Selectivity of cations and nonelectrolytes for acetylcholine-activated channels in cultured muscle cells

Li-Yen Huang, W. A. Catterall, G. Ehrenstein

Research output: Contribution to journalArticle

71 Citations (Scopus)

Abstract

The selectivity of acetylcholine (ACh)-activated channels for alkali cations, organic cations, and nonelectrolytes in cultured muscle cells of chicken embryo has been studied. To test the effect of size, charge, and hydrogen-binding capacity of permeant molecules on their permeability, we have obtained the selectivity sequences of alkali cations, compared the permeability of pairs of permanent molecules with similar size and shape but differing in charge, and studied the permeability of amines of different hydrogen bonding capacity. ACh-activated channels transport alkali cations of small hydration radii and high mobility. The molecules with positive charge and (or) a hydrogen-bond donating moiety are more permeable than the ones without. On the other hand, several nonelectrolytes, i.e., ethylene glycol, formamide, and urea, do have a small, but measurable, permeability through the channels. These results are consistent with a model that ACh-activated channel is a water-filled pore containing dipoles or hydrogen bond accepting groups and a negative charged site with a pK of 4.8.

Original languageEnglish
Pages (from-to)397-410
Number of pages14
JournalJournal of General Physiology
Volume71
Issue number4
StatePublished - 1978
Externally publishedYes

Fingerprint

Muscle Cells
Acetylcholine
Cations
Cultured Cells
Permeability
Alkalies
Hydrogen
Ethylene Glycol
Hydrogen Bonding
Amines
Urea
Chickens
Embryonic Structures
Water

ASJC Scopus subject areas

  • Physiology

Cite this

Selectivity of cations and nonelectrolytes for acetylcholine-activated channels in cultured muscle cells. / Huang, Li-Yen; Catterall, W. A.; Ehrenstein, G.

In: Journal of General Physiology, Vol. 71, No. 4, 1978, p. 397-410.

Research output: Contribution to journalArticle

@article{7e576734a73145b691598f1c2b440be0,
title = "Selectivity of cations and nonelectrolytes for acetylcholine-activated channels in cultured muscle cells",
abstract = "The selectivity of acetylcholine (ACh)-activated channels for alkali cations, organic cations, and nonelectrolytes in cultured muscle cells of chicken embryo has been studied. To test the effect of size, charge, and hydrogen-binding capacity of permeant molecules on their permeability, we have obtained the selectivity sequences of alkali cations, compared the permeability of pairs of permanent molecules with similar size and shape but differing in charge, and studied the permeability of amines of different hydrogen bonding capacity. ACh-activated channels transport alkali cations of small hydration radii and high mobility. The molecules with positive charge and (or) a hydrogen-bond donating moiety are more permeable than the ones without. On the other hand, several nonelectrolytes, i.e., ethylene glycol, formamide, and urea, do have a small, but measurable, permeability through the channels. These results are consistent with a model that ACh-activated channel is a water-filled pore containing dipoles or hydrogen bond accepting groups and a negative charged site with a pK of 4.8.",
author = "Li-Yen Huang and Catterall, {W. A.} and G. Ehrenstein",
year = "1978",
language = "English",
volume = "71",
pages = "397--410",
journal = "Journal of General Physiology",
issn = "0022-1295",
publisher = "Rockefeller University Press",
number = "4",

}

TY - JOUR

T1 - Selectivity of cations and nonelectrolytes for acetylcholine-activated channels in cultured muscle cells

AU - Huang, Li-Yen

AU - Catterall, W. A.

AU - Ehrenstein, G.

PY - 1978

Y1 - 1978

N2 - The selectivity of acetylcholine (ACh)-activated channels for alkali cations, organic cations, and nonelectrolytes in cultured muscle cells of chicken embryo has been studied. To test the effect of size, charge, and hydrogen-binding capacity of permeant molecules on their permeability, we have obtained the selectivity sequences of alkali cations, compared the permeability of pairs of permanent molecules with similar size and shape but differing in charge, and studied the permeability of amines of different hydrogen bonding capacity. ACh-activated channels transport alkali cations of small hydration radii and high mobility. The molecules with positive charge and (or) a hydrogen-bond donating moiety are more permeable than the ones without. On the other hand, several nonelectrolytes, i.e., ethylene glycol, formamide, and urea, do have a small, but measurable, permeability through the channels. These results are consistent with a model that ACh-activated channel is a water-filled pore containing dipoles or hydrogen bond accepting groups and a negative charged site with a pK of 4.8.

AB - The selectivity of acetylcholine (ACh)-activated channels for alkali cations, organic cations, and nonelectrolytes in cultured muscle cells of chicken embryo has been studied. To test the effect of size, charge, and hydrogen-binding capacity of permeant molecules on their permeability, we have obtained the selectivity sequences of alkali cations, compared the permeability of pairs of permanent molecules with similar size and shape but differing in charge, and studied the permeability of amines of different hydrogen bonding capacity. ACh-activated channels transport alkali cations of small hydration radii and high mobility. The molecules with positive charge and (or) a hydrogen-bond donating moiety are more permeable than the ones without. On the other hand, several nonelectrolytes, i.e., ethylene glycol, formamide, and urea, do have a small, but measurable, permeability through the channels. These results are consistent with a model that ACh-activated channel is a water-filled pore containing dipoles or hydrogen bond accepting groups and a negative charged site with a pK of 4.8.

UR - http://www.scopus.com/inward/record.url?scp=0017874437&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017874437&partnerID=8YFLogxK

M3 - Article

VL - 71

SP - 397

EP - 410

JO - Journal of General Physiology

JF - Journal of General Physiology

SN - 0022-1295

IS - 4

ER -