Internalization of E. coli ST mediated by guanylyl cyclase C in T84 human colon carcinoma cells.
Publication/Presentation Date
8-17-1995
Abstract
Internalization of Escherichia coli heat-stable enterotoxin (ST) mediated by guanylyl cyclase C was examined in T84 human colon carcinoma cells. Surface-associated, receptor-bound ST was quantitatively separated from intracellular ligand employing acidic guanidine-HCl. ST was internalized in a time-, temperature-, and ligand concentration-dependent fashion only by cells specifically expressing guanylyl cyclase C. Only receptors which bound reversibly to ST appeared to mediate endocytosis. The rate of internalization of ST empirically determined in these studies was 0.23 min-1. The density of surface receptors for ST was similar at 4 degrees C and 37 degrees C, suggesting that these receptors recycle back to the cell surface following internalization of ligand. Similarly, internalized ST was rapidly cleared from the intracellular compartment following endocytosis. These studies demonstrate that ST undergoes ligand-dependent receptor-mediated endocytosis in human colon carcinoma cells.
Volume
1245
Issue
1
First Page
29
Last Page
36
ISSN
0006-3002
Published In/Presented At
Urbanski, R., Carrithers, S. L., & Waldman, S. A. (1995). Internalization of E. coli ST mediated by guanylyl cyclase C in T84 human colon carcinoma cells. Biochimica et biophysica acta, 1245(1), 29–36. https://doi.org/10.1016/0304-4165(95)00068-m
Disciplines
Business Administration, Management, and Operations | Health and Medical Administration | Management Sciences and Quantitative Methods
PubMedID
7654763
Department(s)
Administration and Leadership
Document Type
Article