You G, Smith C P, Kanai Y, Lee W S, Stelzner M, Hediger M A
Department of Medicine, Brigham and Women's Hospital, Boston, Massachusetts.
Nature. 1993 Oct 28;365(6449):844-7. doi: 10.1038/365844a0.
Urea is the principal end product of nitrogen metabolism in mammals. Movement of urea across cell membranes was originally thought to occur by lipid-phase permeation, but recent studies have revealed the existence of specialized transporters with a low affinity for urea (Km > 200 mM)2. Here we report the isolation of a complementary DNA from rabbit renal medulla that encodes a 397-amino-acid membrane glycoprotein, UT2, with the functional characteristics of the vasopressin-sensitive urea transporter previously described in in vitro-perfused inner medullary collecting ducts. UT2 is not homologous to any known protein and displays a unique pattern of hydrophobicity. Because of the central role of this transporter in fluid balance and nitrogen metabolism, the study of this protein will provide important insights into the urinary concentrating mechanism and nitrogen balance.
尿素是哺乳动物氮代谢的主要终产物。尿素跨细胞膜的转运最初被认为是通过脂相渗透进行的,但最近的研究揭示了存在对尿素亲和力较低(Km>200 mM)的特殊转运体。在这里,我们报告了从兔肾髓质中分离出的一种互补DNA,它编码一种397个氨基酸的膜糖蛋白UT2,具有先前在体外灌注的内髓集合管中描述的血管加压素敏感性尿素转运体的功能特性。UT2与任何已知蛋白质都不同源,并呈现出独特的疏水性模式。由于这种转运体在体液平衡和氮代谢中的核心作用,对该蛋白质的研究将为尿液浓缩机制和氮平衡提供重要的见解。