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dc.contributor.authorADENUGA, G. A.-
dc.date.accessioned2019-01-02T16:14:16Z-
dc.date.available2019-01-02T16:14:16Z-
dc.date.issued1992-05-
dc.identifier.urihttp://adhlui.com.ui.edu.ng/jspui/handle/123456789/559-
dc.descriptionA Thesis in the Department of Biochemistry submitted to the Faculty of Basic Medical Sciences in partial fulfillment of the requirements for the award of Doctor of Philosophy of the University of Ibadan, Nigeria.en_US
dc.description.abstractThe effect of the liver tumour promoter, dicophane, with those of low protein intake (LPI) in the functional expression of rat liver microsomal Ca²⁺-ATPase were compared. The effects of dicophane and LPI on the activity of the microsomal enzyme after carcinogenic initiation by pretreatment with aflatoxin B₁ (AFB), a genotoxic liver carcinogen , were also compared. The status of membrane-bound Ca²⁺ -ATPase of erythrocytes of humans having primary liver cancer (PLC) and kwashiorkor was assessed. The specific activity of membrane-bound microsomal Ca²⁺ -ATPase of the liver of untreated rats was 4.543 ± 0.857 µmole P/mg protein/hr at pH 8.0 and was insensitive to calmodulin. The specific activity of the enzyme was significantly decreased (P<0.01) following the ingestion of low protein diet by rats for 12 weeks. The mean Ca²⁺ -ATPase activity of AFB₁ -treated animals (In the absence of dicophane) was not significantly differently (P>0.05) from that of AFB₁ -treated rats which subsequently received dicophane. In contrast, liver microsomal Ca 2+ -ATPase activity of animals fed low protein diet prior to and after AFB ingestion was higher (P<0.05) than that of animals which were on low protein diet only. Basal activity of erythrocyte Ca²⁺ -ATPase in paediatric controls and those having kwashiorkor (protein-energy-malnutrition) were similar (P>0.05); similar observations were made between normal adults and those suffering from PLC. Erythrocyte Ca²⁺ -ATPase of either PLC or Kwashiorkor patients was however, somewhat, less sensitive (15-40%) to the stimulatory effect of calmodulin, an endogenous activator of the Ca²⁺ -pump. This results suggests that liver microsomal Ca²⁺ -ATPase could be useful biochemical marker to determine the onset or occurence of tumour promotion in liver cells. Finally, chronic dietory protein malnutrition mimics the effect of chemical liver tumour promoters and could possibly enhance the development of human PLC particularly in those areas of the tropics where malnutrition is prevalent. Future confirmatory experiments are however required to fully justify this postulate.en_US
dc.language.isoenen_US
dc.subjectRat liveren_US
dc.subjectmicrosomal calcium ion-pumping ATPaseen_US
dc.subjectLow protein intakeen_US
dc.subjectModulationen_US
dc.subjectDicophaneen_US
dc.titleTHE MODULATION OF RAT LIVER MICROSOMAL CALCIUM ION-PUMPING ATPase BY DICOPHANE AND LOW PROTEIN INTAKEen_US
dc.typeThesisen_US
Appears in Collections:Theses in Biochemistry

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