation enzymes while other peroxisomal enzymes are reduced. The quantitative immunoelectron microscopy with automatic image analysis provides a versatile, highly sensitive and efficient method for rapid detection of modulations of individual proteins in peroxisomes.

Acetyl-CoA C-Acetyltransferase↗

PubMed1986

Isolation and characterization of peroxisomes from the renal cortex of beef, sheep, and cat.

The isolation and characterization of highly purified and structurally well-preserved peroxisomes from the renal cortex of different mammalian species (beef, sheep, and cat) is reported. Renal cortex tissue was homogenized and a peroxisome-enriched light mitochondrial fraction was prepared by differential centrifugation. This was subfractionated by density-dependent banding on a linear gradient of metrizamide (1.12-1.26 g/cm3) using a Beckman VTi 50 vertical rotor. Peroxisomes banded at a mean density of 1.225 cm3. Ultrastructural morphometric examination revealed that peroxisomes made up 97 to 98% of the isolated fractions. By biochemical analysis the contamination with marker enzymes of mitochondria and lysosomes was extremely low. The specific activity of catalase was enriched, depending on the species, between 28- and 38-fold over the homogenate. Peroxisome preparations from all three species exhibited a high but varying level of activity for cyanide-insensitive lipid beta-oxidation. In beef and sheep preparations a small amount of esterase activity cosediments with peroxisomes. These peroxisomes show distinct structural membrane associations with smooth elements of ER. Urate oxidase, a marker enzyme for rat liver peroxisomes, is found only in peroxisomes prepared from beef kidney cortex, with sheep and cat preparations being negative. This correlated with the occurrence of polytubular inclusions in the beef kidney peroxisomes. The large size and the angular shape of isolated peroxisomes as well as the presence of paracrystalline matrical inclusions imply that the majority of peroxisomes are derived from the epithelial cells of the proximal tubule of the kidney cortex. The significant differences found in the characteristics of the renal peroxisomes in three different species investigated, demonstrate the remarkable adaptability and plasticity of this organelle.

Animals↗

PubMed1986

Formation of chenodeoxycholic acid from 3 alpha, 7 alpha-dihydroxy-5 beta-cholestanoic acid by rat liver peroxisomes.

The oxidation of the side chain of 3 alpha, 7 alpha-dihydroxy-5 beta-cholestanoic acid (DHCA) into chenodeoxycholic acid has been studied in subcellular fractions of rat liver. The product was separated from the substrate by high pressure liquid chromatography and identified by gas-liquid chromatography-mass spectrometry. The highest specific rate of conversion was found in the heavy (M) and the light (L) mitochondrial fractions with the highest enrichment in the L fraction. Washing the M fraction reduced the side chain cleavage activity by 90%. The peroxisomal marker enzyme urate oxidase was reduced to the same extent. The activity found in the M fraction may thus be due to peroxisomal contamination. After centrifugation of the L fraction on a Nycodenz density gradient, the highest specific activity for side chain cleavage of DHCA (31 nmol X mg-1 X h-1) was found in the fraction with the highest peroxisomal marker enzyme activity. This fraction also catalyzed conversion of 3 alpha,7 alpha,12 alpha-5 beta-cholestanoic acid (THCA) into cholic acid at the highest rate (32 nmol X mg-1 X h-1). The peroxisomal oxidation of DHCA into chenodeoxycholic acid required the presence of ATP, CoA, Mg2+, and NAD in the incubation medium. The reaction was not inhibited by KCN. It is concluded that rat liver peroxisomes contain enzymes able to catalyze the cleavage of the side chain of both DHCA and THCA. The enzymes involved are similar to, but not necessarily identical to, those involved in the peroxisomal beta-oxidation of fatty acids.

Animals↗

PubMed1985

[Acute hyperleukocytic lymphoblastic leukemia (greater than or equal to 100,000 leukocytes/mm3). Metabolic changes during induction treatment. Study, prevention and treatment].

Acute leukemias with high white blood count have a poor immediate prognosis and the treatment must be started within the first hours following diagnosis. It is necessary to prevent and to treat the severe metabolic disorders observed during induction treatment of acute lymphoblastic leukemia with WBC greater than or equal to 100,000/mm3. We analysed all the metabolic disorders in a retrospective study of 45 patients in order to determine their adequate prevention and treatment. Prevention of hyperuricemia and of secondary renal failure is now possible with urate oxidase, allowing an aggressive and rapid induction. Hyperkalemia can be prevented by urinary alkalinization and hyperphosphoremia with hypocalcemia by high dose intravenous calcium therapy. Renal failure is often transitory and functional. Disseminated intravascular coagulation is treated by heparin and platelets infusion and severe hyperglycemia requires insulin therapy.

Adolescent↗

PubMed1983

[Effect of clofibrate on the polypeptide content of a purified fraction of rat liver peroxisomes].

The effects of the hypolipaemic agent clofibrate on rat liver peroxisomes and of its "ghosts" obtained by solubilization of peroxisomal matrix peptides were studied by Na-DS polyacrylamide gel electrophoresis. Clofibrate significantly altered the amount of some peroxisomal polypeptides which is correlated with its effect on the enzyme composition of these organelles. The possibility of identification of polypeptides in gels with subunits of some peroxisomal enzymes (catalase, urate oxidase, components of fatty acid beta-oxidation chain, etc.) is discussed.

Animals↗