Open Access Original Research Article

Monosodium Glutamate Induces Oxidative Stress and Affects Glucose Metabolism in the Kidney of Rats

Onyema Oscar Okwudiri, Alisi Chinwe Sylvanus, Ihetuge Adaeze Peace

International Journal of Biochemistry Research & Review, Page 1-11
DOI: 10.9734/IJBCRR/2012/827

Monosodium glutamate (MSG) is a widely used flavour enhancer with a number of adverse effects. Earlier studies have shown the induction of oxidative stress in some organs of experimental animals after chronic administration of MSG. Some reports have also shown some alterations in hepatic glucose metabolism as a result of MSG administration. In this study, we have tested the hypothesis that alteration in glucose metabolism following MSG administration might be a contributor to the changes in the markers of oxidative stress observed in the animals. Twenty four male Wistar rats were divided into two groups. MSG was orally administered to one group of rats at a dose of 4g/kg body weight for ten days while the other group received normal saline. MSG-treated rats showed a significant alteration (P<0.05) in a number of oxidative stress parameters and a significant (P<0.05) increase in the activity of glucose-6-Phosphatase (G6Pase), corroborating earlier observations. In addition, there was a decrease in the activity of glucose-6-phosphate dehydrogenase (G6PD) and a significantly (P<0.05) higher blood glucose and renal glucose concentration in MSG-treated rats. There was no change in renal glycogen concentration following MSG administration. The pattern of induction of oxidative stress and alteration of glucose metabolic enzymes in the animals is an indication that oxidative stress induced by MSG in the renal tissues of rats might be contributed by increased tissue glucose concentration resulting from enhanced renal gluconeogenesis.

Open Access Original Research Article

Genome Wide Identification of Target Heat Shock Protein90 Genes and Their Differential Expression against Heat Stress in Wheat

Ranjeet R. Kumar, Suneha Goswami, Sushil K. Sharma, Himanshu Pathak, Gyanendra K. Rai, Raj D. Rai

International Journal of Biochemistry Research & Review, Page 12-30
DOI: 10.9734/IJBCRR/2012/1134

Aims: To study the genetic and transcript profiling of the genes specifying cytosolic HSP90s in Triticum aestivum.
Study Design: Random sampling.
Place and Duration of Study: Indian Agricultural Research Institute, New Delhi, India, between August to December, 2011.
Methodology: We include C-306 (thermotolerant) and PBW343 (thermosusceptible) cultivars of wheat for the study. Total RNA was isolated using Trizol method and gene was identified and isolated using RT-PCR. In silico characterization was done using different bioinformatic tools. Quantitative real time PCR was carried out using BioRad CFX96 platform and Pfaffl’s method was used for the comparative change in fold expression of the gene.
Results: Here, we report cloning of an HSP90 gene from C-306 wheat cultivar having an ORF of 700 amino acids. Genome Blast identified 3 different clusters of reference sequence on chromosome no 4, 8 and 9 having LOC 100125696 and showing maximum homology with HSP90 reported from Triticum aestivum. Pure amino acid composition revealed highest composition of glutamic acid followed by lysine and leucine whereas, cysteine composition was lowest. Protein characterization showed the existence of 10 networks of coevolved amino acids. Quantitative real time PCR showed 1.5, 4.5, 5 & 7.4 fold increase in expression of HSP90 in case of C-306 compared to 2.5, 6.4, 6.9 & 5.6 fold increase in case of PBW343 at vegetative (root & shoot), pollination and milky dough stage. Multiple co-chaperones of HSP90 were observed by immunoblot assay in response to differential heat shock.
Conclusion: This investigation proves that HSP90 is one of the key components of defense mechanism in wheat against heat stress which requires the formation of co-chaperone complexes with HSP70 for its functional activity. There is a need to exploit the transcription factors associated with HSP90 and its regulation and differential expression in order to use it for developing thermotolerant wheat cultivars.

Open Access Original Research Article

Comparative Study of Thiaminase in Headfoot and Hepatopancreas of Limicolaria flammea (Müller, 1774)

Adenike Kuku, Raphael Emuebie Okonji, Busayo Deborah Akinrinola

International Journal of Biochemistry Research & Review, Page 31-49
DOI: 10.9734/IJBCRR/2012/1087

Aims: This study aimed at determining the level of thiaminase in the Limicolaria flammea with a view to ascertaining the nutritional and health implications of its consumption.
Methodology: Proximate analyses of two tissues, headfoot and hepatopancreas, were investigated to assess their nutritional qualities. The thiaminases in the tissues were purified by chromatographic separations using DEAE-Sephacel ion - exchange and Biogel P-100 columns.
Results: The Michealis Menten constant obtained for hepatopancreas thiaminase was 0.83 mM and 0.13 mM for thiamine and aniline respectively; for the headfoot thiaminase, 1.06 mM and 0.16 mM was obtained for thiamine and aniline respectively. An optimum pH of 8.5 was obtained for thiaminase in the two tissues. Temperature optimum of 65°C and 70°C was obtained for the headfoot and hepatopancreas enzymes respectively. The amino acids and glutathione activated the enzyme from hepatopancreas, while the headfoot enzyme was significantly inhibited except proline which showed very high activation. The cations: NH4+, Hg2+, Mn2+, Na+, Ni2+, and Zn2+ tested showed no inhibition of the enzymes in both tissues. Increased concentrations of 2-mercaptoethanol, 6-amino hexanoic acid and ethylenediaminetetraacetic acid (EDTA) inhibited the activities of thiaminases from the two tissues.
Conclusion: The study concluded that the tissues, hepatopancreas and headfoot of Limicolaria flammea contained high level of thiaminase. This may have medical implication in its consumption as a good source of high quality protein.