Escherichia coli enterotoxin (STa) binds to receptors, stimulates guanyl cyclase, and impairs absorption in rat colon.
Escherichia coli enterotoxin (STa) binds to receptors, stimulates guanyl cyclase, and impairs absorption in rat colon.
复制标题
大肠杆菌肠毒素 (STa) 与受体结合,刺激鸟苷酸环化酶,并损害大鼠结肠的吸收。
DOI:
10.1016/0016-5085(92)90163-s
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发表时间:
1992
期刊:
影响因子:
29.4
通讯作者:
Cohen,MB
中科院分区:
文献类型:
--
作者:
Mezoff,AG;Giannella,RA;Eade,MN;Cohen,MB
To determine the contribution of the colon inEscherichia coliheat-stable enterotoxin-mediated diarrheal disease, toxin binding, guanyl cyclase activation, and toxin-induced water flux in the rat colon and ileum were compared. Scatchard analysis suggested a single class of heat-stable enterotoxin receptors with an affinity constant of binding of 109L/mol in both colonocytes and ileocytes; however, the number of toxin receptors per cell was 3.5-fold greater in colonocytes than ileocytes (8.32 ± 1.33 × 105vs. 2.33 ± 0.28 × 105receptors per cell;P= 0.02). Heat-stable enterotoxin stimulated guanyl cyclase activation in an identical dose-dependent manner in proximal colonic and ileal membranes, with similar sensitivity and maximum response. Heat-stable enterotoxin also inhibited net water flux to a similar degree in both colon and ileum (−47.8 vs. −48.4 μL · cm−1· h−1, respectively) at a dose of 8 nmol/L. At this dose in the colon, because of a higher baseline of absorption, absorption continued, but at a diminished level. At this dose in the ileum, heat-stable enterotoxin induced net secretion. These data are consistent with the concept that heat-stable enterotoxin-induced diarrheal disease results from a decreased absorptive capacity in the colon in the face of increased small intestinal fluid secretion.