White A A, Krause W J, Turner J T, Forte L R
John M. Dalton Research Center, Department of Biochemistry, University of Missouri-Columbia 65211.
Biochem Biophys Res Commun. 1989 Feb 28;159(1):363-7. doi: 10.1016/0006-291x(89)92447-9.
The Escherichia coli heat-stable enterotoxin (ST1 or STa) binds to specific receptors on mammalian intestinal brush border membranes, and stimulates guanylate cyclase in those membranes. We have found a similar signal transduction system in brush border membranes prepared from kidney cortex of the American opossum (Didelphis virginiana, and in a cell line (OK cell) derived from that tissue. Activation of guanylate cyclase by ST1 is therefore not limited to intestinal cells. Furthermore, since it is unlikely that ST1 which is produced in the intestinal lumen, would have access to kidney receptors, this suggests the existence of an endogenous peptide resembling ST1, at least in marsupials.
大肠杆菌热稳定肠毒素(ST1或STa)与哺乳动物肠道刷状缘膜上的特定受体结合,并刺激这些膜中的鸟苷酸环化酶。我们在美国负鼠(弗吉尼亚负鼠)肾皮质制备的刷状缘膜以及从该组织衍生的细胞系(OK细胞)中发现了类似的信号转导系统。因此,ST1对鸟苷酸环化酶的激活并不局限于肠道细胞。此外,由于肠腔中产生的ST1不太可能接触到肾脏受体,这表明至少在有袋动物中存在一种类似于ST1的内源性肽。