Association and dissociation of Escherichia coli heat-stable enterotoxin from rat brush border membrane receptors.

Abstract:

:Escherichia coli heat-stable enterotoxin (ST) binds to receptors on rat intestinal cells and brush border membranes (BBM). We devised experiments to examine the reversibility of ST binding. We found that both 125I-labeled ST and native ST were spontaneously dissociable from the BBM receptor. Radiolabeled ST bound to BBM was also dissociated by the addition of avid goat anti-ST antiserum. Furthermore, using a computer program for analysis of ligand binding, we calculated an apparent Ka of 10(8) liters/mol from competitive inhibition and saturation-binding data. This is significantly lower than the value previously reported by others. Our findings, of a lower Ka and a reversible ST-binding process, suggest that a therapeutic strategy of removing bound ST from its receptor or competing with the enterocyte receptor for unbound ST might be successful in terminating ST-induced secretion.

journal_name

Infect Immun

journal_title

Infection and immunity

authors

Cohen MB,Thompson MR,Overmann GJ,Giannella RA

doi

10.1128/IAI.55.2.329-334.1987

subject

Has Abstract

pub_date

1987-02-01 00:00:00

pages

329-34

issue

2

eissn

0019-9567

issn

1098-5522

journal_volume

55

pub_type

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