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Single channel properties of human α3 AChRs: impact of β2, β4 and α5 subunits
Author(s) -
Nelson Mark E.,
Lindstrom Jon
Publication year - 1999
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1111/j.1469-7793.1999.0657u.x
Subject(s) - hexamethonium , xenopus , protein subunit , acetylcholine receptor , mecamylamine , chemistry , biophysics , receptor , biology , biochemistry , gene
1 We performed single channel analysis on human α3 acetylcholine receptors (AChRs) in Xenopus oocytes and native AChRs from the human neuroblastoma cell line IMR‐32. α3 AChRs exhibit channel properties that reflect subunit composition. 2 α3β2 AChR open times were 0.71 ± 0.14 and 3.5 ± 0.4 ms with a predominant conductance of 26 pS. α3β4 AChRs had open times of 1.4 ± 0.2 and 6.5 ± 0.8 ms and a predominant conductance of 31 pS. Burst times were 0.82 ± 0.12 and 5.3 ± 0.7 ms for α3β2 and 1.7 ± 0.1 and 16 ± 1 ms for α3β4. Desensitization was faster for AChRs with the β2 subunit than for those with the β4 subunit. 3 One open time for α3α5β2 AChRs (5.5 ± 0.3 ms) was different from those of α3β2 AChRs. For α3α5β4 AChRs, an additional conductance, open time and burst time (36 pS, 22 ± 3 ms and 43 ± 4 ms, respectively) were different from those for α3β4 AChRs. 4 α3 AChRs were inhibited by hexamethonium or mecamylamine. The rate constants for block of α3β4 by hexamethonium and of α3β2 by mecamylamine were 1.2 × 10 7 and 4.6 × 10 7 M −1 s −1 , respectively. 5 AChRs from IMR‐32 cells had a predominant conductance of 32 pS and open times of 1.5 ± 0.3 and 9.6 ± 1.2 ms. These properties were most similar to those of α3β4 AChRs expressed in oocytes. Antibodies revealed that 5 ± 2 % of IMR‐32 α3 AChRs contained α5 subunits and 6 ± 2 % contained β2 subunits. IMR‐32 α3 AChRs are primarily α3β4 AChRs.