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1.
J Ethnopharmacol ; 137(1): 796-801, 2011 Sep 01.
Article in English | MEDLINE | ID: mdl-21762770

ABSTRACT

AIM OF THE STUDY: Hydnora johannis Becca. (Hydnoraceae) commonly is used for the treatment of dysentery, diarrhoea, cholera and swelling tonsillitis in the folk medicine of Sudan and other African countries. This study evaluates the toxicological effects of Hydnora johannis roots on Wistar rats. MATERIALS AND METHODS: Rats were randomized into control, groups fed with 2, 10, 20% of dried roots for 8 weeks and other groups given ethanol extract (50, 100, 200 and 400mg/kg/day) through oral and intramuscularly administration for 2 weeks. Toxicity was evaluated using biochemical and histopathological assays. RESULTS: Alterations in the levels of aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase, cholesterol and urea were observed. Histopathological analysis revealed that the toxic effect were mainly on the liver, kidney and spleen on all treated groups. However, the impact of the dried roots was mild compared to the ethanol extract. Remarkably, there was a drop in cholesterol level in all treatment groups suggesting the antiartherogenic effect of Hydnora johannis roots. CONCLUSION: The results from this study suggest that the powder preparation as well as ethanolic extract of Hydnora johannis roots induced toxic effect on Wistar rats. The observed toxic effect might be due to the dose and/or frequency of administration. Although in traditional medicine the extract is administrated in low dose, the results suggest the necessity of standardization of the drug.


Subject(s)
Ethanol/chemistry , Piperaceae , Plant Extracts/toxicity , Solvents/chemistry , Administration, Oral , Alanine Transaminase/blood , Alkaline Phosphatase/blood , Animals , Aspartate Aminotransferases/blood , Biomarkers/blood , Cholesterol/blood , Dose-Response Relationship, Drug , Female , Injections, Intramuscular , Kidney/drug effects , Kidney/metabolism , Kidney/pathology , Liver/drug effects , Liver/metabolism , Liver/pathology , Male , Piperaceae/chemistry , Plant Extracts/administration & dosage , Plant Extracts/chemistry , Plant Extracts/isolation & purification , Plant Roots , Plants, Medicinal , Rats , Rats, Wistar , Spleen/drug effects , Spleen/metabolism , Spleen/pathology , Time Factors , Toxicity Tests , Urea/blood
2.
Vet Parasitol ; 170(3-4): 344-7, 2010 Jun 24.
Article in English | MEDLINE | ID: mdl-20434269

ABSTRACT

The effect of temperature and humidity on the oviposition and hatchability of Ablyomma lepidum was studied. Above 90% of adult ticks applied on calves succeeded to attach and feed through 6-13 days. The development process was studied under three levels of temperature: 27, 35 and 40 degrees C, each level with five sets of humidity. Temperature rather than humidity affected all developmental parameters. It was found that high temperature of 40 degrees C, even at high humidity 75.5-97.8% significantly affected pre-oviposition, oviposition, pre-hatching periods, egg mass weight and egg conversion ratio (p

Subject(s)
Humidity , Ixodidae/physiology , Oviposition/physiology , Ovum/physiology , Temperature , Animals , Body Weight , Feeding Behavior , Female , Male
3.
Mol Cell Biol ; 21(18): 6243-53, 2001 Sep.
Article in English | MEDLINE | ID: mdl-11509667

ABSTRACT

We report here on the identification and characterization of novel 2-enoyl thioester reductases of fatty acid metabolism, Etr1p from Candida tropicalis and its homolog Ybr026p (Mrf1'p) from Saccharomyces cerevisiae. Overexpression of these proteins in S. cerevisiae led to the development of significantly enlarged mitochondria, whereas deletion of the S. cerevisiae YBR026c gene resulted in rudimentary mitochondria with decreased contents of cytochromes and a respiration-deficient phenotype. Immunolocalization and in vivo targeting experiments showed these proteins to be predominantly mitochondrial. Mitochondrial targeting was essential for complementation of the mutant phenotype, since targeting of the reductases to other subcellular locations failed to reestablish respiratory growth. The mutant phenotype was also complemented by a mitochondrially targeted FabI protein from Escherichia coli. FabI represents a nonhomologous 2-enoyl-acyl carrier protein reductase that participates in the last step of the type II fatty acid synthesis. This indicated that 2-enoyl thioester reductase activity was critical for the mitochondrial function. We conclude that Etr1p and Ybr026p are novel 2-enoyl thioester reductases required for respiration and the maintenance of the mitochondrial compartment, putatively acting in mitochondrial synthesis of fatty acids.


Subject(s)
Candida/enzymology , Fatty Acid Synthases/genetics , Mitochondria/enzymology , NADH, NADPH Oxidoreductases , Saccharomyces cerevisiae Proteins , Saccharomyces cerevisiae/enzymology , Amino Acid Sequence , Candida/genetics , Candida/ultrastructure , Cloning, Molecular , Electron Transport , Fatty Acid Desaturases/genetics , Fatty Acid Desaturases/metabolism , Fatty Acid Synthases/metabolism , Fungal Proteins/genetics , Fungal Proteins/metabolism , Mitochondrial Proteins , Molecular Sequence Data , Oxidoreductases Acting on CH-CH Group Donors , Saccharomyces cerevisiae/genetics , Saccharomyces cerevisiae/ultrastructure , Sequence Alignment , Transcription Factors/genetics
4.
Biochem J ; 344 Pt 3: 903-14, 1999 Dec 15.
Article in English | MEDLINE | ID: mdl-10585880

ABSTRACT

Human 2,4-dienoyl-CoA reductase (2,4-reductase; DECR) and rat monofunctional Delta(3)-Delta(2)-enoyl-CoA isomerase (rat 3, 2-isomerase; ECI) are thought to be mitochondrial auxiliary enzymes involved in the beta-oxidation of unsaturated fatty acids. However, their function during this process has not been demonstrated. Although they lack obvious peroxisomal targeting signals (PTSs), both proteins have been suggested previously to also occur in the mammalian peroxisomal compartment. The putative function and peroxisomal location of the two mammalian proteins can be examined in yeast, since beta-oxidation of unsaturated fatty acids is a compartmentalized process in Saccharomyces cerevisiae requiring peroxisomal 2,4-dienoyl-CoA reductase (Sps19p) and peroxisomal 3, 2-isomerase (Eci1p). A yeast sps19Delta mutant expressing human 2, 4-reductase ending with the native C-terminus could not grow on petroselinic acid [cis-C(18:1(6))] medium but could grow when the protein was extended with a PTS tripeptide, SKL (Ser-Lys-Leu). We therefore reason that the human protein is a physiological 2, 4-reductase but that it is probably not peroxisomal. Rat 3, 2-isomerase expressed in a yeast eci1Delta strain was able to re-establish growth on oleic acid [cis-C(18:1(9))] medium irrespective of an SKL extension. Since we had shown that Delta(2,4) double bonds could not be metabolized extra-peroxisomally to restore growth of the sps19Delta strain, we postulate that rat 3,2-isomerase acted on the Delta(3) unsaturated metabolite of oleic acid by replacing the mutant's missing activity from within the peroxisomes. Immunoblotting of fractionated yeast cells expressing rat 3, 2-isomerase in combination with electron microscopy supported our proposal that the protein functioned in peroxisomes. The results presented here shed new light on the function and location of human mitochondrial 2,4-reductase and rat monofunctional 3,2-isomerase.


Subject(s)
Carbon-Carbon Double Bond Isomerases/metabolism , Fatty Acid Desaturases/metabolism , Fatty Acids, Unsaturated/metabolism , Mitochondria, Liver/enzymology , Oxidoreductases Acting on CH-CH Group Donors , Saccharomyces cerevisiae/enzymology , Animals , Cell Division , Dodecenoyl-CoA Isomerase , Gene Expression Regulation, Enzymologic , Humans , Microscopy, Electron , Mutation , Oleic Acid/metabolism , Oleic Acids/metabolism , Oligopeptides/genetics , Peroxisomes/enzymology , Plasmids , Rats , Saccharomyces cerevisiae/genetics
5.
J Biol Chem ; 274(35): 24514-21, 1999 Aug 27.
Article in English | MEDLINE | ID: mdl-10455114

ABSTRACT

Fatty acids with double bonds at odd-numbered positions such as oleic acid can enter beta-oxidation via a pathway relying solely on the auxiliary enzyme Delta(3)-Delta(2)-enoyl-CoA isomerase, termed the isomerase-dependent pathway. Two novel alternative pathways have recently been postulated to exist in mammals, and these additionally depend on Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase (di-isomerase-dependent) or on Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase and 2,4-dienoyl-CoA reductase (reductase-dependent). We report the identification of the Saccharomyces cerevisiae oleic acid-inducible DCI1 (YOR180c) gene encoding peroxisomal di-isomerase. Enzyme assays conducted on soluble extracts derived from yeast cells overproducing Dci1p using 3,5,8,11,14-eicosapentenoyl-CoA as substrate demonstrated a specific di-isomerase activity of 6 nmol x min(-1) per mg of protein. Similarly enriched extracts from eci1Delta cells lacking peroxisomal 3,2-isomerase additionally contained an intrinsic 3,2-isomerase activity that could generate 3, 5,8,11,14-eicosapentenoyl-CoA from 2,5,8,11,14-eicosapentenoyl-CoA but not metabolize trans-3-hexenoyl-CoA. Amplification of this intrinsic activity replaced Eci1p since it restored growth of the eci1Delta strain on petroselinic acid for which di-isomerase is not required whereas Eci1p is. Heterologous expression in yeast of rat di-isomerase resulted in a peroxisomal protein that was enzymatically active but did not re-establish growth of the eci1Delta mutant on oleic acid. A strain devoid of Dci1p grew on oleic acid to wild-type levels, whereas one lacking both Eci1p and Dci1p grew as poorly as the eci1Delta mutant. Hence, we reasoned that yeast di-isomerase does not additionally represent a physiological 3,2-isomerase and that Dci1p and the postulated alternative pathways in which it is entrained are dispensable for degrading oleic acid.


Subject(s)
Carbon-Carbon Double Bond Isomerases/biosynthesis , Oleic Acid/metabolism , Saccharomyces cerevisiae/enzymology , Acyl Coenzyme A/metabolism , Carbon-Carbon Double Bond Isomerases/chemistry , Enzyme Induction/drug effects , Gene Expression Regulation, Enzymologic/drug effects , Gene Expression Regulation, Fungal/drug effects , Microbodies/enzymology , Mutation , Saccharomyces cerevisiae/genetics
7.
J Biol Chem ; 273(1): 349-55, 1998 Jan 02.
Article in English | MEDLINE | ID: mdl-9417087

ABSTRACT

rECH1, a recently identified rat cDNA (FitzPatrick, D. R., Germain-Lee, E., and Valle, D. (1995) Genomics 27, 457-466) encodes a polypeptide belonging to the hydratase/isomerase superfamily. We modeled the structure of rECH1 based on rat mitochondrial 2-enoyl-CoA hydratase 1. The model predicts that rECH1p has the hydratase fold in the core domain and two domains for interaction with other subunits. When we incubated 3,5,8,11, 14-eicosapentaenoyl-CoA with purified rECH1p, the spectral data suggested a switching of the double bonds from the Delta3-Delta5 to the Delta2-Delta4 positions. This was confirmed by demonstrating that the product was a valid substrate for 2,4-dienoyl-CoA reductase. These results indicate that rECH1p is Delta3,5-Delta2,4-dienoyl-CoA isomerase. Subcellular fractionation and immunoelectron microscopy using antibodies to a synthetic polypeptide derived from the C terminus of rECH1p showed that rECH1p is located in the matrix of both mitochondria and peroxisomes in rat liver. Consistent with these observations, the 36,000-Da rECH1p has a potential N-terminal mitochondrial targeting signal as well as a C-terminal peroxisomal targeting signal type 1. Transport of the protein into the mitochondria with cleavage of the targeting signal results in a mature mitochondrial form with a molecular mass of 32,000 Da; transport to peroxisomes yields a protein of 36,000 Da.


Subject(s)
Carbon-Carbon Double Bond Isomerases/metabolism , Mitochondria, Liver/enzymology , Amino Acid Sequence , Animals , Carbon-Carbon Double Bond Isomerases/chemistry , Carbon-Carbon Double Bond Isomerases/genetics , Kinetics , Microscopy, Immunoelectron , Mitochondria, Liver/ultrastructure , Models, Molecular , Molecular Sequence Data , Rats , Sequence Homology, Amino Acid , Subcellular Fractions/enzymology
8.
Vet Hum Toxicol ; 33(6): 557-60, 1991 Dec.
Article in English | MEDLINE | ID: mdl-1808830

ABSTRACT

Ochratoxin A was fed at 0.5 ppm to Lohmann-type chicks from 7 d of age for 4 w. Body weights and efficiency of feed utilization were depressed and the activity of serum SDH and GDH and the concentration of uric acid were significantly increased. The concentration of serum total protein and potassium and Hb, PCV, RBC and WBC were significantly decreased in the test group. Lesions were seen in vital organs, with hemorrhage in the thigh. A slow recovery in the kidney was observed 3 w after removal from the experimental diet.


Subject(s)
Ochratoxins/toxicity , Poultry Diseases/chemically induced , Animal Feed , Animals , Blood Cell Count , Body Weight/drug effects , Chickens , Female , Gastrointestinal Hemorrhage/chemically induced , Gastrointestinal Hemorrhage/pathology , Gastrointestinal Hemorrhage/veterinary , Glutamate Dehydrogenase/blood , Kidney/pathology , Liver/pathology , Male , Myocardium/pathology , Potassium/blood , Poultry Diseases/pathology , Spleen/pathology , Succinate Dehydrogenase/blood , Thigh/pathology , Uric Acid/blood
9.
J Helminthol ; 60(2): 123-34, 1986 Jun.
Article in English | MEDLINE | ID: mdl-3734396

ABSTRACT

The pathogenesis of unirradiated, 3 krad-irradiated and 20 krad-irradiated metacercarial infections was compared in zebu calves studied over a 10-week period. Calves exposed to 1000 unirradiated metacercariae (mc) became hypoalbuminaemic, and showed elevated serum concentrations of liver enzymes, whereas neither of the other groups was significantly affected. At slaughter, a mean of 332 flukes was recovered from the 0 krad group, while only 23% and 12% of this number were recovered from the 3 krad and and 20 krad groups, respectively. All the worms recovered from the 20 krad group were stunted, and found in biliary ductules, but a mean of 13% of the flukes recovered from the 3 krad group were large, and dwelling in main bile-ducts. Liver lesions typical of acute fascioliasis were present in the 0 krad group, but lesions in the other groups, and particularly the 20 krad group, were far less severe. Judged on clinico-pathological criteria, a single vaccination of calves with 1000 3 krad-irradiated mc induced partial resistance to a challenge with 1000 normal mc eight weeks later, but the reduction in worm recovery was not statistically significant. There was less evidence of protection when two vaccinating doses of 3 krad mc were given within four weeks, with challenge at week 8, and a single vaccination was ineffective against a challenge four weeks later. However, when the irradiation dose was increased to 20 krad, a hgh level of resistance (69% worm reduction) was induced by a single vaccination, given eight weeks before challenge, and liver pathology was strikingly reduced in the vaccinated animals.


Subject(s)
Cattle Diseases/prevention & control , Fasciola/immunology , Fascioliasis/veterinary , Vaccination/veterinary , Vaccines, Attenuated , Animals , Cattle , Cattle Diseases/parasitology , Fasciola/radiation effects , Fascioliasis/prevention & control , Gamma Rays , Liver/parasitology , Liver/pathology
10.
J Helminthol ; 60(1): 55-9, 1986 Mar.
Article in English | MEDLINE | ID: mdl-3701021

ABSTRACT

Using the local strains of Schistosoma bovis and Fasciola gigantica, it was shown that Sudanese zebu calves with mature primary infections of F. gigantica were highly resistant to challenge with S. bovis cercariae, and vice versa. Liver enzyme tests showed that, in both cases, the primary infections had caused some liver damage. Primary infection with irradiated S. bovis cercariae, which did not cause significant liver damage, did not protect significantly against challenge with F. gigantica.


Subject(s)
Cattle Diseases/immunology , Fascioliasis/veterinary , Schistosomiasis/veterinary , Animals , Cattle , Cattle Diseases/parasitology , Cross Reactions , Fasciola/immunology , Fascioliasis/immunology , Fascioliasis/parasitology , Glutamate Dehydrogenase/blood , Immunity, Active , Immunization , L-Iditol 2-Dehydrogenase/blood , Liver/enzymology , Liver/parasitology , Liver/pathology , Schistosoma/immunology , Schistosomiasis/immunology , Schistosomiasis/parasitology
11.
Bull Anim Health Prod Afr ; 24(1): 89-92, 1976 Mar.
Article in English | MEDLINE | ID: mdl-1052886

Subject(s)
Culex , Animals , Breeding , Larva , Pupa , Sudan
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