scholarly journals The Heat-Stable Enterotoxin Receptor, Guanylyl Cyclase C, as a Pharmacological Target in Colorectal Cancer Immunotherapy: A Bench-to-Bedside Current Report

Toxins ◽  
2017 ◽  
Vol 9 (9) ◽  
pp. 282 ◽  
Author(s):  
Trevor Baybutt ◽  
Allison Aka ◽  
Adam Snook
Keyword(s):  
Colorectal Cancer ◽  
Cancer Immunotherapy ◽  
Guanylyl Cyclase ◽  
Guanylyl Cyclase C ◽  
Heat Stable ◽  
Pharmacological Target ◽  
Current Report

Identification of a binding region onEscherichia coli heat-stable enterotoxin to intestinal guanylyl cyclase C

1997 ◽  
Vol 4 (1) ◽  
pp. 1-11 ◽  
Author(s):  
Makoto Hasegawa ◽  
Yuki Kawano ◽  
Kazuya Matsumoto ◽  
Yuji Hidaka ◽  
Takashi Sato ◽  
...  
Keyword(s):  
Guanylyl Cyclase ◽  
Guanylyl Cyclase C ◽  
Binding Region ◽  
Heat Stable

scholarly journals A Novel PDZ Protein Regulates the Activity of Guanylyl Cyclase C, the Heat-stable Enterotoxin Receptor

2002 ◽  
Vol 277 (25) ◽  
pp. 22934-22941 ◽  
Author(s):  
Robert O. Scott ◽  
William R. Thelin ◽  
Sharon L. Milgram
Keyword(s):  
Guanylyl Cyclase ◽  
Guanylyl Cyclase C ◽  
Heat Stable ◽  
Pdz Protein

Guanylyl Cyclase C Messenger RNA Is a Biomarker for Recurrent Stage II Colorectal Cancer

1999 ◽  
Vol 131 (11) ◽  
pp. 805 ◽  
Author(s):  
Burt Cagir ◽  
Alyssa Gelmann ◽  
Jason Park ◽  
Tracy Fava ◽  
Alexander Tankelevitch ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Guanylyl Cyclase ◽  
Messenger Rna ◽  
Stage Ii ◽  
Guanylyl Cyclase C ◽  
Stage Ii Colorectal Cancer

Differential processing of guanylyl cyclase C along villus-crypt axis of rat small intestine

1997 ◽  
Vol 272 (6) ◽  
pp. C1995-C2004 ◽  
Author(s):  
L. A. Scheving ◽  
K. M. Chong
Keyword(s):  
Guanylyl Cyclase ◽  
Limited Proteolysis ◽  
Structural Heterogeneity ◽  
Proteolytic Processing ◽  
Enterotoxigenic Escherichia Coli ◽  
Guanylyl Cyclase C ◽  
Heat Stable ◽  
Molecular Events ◽  
Cell Fractions ◽  
Carboxy Terminal

Many strains of enterotoxigenic Escherichia coli produce a heat-stable peptide enterotoxin (STa) that binds to the intestinal receptor guanylyl cyclase C (GC-C). STa receptors are structurally heterogeneous, but the molecular events causing this heterogeneity remain obscure. We examined the influence of cell position along the villus-crypt axis on STa receptor heterogeneity by fractionating EDTA-dissociated cells that detached in a villus-to-crypt direction. STa affinity labeling experiments revealed that the initially released villus “tip” fraction had four major STa binding proteins (STBPs), with relative molecular weight (M(r)) of 150,000, 135,000, 125,000, and 95,000, that did not react with a GC-C carboxy-terminal antibody. Yet succeeding villus cell fractions had major immunoreactive STBPs with M(r) of 275,000 and 250,000. Limited proteolysis of these larger GC-C isoforms produced 1) smaller STBPs that had M(r) similar to those in the initial villus fraction, 2) a 65,000 M(r) protein GC-C isoform that did not bind STa, and 3) elevated basal and STa-induced cyclase activity. Our data show that STBP structural heterogeneity in the intact intestine arises largely from multisite proteolytic processing of GC-C.

Sign in / Sign up

Export Citation Format

Share Document