Sandbox 174
From Proteopedia
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Contents |
Alpha-Bungarotoxin
Alpha-Bungarotoxin (α-BGT) is a nicotinic cholinergic antagonist that is found within the venom of Bungarus multicinctus, a South-asian snake commonly known as kraits. α-BGT is known to bind irreversibly to the acetylcholine receptor found at the neuromuscular junction, causing respiratory failure, paralysis, and death, as well as play an antagonstic role in binding the α7 nicotinic acetylcholine receptor in the brain.
Structure
General Structure
Functions
α7 nicotinic acetylcholine receptor binding
Reponse to sensory stimuli and seizure genesis has been linked to nicotinic mechanisms[1].
Seizure genesisa nd habituation of responseto sensorys timuli have been linked to nicotinic mechanisms (Marks et al., 1989;
Luntz-Leybman et al., 1992). These functions are closely associated
with the CA3 field (Schwartzkroin, 1986; Bickford-
Wimer et al., 1990). Nicotinic responsesa re mediated by two
major classeso f receptors, ganglionic type and neuromuscular
type. Pharmacological analysis of both seizure genesis and habituation
in rat brain implicates mediation by a neuromuscular
type (Miner and Collins, 1989; Luntz-Leybman et al., 1992).
These data are supported by the prominent binding of the neuromuscular-
type antagonist oc-bungarotoxin (a-BT) in the CA3
field of the hippocampus (Hunt and Schmidt, 1978; Segal et al.,
1978; Clarke et al., 1985
neuromuscular acetylcholine receptor binding
References
- ↑ a-Bungarotoxin Binding to Hippocampal Interneurons: lmmunocytochemical Characterization and Effects on Growth Factor Expression
| Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof.Andrea Gorrell. |
