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Receptors for Escherichia coli heat stable enterotoxin in human intestine and in a human intestinal cell line (Caco-2)

✍ Scribed by Mitchell B. Cohen; Nancy J. Jensen; Jennifer A. Hawkins; Elizabeth A. Mann; Michael R. Thompson; Michael J. Lentze; Ralph A. Giannella

Publisher
John Wiley and Sons
Year
1993
Tongue
English
Weight
777 KB
Volume
156
Category
Article
ISSN
0021-9541

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✦ Synopsis

bcherichia coli heat stable enterotoxin (ST,) and the newly identified endogenous ligand guanylin bind to an intestinal receptor and activate membrane bound guanylate cyclase. We compared ST, binding and affinity crosslinking of ST, receptors in human small intestine to those in the Caco-2 human colon carcinoma cell line. ST, had similar kinetics of binding in human intestinal and Caco-2 brush border membranes. In both human intestine and Caco-2 brush border membranes, multiple specifically radiolabeled bands, including a 140-1 65 kDa band, were identified by affinity crosslinking. However, in human intestine the most prominent autoradiographic species was a 60 kDa band. A 60 kDa protein was also specifically immunoprecipitated from solubilized human brush border membranes using antisera raised against a cloned ST, receptor fusion protein. Our observations of multiple crosslinked proteins in human intestine and Caco-2 cells could be explained by the existence of several members of a family of ST, receptors and/or the existence of smaller ST, binding proteins generated by the protease cleavage of a larger complete ST, receptor. o 1993 ~~l e y -~i s s , Inc.

Methods

ST, and ~-T Y ~-~' ~I -S T , ST, from E. coli 18D was purified as previously described by Staples et al. (1980). Nal"I (Amersham, Ar-

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