Descriptor English: | Cholera Toxin | ||||||
Descriptor Spanish: |
Toxina del Cólera
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Descriptor Portuguese: | Toxina da Cólera | ||||||
Descriptor French: | Toxine cholérique | ||||||
Entry term(s): |
CT, Cholera Enterotoxin Cholera Enterotoxin CT Cholera Exotoxin Cholera Toxin A Cholera Toxin A Subunit Cholera Toxin B Cholera Toxin B Subunit Cholera Toxin Protomer A Cholera Toxin Protomer B Cholera Toxin Subunit A Cholera Toxin Subunit B Choleragen Choleragenoid Enterotoxin CT, Cholera Exotoxin, Cholera Procholeragenoid Toxin A, Cholera Toxin B, Cholera Toxin, Cholera |
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Tree number(s): |
D08.811.913.400.725.115.180 D23.946.123.194 D23.946.330.150 |
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RDF Unique Identifier: | https://id.nlm.nih.gov/mesh/D002772 | ||||||
Scope note: | An ENTEROTOXIN from VIBRIO CHOLERAE. It consists of two major protomers, the heavy (H) or A subunit and the B protomer which consists of 5 light (L) or B subunits. The catalytic A subunit is proteolytically cleaved into fragments A1 and A2. The A1 fragment is a MONO(ADP-RIBOSE) TRANSFERASE. The B protomer binds cholera toxin to intestinal epithelial cells and facilitates the uptake of the A1 fragment. The A1 catalyzed transfer of ADP-RIBOSE to the alpha subunits of heterotrimeric G PROTEINS activates the production of CYCLIC AMP. Increased levels of cyclic AMP are thought to modulate release of fluid and electrolytes from intestinal crypt cells. |
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Annotation: | /antag permitted but consider also ANTITOXINS |
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Allowable Qualifiers: |
AD administration & dosage AE adverse effects AG agonists AI antagonists & inhibitors AN analysis BI biosynthesis BL blood CF cerebrospinal fluid CH chemistry CL classification CS chemical synthesis EC economics GE genetics HI history IM immunology IP isolation & purification ME metabolism PD pharmacology PH physiology PK pharmacokinetics PO poisoning RE radiation effects SD supply & distribution ST standards TO toxicity TU therapeutic use UR urine |
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Pharm Action: |
Adjuvants, Immunologic Poisons |
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Registry Number: | 9012-63-9 | ||||||
Previous Indexing: |
Bacterial Proteins (1966-1977) Bacterial Toxins (1977) Enterotoxins (1966-1977) Toxins (1966-1967) |
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Public MeSH Note: | 78 |
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History Note: | 78 |
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DeCS ID: | 2822 | ||||||
Unique ID: | D002772 | ||||||
NLM Classification: | WC 262 | ||||||
Documents indexed in the Virtual Health Library (VHL): | Click here to access the VHL documents | ||||||
Date Established: | 1978/01/01 | ||||||
Date of Entry: | 1977/04/22 | ||||||
Revision Date: | 2020/05/27 |
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CHEMICALS AND DRUGS
Enzymes and Coenzymes [D08]Enzymes and Coenzymes -
CHEMICALS AND DRUGS
Biological Factors [D23]Biological Factors -
CHEMICALS AND DRUGS
Biological Factors [D23]Biological Factors
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Cholera Toxin
- Preferred
Choleragenoid
- Narrower
Procholeragenoid
- Narrower
Cholera Toxin Protomer A
- Narrower
Concept UI |
M0004245 |
Scope note | An ENTEROTOXIN from VIBRIO CHOLERAE. It consists of two major protomers, the heavy (H) or A subunit and the B protomer which consists of 5 light (L) or B subunits. The catalytic A subunit is proteolytically cleaved into fragments A1 and A2. The A1 fragment is a MONO(ADP-RIBOSE) TRANSFERASE. The B protomer binds cholera toxin to intestinal epithelial cells and facilitates the uptake of the A1 fragment. The A1 catalyzed transfer of ADP-RIBOSE to the alpha subunits of heterotrimeric G PROTEINS activates the production of CYCLIC AMP. Increased levels of cyclic AMP are thought to modulate release of fluid and electrolytes from intestinal crypt cells. |
Preferred term | Cholera Toxin |
Entry term(s) |
CT, Cholera Enterotoxin Cholera Enterotoxin CT Cholera Exotoxin Choleragen Enterotoxin CT, Cholera Exotoxin, Cholera Toxin, Cholera |
Concept UI |
M0004246 |
Scope note | An ENTEROTOXIN from VIBRIO CHOLERAE. It consists of two major protomers, the heavy (H) or A subunit and the B protomer which consists of 5 light (L) or B subunits. The catalytic A subunit is proteolytically cleaved into fragments A1 and A2. The A1 fragment is a MONO(ADP-RIBOSE) TRANSFERASE. The B protomer binds cholera toxin to intestinal epithelial cells and facilitates the uptake of the A1 fragment. The A1 catalyzed transfer of ADP-RIBOSE to the alpha subunits of heterotrimeric G PROTEINS activates the production of CYCLIC AMP. Increased levels of cyclic AMP are thought to modulate release of fluid and electrolytes from intestinal crypt cells. |
Preferred term | Choleragenoid |
Entry term(s) |
Cholera Toxin B Cholera Toxin B Subunit Cholera Toxin Protomer B Cholera Toxin Subunit B Toxin B, Cholera |
Concept UI |
M0004250 |
Scope note | An ENTEROTOXIN from VIBRIO CHOLERAE. It consists of two major protomers, the heavy (H) or A subunit and the B protomer which consists of 5 light (L) or B subunits. The catalytic A subunit is proteolytically cleaved into fragments A1 and A2. The A1 fragment is a MONO(ADP-RIBOSE) TRANSFERASE. The B protomer binds cholera toxin to intestinal epithelial cells and facilitates the uptake of the A1 fragment. The A1 catalyzed transfer of ADP-RIBOSE to the alpha subunits of heterotrimeric G PROTEINS activates the production of CYCLIC AMP. Increased levels of cyclic AMP are thought to modulate release of fluid and electrolytes from intestinal crypt cells. |
Preferred term | Procholeragenoid |
Concept UI |
M0004247 |
Scope note | An ENTEROTOXIN from VIBRIO CHOLERAE. It consists of two major protomers, the heavy (H) or A subunit and the B protomer which consists of 5 light (L) or B subunits. The catalytic A subunit is proteolytically cleaved into fragments A1 and A2. The A1 fragment is a MONO(ADP-RIBOSE) TRANSFERASE. The B protomer binds cholera toxin to intestinal epithelial cells and facilitates the uptake of the A1 fragment. The A1 catalyzed transfer of ADP-RIBOSE to the alpha subunits of heterotrimeric G PROTEINS activates the production of CYCLIC AMP. Increased levels of cyclic AMP are thought to modulate release of fluid and electrolytes from intestinal crypt cells. |
Preferred term | Cholera Toxin Protomer A |
Entry term(s) |
Cholera Toxin A Cholera Toxin A Subunit Cholera Toxin Subunit A Toxin A, Cholera |
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