Characterization of nicotinic acetylcholine receptors on cultured bovine adrenal chromaffin cells using modified l-[3H]nicotine binding assay

1992 ◽  
Vol 345 (4) ◽  
Author(s):  
Ken Lee ◽  
Soichi Miwa ◽  
Kunio Koshimura ◽  
Akihiro Ito
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Chromaffin Cells ◽  
Binding Assay ◽  
Adrenal Chromaffin Cells ◽  
Nicotinic Acetylcholine ◽  
Adrenal Chromaffin

Characterization of the functional subunit combination of nicotinic acetylcholine receptors in bovine adrenal chromaffin cells

2001 ◽  
Vol 312 (3) ◽  
pp. 161-164 ◽  
Author(s):  
Eiichi Tachikawa ◽  
Kenzo Mizuma ◽  
Kenzo Kudo ◽  
Takeshi Kashimoto ◽  
Susumu Yamato ◽  
...  
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Chromaffin Cells ◽  
Adrenal Chromaffin Cells ◽  
Nicotinic Acetylcholine ◽  
Subunit Combination ◽  
Adrenal Chromaffin

scholarly journals Expression of α3β2β4 nicotinic acetylcholine receptors by rat adrenal chromaffin cells determined using novel conopeptide antagonists

2020 ◽  
Vol 154 (2) ◽  
pp. 158-176 ◽  
Author(s):  
Arik J. Hone ◽  
Lola Rueda‐Ruzafa ◽  
Thomas J. Gordon ◽  
Joanna Gajewiak ◽  
Sean Christensen ◽  
...  
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Chromaffin Cells ◽  
Adrenal Chromaffin Cells ◽  
Nicotinic Acetylcholine ◽  
Adrenal Chromaffin

scholarly journals Monkey Adrenal Chromaffin Cells Express α6β4* Nicotinic Acetylcholine Receptors

PLoS ONE ◽  
2014 ◽  
Vol 9 (4) ◽  
pp. e94142 ◽  
Author(s):  
Alicia Hernández-Vivanco ◽  
Arik J. Hone ◽  
Mick´l Scadden ◽  
Beatriz Carmona-Hidalgo ◽  
J. Michael McIntosh ◽  
...  
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Chromaffin Cells ◽  
Adrenal Chromaffin Cells ◽  
Nicotinic Acetylcholine ◽  
Adrenal Chromaffin

A Neurosteroid Anesthetic, Alphaxalone, Inhibits Nicotinic Acetylcholine Receptors in Cultured Bovine Adrenal Chromaffin Cells

2002 ◽  
Vol 95 (4) ◽  
pp. 900-906 ◽  
Author(s):  
Munehiro Shiraishi ◽  
Izumi Shibuya ◽  
Kouichiro Minami ◽  
Yasuhito Uezono ◽  
Takashi Okamoto ◽  
...  
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Chromaffin Cells ◽  
Adrenal Chromaffin Cells ◽  
Nicotinic Acetylcholine ◽  
Adrenal Chromaffin

scholarly journals Metabolic stability and antigenic modulation of nicotinic acetylcholine receptors on bovine adrenal chromaffin cells.

1988 ◽  
Vol 107 (3) ◽  
pp. 1147-1156 ◽  
Author(s):  
L S Higgins ◽  
D K Berg
Keyword(s):  
Plasma Membrane ◽  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Chromaffin Cells ◽  
Splanchnic Nerve ◽  
Temperature Sensitive ◽  
Adrenal Chromaffin Cells ◽  
Antigenic Modulation ◽  
Nicotinic Acetylcholine ◽  
Adrenal Chromaffin

Bovine adrenal chromaffin cells have nicotinic acetylcholine receptors (AChRs) that are activated by the splanchnic nerve, resulting in release of catecholamines from the cells. Examination of the AChRs can provide information about the regulation and turnover of synaptic components on neurons and endocrine cells. Previous studies have shown that mAb 35 recognizes the AChR on the cells. Here we show that mAb 35 can remove AChRs from the surface of the cells by antigenic modulation, and that the modulation can be used together with other methods to examine the stability and turnover of the receptors in the plasma membrane. Unexpectedly, the results indicate a disparity between the rate at which AChRs reappear on the cells and the rate at which the ACh response recovers after preexisting AChRs have been removed. Exposure of bovine adrenal chromaffin cultures to mAb 35 results in a parallel decrease in the magnitude of the nicotinic response and the number of AChRs on the cells. The decrease depends on the concentration and divalence of mAb 35, and on the time and temperature of the incubation. The antibody induces receptor aggregation in the plasma membrane under conditions where receptor loss subsequently occurs. After binding to receptor, mAb 35 appears to be internalized, degraded, and released from the cells through a temperature sensitive pathway that requires lysosomal function. These features are characteristic of antigenic modulation. Appearance of new AChRs on the cells either after antigenic modulation or after blockade of existing AChRs with monovalent antibody fragments occurs at a rate equivalent to 3% of the receptors present on control cells per hour. The rate of receptor loss from the cells was measured in the presence of either tunicamycin or puromycin to block appearance of new receptors. Both conditions indicated a receptor half-life of approximately 24 h and a rate of loss of approximately 3%/h. The finding that the rate of receptor loss equaled the rate of receptor appearance was consistent with the observation that the total number of AChRs on untreated cells did not increase with time. In the presence of tunicamycin, loss of receptor-mediated response to nicotine also occurred with a half-time of 24 h. Paradoxically, the rate of recovery of the nicotinic response, determined using two procedures, was more than twice as great as the rate at which new AChRs appeared on the cells.(ABSTRACT TRUNCATED AT 400 WORDS)

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