Video Experimental Relacionado

Updated: May 12, 2026

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance

Published on: January 3, 2012

La guanilil ciclasa es un receptor de enterotoxinas térmicamente estable

S Schulz¹, C K Green, P S Yuen

¹Howard Hughes Medical Institute, Vanderbilt University Medical Center, Nashville, Tennessee 37232.

|November 30, 1990

Resumen

Los investigadores identificaron un nuevo receptor de guanilil ciclasa C (GC-C) para la enterotoxina térmicamente estable. Este descubrimiento revela la base molecular para la diarrea inducida por enterotoxinas térmicamente estables, identificando a GC-C como el receptor específico.

Área de la Ciencia:

Biología Molecular Biología Molecular
Gastroenterología y Gastroenterología.
La bioquímica es la bioquímica.

Sus antecedentes:

Las membranas plasmáticas de las guanililciclasas son conocidos como receptores de péptidos natriuréticos.
El receptor específico para la enterotoxina estable al calor, una causa de diarrea aguda, no se había caracterizado previamente.

Objetivo del estudio:

Clonar y caracterizar el receptor de la enterotoxina térmicamente estable.
Para determinar si este receptor es una forma de guanylil ciclasa.

Principales métodos:

La clonación del gen GC-C.
Expresión de GC-C en las células COS-7.
Medición de la actividad de la guanylil ciclasa.
Ensayos de unión con enterotoxina térmicamente estable y péptidos natriuréticos.
Mediciones cíclicas del nivel de BPF.

Principales resultados:

Se identificó un nuevo clon de guanilil ciclasa, GC-C.
GC-C codifica un receptor con distintas secuencias extracelulares pero conservando dominios intracelulares.
Las células que expresan GC-C mostraron una alta actividad de la guanylil ciclasa.
Enterotoxina térmicamente estable, pero no péptidos natriuréticos, específicamente unidos a GC-C y niveles elevados de GMP cíclico en las células transfectadas.

Conclusiones:

El receptor de enterotoxinas térmicamente estable es una forma de membrana plasmática de la guanylil ciclasa, designada GC-C.
GC-C media los efectos de la enterotoxina estable al calor, incluida la elevación y unión cíclica de GMP.
Este hallazgo aclara el mecanismo de la diarrea inducida por enterotoxinas térmicamente estables.

Más Videos Relacionados

Analysis of Yersinia enterocolitica Effector Translocation into Host Cells Using Beta-lactamase Effector Fusions

Analysis of Yersinia enterocolitica Effector Translocation into Host Cells Using Beta-lactamase Effector Fusions

Published on: October 13, 2015

A "Dual-Addition" Calcium Fluorescence Assay for the High-Throughput Screening of Recombinant G Protein-Coupled Receptors

A "Dual-Addition" Calcium Fluorescence Assay for the High-Throughput Screening of Recombinant G Protein-Coupled Receptors

Published on: December 2, 2022

Videos de Conceptos Relacionados

G-protein Coupled Receptors

G-protein Coupled Receptors

G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.

G-protein Coupled Receptors

G-protein Coupled Receptors

G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.

Activation and Inactivation of G Proteins

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...

GPCRs Regulate Adenylyl Cylase Activity

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
Two...

Bacterial Gastroenteritis

Bacterial Gastroenteritis

Bacterial gastroenteritis, characterized by diarrhea, abdominal cramps, and vomiting, is often caused by ingestion of contaminated food or water and is frequently associated with pathogenic Escherichia coli strains. These microbes exploit two principal mechanisms to inflict disease.Shiga toxin–producing E. coli, also referred to as STEC—notably O157:H7—release Shiga toxins that target ribosomes, blocking protein synthesis. The B subunit of the toxin binds the host glycolipid receptor...

Cholera

Cholera

Cholera is an acute gastrointestinal disease caused by the Gram-negative bacterium Vibrio cholerae. It is transmitted primarily via the fecal-oral route through the ingestion of contaminated water or food.Vibrio cholerae is a motile, Gram-negative bacterium of the family Vibrionaceae, primarily associated with waterborne outbreaks in areas with inadequate sanitation. Although over 200 serogroups of V. cholerae exist, only O1 and O139 are responsible for epidemic cholera. The O1 serogroup,...