Changes in activities of lipogenic enzymes in adipose tissue and liver of growing goats.
The lipogenic capacity of omental adipose tissue and liver was measured in vitro from samples obtained at slaughter from 33 young male goats. The animals were slaughtered either on the day of weaning (d 0) or 2, 14, or 56 d after weaning. Ages at weaning were 4 wk (early weaning) or 6 or 8 wk (late weaning). Blood samples from the jugular vein were taken before slaughter to measure the concentrations of plasma glucose and nonesterified fatty acids. There was a 30% decrease in glucose concentration after weaning. Nonesterified fatty acid concentration increased fourfold between d 0 and 2 after weaning. By d 14 after weaning, nonesterified fatty acids returned to basal concentration. The lipoprotein lipase (LPL) activity of adipose tissue declined markedly (90%) on d 2 after weaning. Lipoprotein lipase activity returned to preweaning values by d 56 after weaning in those goats that had ad libitum access to feed. In adipose tissue, nicotinamide adenine dinucleotide phosphate (NADP)-malate dehydrogenase activity fell by only 17% by d 2 after weaning and to 63% by d 14 after weaning. Lipoprotein lipase activity was closely related to metabolizable energy intake the day before slaughter. Acetyl-coenzyme A carboxylase activity was low in adipose tissue and it increased only slightly by d 56 after weaning. The data indicated that LPL played a preponderant role in the restoration of lipid stores after weaning. High NADP-malate dehydrogenase activity together with a high concentration of plasma glucose by d 56 after weaning suggested that this enzyme activity could be enhanced by high glucose availability in goat kids. Activities of lipase, acetyl-coenzyme A carboxylase, NADP-malate dehydrogenase, and glucose-6-phosphate dehydrogenase in liver were essentially unaffected by weaning. The extent and rapidity of change of lipogenic enzymes of goat kids was much more pronounced in adipose tissue than in liver.
Station de Nutrition et Alimentation, INRA, Paris, France.
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D000103:Acetyl-CoA Carboxylase / Q000032:analysis; D000273:Adipose Tissue / Q000201:enzymology* / Q000254:growth & development; D000818:Animals; D001786:Blood Glucose / Q000032:analysis; D005230:Fatty Acids, Nonesterified / Q000097:blood; D005954:Glucosephosphate Dehydrogenase / Q000032:analysis; D006041:Goats / Q000097:blood / Q000254:growth & development / Q000378:metabolism*; D008049:Lipase / Q000032:analysis; D008071:Lipoprotein Lipase / Q000032:analysis; D008099:Liver / Q000201:enzymology* / Q000254:growth & development; D008291:Malate Dehydrogenase / Q000032:analysis; D008297:Male; D009852:Omentum; D009929:Organ Size
D001786:Blood Glucose; D005230:Fatty Acids, Nonesterified; D008291:Malate Dehydrogenase; D005954:Glucosephosphate Dehydrogenase; D008049:Lipase; D008071:Lipoprotein Lipase; D000103:Acetyl-CoA Carboxylase