Sanchís D, Alemany M, Remesar X
Departament de Bioquímica i Fisiologia, Facultat de Biologia, Universitat de Barcelona, Spain.
Biochim Biophys Acta. 1994 Jun 22;1192(2):159-66. doi: 10.1016/0005-2736(94)90114-7.
Membrane vesicles from the small intestine brush border were obtained and used to determine the possible effects of genetic or nutritional obesity on L-alanine uptake. Membrane vesicles from Zucker fa/fa obese rats and cafeteria diet-fed Zucker Fa/? rats showed the same characteristics as those of standard diet-fed lean animals. All preparations showed sodium-dependent transport as the main pathway for L-alanine uptake within the substrate concentration range tested. The apparent substrate affinity constant (Km) values and the pattern of inhibition of Na(+)-dependent L-alanine uptake by other amino acids (L-leucine and L-glutamine), suggests that system B involved in the transport of dipolar amino acids (formerly named Neutral Brush Border System) participates in the Na(+)-dependent transport of L-alanine. The affinity constant (Km) for L-alanine was essentially the same for all the groups studied (in the range of 10 mM). However, there was a higher (P < 0.05) maximal capacity (Vmax) in preparations from diet-induced obese animals (cafeteria diet) than that of genetically obese rats. These results indicate that either nutritional or genetic obesity may modify the capacity but not the affinity of transport systems for L-alanine uptake in the brush border of rat small intestine.
从小肠刷状缘获取膜囊泡,并用于确定遗传或营养性肥胖对L-丙氨酸摄取的可能影响。来自Zucker fa/fa肥胖大鼠和喂食自助餐厅饮食的Zucker Fa/?大鼠的膜囊泡表现出与喂食标准饮食的瘦动物相同的特征。在测试的底物浓度范围内,所有制剂均显示钠依赖性转运是L-丙氨酸摄取的主要途径。表观底物亲和力常数(Km)值以及其他氨基酸(L-亮氨酸和L-谷氨酰胺)对Na(+)-依赖性L-丙氨酸摄取的抑制模式表明,参与双极性氨基酸转运的系统B(以前称为中性刷状缘系统)参与了L-丙氨酸的Na(+)-依赖性转运。所研究的所有组中L-丙氨酸的亲和力常数(Km)基本相同(在10 mM范围内)。然而,饮食诱导的肥胖动物(自助餐厅饮食)的制剂中的最大容量(Vmax)高于遗传性肥胖大鼠(P < 0.05)。这些结果表明,营养性或遗传性肥胖可能会改变大鼠小肠刷状缘中L-丙氨酸摄取转运系统的容量,但不会改变其亲和力。