• Korean Journal of Poultry Science
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• v.41 no.2
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• pp.105-113
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• 2014

The current study was performed to investigate the effects of dietary supplementation of dried coffee meal (CM) on growth performance, intestinal and blood biochemical index, intestinal enzymes, and cecal microbial populations. A total of 162, 3-day-old male broiler chicks were randomly allocated into three dietary groups: control group (CON), basal diet added with 0.5% CM (CM I), and basal diet added with 1.0% CM (CM II). Dietary supplementation of CM did not change bird performance and the relative weight of intestinal mucosal tissues. The birds fed the diet supplemented with CM (0.5 and 1.0%) significantly decreased mucosal glucose concentration (P<0.05) without affecting blood glucose level compared with those fed control diet. The level of blood aspartate aminotransferase (AST) significantly increased in CM II group (P<0.05) without affecting ${\gamma}$-glutamyl transpeptidase (${\gamma}$-GTP) compared with that in the CON group. The specific activity of intestinal maltase, leucine aminopeptidase (LAP) and alkaline phosphatase (ALP) were not affected by dietary supplementation of CM, whereas sucrase activity in birds fed the diet supplemented with CM was decreased (P<0.05) compared to that in the control birds. The colony forming units (CFU) of E. coli in the cecum of CM-fed birds was significantly decreased (P<0.05) compared with that of control birds without changing the CFU of Lactobacillus. In conclusion, dietary supplementation of lower level of CM (0.5%) can be used as a beneficial feed resource without liver toxicity in broiler chicks.

• Clinical and Experimental Reproductive Medicine
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• v.34 no.2
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• pp.95-106
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• 2007

Objective: We previously identified differentially expressed genes (DEGs) between germinal vesicle (GV) and metaphase II (MII) mouse oocyte. The present study was accomplished as a preliminary study to elucidate the role of ribose 5-phosphate isomerase A (Rpia), the essential enzyme of the pentose phosphate pathway (PPP), in oocyte maturation. We observed expression of Rpia in the mouse and porcine oocytes. Methods: Expression pattern of the 11 MII-selective DEGs in various tissues was evaluated using RT-PCR and selected 4 genes highly expressed in the ovary. According to the oocyte-selective expression profile, we selected Rpia as a target for this study. We identified the porcine Rpia sequence using EST clustering technique, since it is not yet registered in public databases. Results: The extended porcine Rpia nucleotide sequence was submitted and registered to GenBank (accession number EF213106). We prepared primers for porcine Rpia according to this sequence. In contrast to the oocyte-specific expression in the mouse, Rpia was expressed in porcine cumulus and granulosa cells as well as in oocytes. Conclusion: This is the first report on the characterization of the Rpia gene in the mouse and porcine ovarian cells. Results of the present study suggest that the mouse and porcine COCs employ different mechanism of glucose metabolism. Therefore, the different metabolic pathways during in vitro oocyte maturation (IVM) in different species may lead different maturation rates. It is required to study further regarding the role of Rpia in glucose metabolism of oocytes and follicular cell fore exploring the regulatory mechanism of oocyte maturation as well as for finding the finest culture conditions for in vitro maturation.