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Vol. 286, Issue 1, 311-320, July 1998
5 Subunit Alters Desensitization, Pharmacology,
Ca++ Permeability and Ca++ Modulation of Human
Neuronal 3 Nicotinic Receptors1
Department of Neuroscience, University of Pennsylvania Medical
School, Philadelphia, Pennsylvania
Functional effects of human 
5 nicotinic ACh receptor (AChR) subunits
coassembled with 3 and 
2 or with 3 and 4 subunits, were
investigated in Xenopus oocytes. The presence of 5
subunits altered some properties of both 3 AChRs and differentially
altered other properties of 32 AChRs vs. 34
AChRs. 5 subunits increased desensitization and Ca++
permeability of all 3 AChRs. The Ca++ permeabilities of
both 325 and 345 AChRs were comparable to that of
7 AChRs. As we have shown previously, 5 subunits increased the
ACh sensitivity of 32 AChRs 50-fold but had little effect on
34 AChRs. 5 caused only subtle changes in the activation potencies of 3 AChRs for nicotine, cytisine and
1,1-dimethyl-4-plenylpiperazinium (DMPP). However, 5 increased the
efficacies of nicotine and DMPP on 32 AChRs but decreased them on
34 AChRs. Immunoisolation of cloned human AChRs expressed in
oocytes showed that 5 efficiently coassembled with 3 plus 2
and/or 4 subunits. As expected, human AChRs immunoisolated from
SH-SY5Y neuroblastoma cells showed that AChRs containing 3 and
probably 5 subunits were present, but 4 AChRs were not. In brain,
by contrast, 42 AChRs were shown to predominate over 3 AChRs.
Some of the brain 42 AChRs were found to contain 5 subunits.
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