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Vol. 57, Issue 5, 913-925, May 2000
-Conotoxin MII Identifies a Novel Nicotinic
Acetylcholine Receptor Population in Mouse Brain
Institute for Behavioral Genetics, University of Colorado, Boulder,
Colorado (P.W., A.C.C., M.J.W.), and Departments of Biology
(J.M.M., S.L.) and Psychiatry (J.M.M.), University of Utah,
Salt Lake City, Utah.
-Conotoxin MII (CtxMII), a peptide toxin from the venom of the
predatory cone snail Conus magus, displays an unusual
nicotinic pharmacology. Specific binding of a radioiodinated derivative (125I--CtxMII) was identified in brain region
homogenates and tissue sections. Quantitative autoradiography indicated
that 125I--CtxMII binding sites have an unique
pharmacological profile and distribution in mouse brain, being largely
confined to the superficial layers of the superior colliculus,
nigrostriatal pathway, optic tract, olivary pretectal, and mediolateral
and dorsolateral geniculate nuclei. Expression of -CtxMII binding
sites in the nigrostriatal pathway, combined with evidence for
-CtxMII-sensitivity of nicotine-induced
[3H]dopamine release in rodent striatal preparations
indicates that 125I--CtxMII binding nicotinic
acetylcholine receptors are likely to be physiologically important.
Unlabeled -CtxMII potently (Ki < 3 nM) competed for a subset of [3H]epibatidine binding
sites in mouse brain homogenates, but weakly (IC50 > 10 µM) interacted with 125I--bungarotoxin and
(
)-[3H]nicotine binding sites, confirming this
compound's novel nicotinic pharmacology. Quantitative autoradiography
revealed that -CtxMII binds with high affinity at a subset of
[3H]epibatidine binding sites with relatively low
cytisine affinity ("cytisine-resistant" sites), resolving
[3H]epibatidine binding into three different populations,
each probably corresponding to a receptor subtype. The majority
population seems to correspond to that which binds nicotine and
cytisine with high affinity ("cytisine-sensitive" sites).
Comparison of the cytisine-resistant population's distribution with
that of 3 subunit mRNA expression suggests that the fractions both
more and less sensitive to -CtxMII probably contain the 3
subunit, perhaps in combination with different 
subunits.
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