Biochemical properties and subcellular distribution of the neuronal class E calcium channel α1 subunit

Charles T. Yokoyama, Ruth E. Westenbroek, Johannes W Hell, Tuck Wah Soong, Terry P. Snutch, William A. Catterall

Research output: Contribution to journalArticle

143 Citations (Scopus)

Abstract

Anti-peptide antibodies specific for the neuronal calcium channel α(1E) subunit (anti-CNE1 and anti-CNE2) were produced to study the biochemical properties and subcellular distribution of the α(1E) polypeptide from rat brain. Immunoblotting identified a single size form of 245-255 kDa which was a substrate for phosphorylation by cAMP-dependent protein kinase, protein kinase C, cGMP-dependent protein kinase, and calcium/calmodulin-dependent protein kinase II. Ligand-binding studies of α(1E) indicate that it is not a high affinity receptor for the dihydropyridine isradipine or the peptide toxins ω-conotoxin GVIA or ω-conotoxin MVIIC at concentrations which elicit high affinity binding to other channel types in the same membrane preparation. The α(1E) subunit is widely distributed in the brain with the most prominent immunocytochemical staining in deep midline structures such as caudate-putamen, thalamus, hypothalamus, amygdala, cerebellum, and a variety of nuclei in the ventral midbrain and brainstem. Staining is primarily in the cell soma but is also prominent in the dendritic field of a discrete subset of neurons including the mitral cells of the olfactory bulb and the distal dendritic branches of the cerebellar Purkinje cells. Our observations indicate that the 245-255 kDa α(1E) subunit is localized in cell bodies, and in some cases in dendrites, of a broad range of central neurons and is potentially modulated by multiple second messenger-activated protein kinases.

Original languageEnglish (US)
Pages (from-to)6419-6432
Number of pages14
JournalJournal of Neuroscience
Volume15
Issue number10
StatePublished - Oct 1995
Externally publishedYes

Fingerprint

Calcium Channels
Conotoxins
Calcium-Calmodulin-Dependent Protein Kinase Type 2
Peptides
Calcium-Calmodulin-Dependent Protein Kinase Kinase
Isradipine
Staining and Labeling
Neurons
Cyclic GMP-Dependent Protein Kinases
L-Type Calcium Channels
Olfactory Bulb
Purkinje Cells
Putamen
Brain
Carisoprodol
Second Messenger Systems
Dendrites
Mesencephalon
Cyclic AMP-Dependent Protein Kinases
Amygdala

Keywords

  • calcium channel
  • immunocytochemistry
  • ion channel
  • peptide toxin
  • phosphorylation
  • Purkinje cell

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Yokoyama, C. T., Westenbroek, R. E., Hell, J. W., Soong, T. W., Snutch, T. P., & Catterall, W. A. (1995). Biochemical properties and subcellular distribution of the neuronal class E calcium channel α1 subunit. Journal of Neuroscience, 15(10), 6419-6432.

Biochemical properties and subcellular distribution of the neuronal class E calcium channel α1 subunit. / Yokoyama, Charles T.; Westenbroek, Ruth E.; Hell, Johannes W; Soong, Tuck Wah; Snutch, Terry P.; Catterall, William A.

In: Journal of Neuroscience, Vol. 15, No. 10, 10.1995, p. 6419-6432.

Research output: Contribution to journalArticle

Yokoyama, CT, Westenbroek, RE, Hell, JW, Soong, TW, Snutch, TP & Catterall, WA 1995, 'Biochemical properties and subcellular distribution of the neuronal class E calcium channel α1 subunit', Journal of Neuroscience, vol. 15, no. 10, pp. 6419-6432.
Yokoyama CT, Westenbroek RE, Hell JW, Soong TW, Snutch TP, Catterall WA. Biochemical properties and subcellular distribution of the neuronal class E calcium channel α1 subunit. Journal of Neuroscience. 1995 Oct;15(10):6419-6432.
Yokoyama, Charles T. ; Westenbroek, Ruth E. ; Hell, Johannes W ; Soong, Tuck Wah ; Snutch, Terry P. ; Catterall, William A. / Biochemical properties and subcellular distribution of the neuronal class E calcium channel α1 subunit. In: Journal of Neuroscience. 1995 ; Vol. 15, No. 10. pp. 6419-6432.
@article{36acda2b530a482b9b9f06bb3e8c9b9b,
title = "Biochemical properties and subcellular distribution of the neuronal class E calcium channel α1 subunit",
abstract = "Anti-peptide antibodies specific for the neuronal calcium channel α(1E) subunit (anti-CNE1 and anti-CNE2) were produced to study the biochemical properties and subcellular distribution of the α(1E) polypeptide from rat brain. Immunoblotting identified a single size form of 245-255 kDa which was a substrate for phosphorylation by cAMP-dependent protein kinase, protein kinase C, cGMP-dependent protein kinase, and calcium/calmodulin-dependent protein kinase II. Ligand-binding studies of α(1E) indicate that it is not a high affinity receptor for the dihydropyridine isradipine or the peptide toxins ω-conotoxin GVIA or ω-conotoxin MVIIC at concentrations which elicit high affinity binding to other channel types in the same membrane preparation. The α(1E) subunit is widely distributed in the brain with the most prominent immunocytochemical staining in deep midline structures such as caudate-putamen, thalamus, hypothalamus, amygdala, cerebellum, and a variety of nuclei in the ventral midbrain and brainstem. Staining is primarily in the cell soma but is also prominent in the dendritic field of a discrete subset of neurons including the mitral cells of the olfactory bulb and the distal dendritic branches of the cerebellar Purkinje cells. Our observations indicate that the 245-255 kDa α(1E) subunit is localized in cell bodies, and in some cases in dendrites, of a broad range of central neurons and is potentially modulated by multiple second messenger-activated protein kinases.",
keywords = "calcium channel, immunocytochemistry, ion channel, peptide toxin, phosphorylation, Purkinje cell",
author = "Yokoyama, {Charles T.} and Westenbroek, {Ruth E.} and Hell, {Johannes W} and Soong, {Tuck Wah} and Snutch, {Terry P.} and Catterall, {William A.}",
year = "1995",
month = "10",
language = "English (US)",
volume = "15",
pages = "6419--6432",
journal = "Journal of Neuroscience",
issn = "0270-6474",
publisher = "Society for Neuroscience",
number = "10",

}

TY - JOUR

T1 - Biochemical properties and subcellular distribution of the neuronal class E calcium channel α1 subunit

AU - Yokoyama, Charles T.

AU - Westenbroek, Ruth E.

AU - Hell, Johannes W

AU - Soong, Tuck Wah

AU - Snutch, Terry P.

AU - Catterall, William A.

PY - 1995/10

Y1 - 1995/10

N2 - Anti-peptide antibodies specific for the neuronal calcium channel α(1E) subunit (anti-CNE1 and anti-CNE2) were produced to study the biochemical properties and subcellular distribution of the α(1E) polypeptide from rat brain. Immunoblotting identified a single size form of 245-255 kDa which was a substrate for phosphorylation by cAMP-dependent protein kinase, protein kinase C, cGMP-dependent protein kinase, and calcium/calmodulin-dependent protein kinase II. Ligand-binding studies of α(1E) indicate that it is not a high affinity receptor for the dihydropyridine isradipine or the peptide toxins ω-conotoxin GVIA or ω-conotoxin MVIIC at concentrations which elicit high affinity binding to other channel types in the same membrane preparation. The α(1E) subunit is widely distributed in the brain with the most prominent immunocytochemical staining in deep midline structures such as caudate-putamen, thalamus, hypothalamus, amygdala, cerebellum, and a variety of nuclei in the ventral midbrain and brainstem. Staining is primarily in the cell soma but is also prominent in the dendritic field of a discrete subset of neurons including the mitral cells of the olfactory bulb and the distal dendritic branches of the cerebellar Purkinje cells. Our observations indicate that the 245-255 kDa α(1E) subunit is localized in cell bodies, and in some cases in dendrites, of a broad range of central neurons and is potentially modulated by multiple second messenger-activated protein kinases.

AB - Anti-peptide antibodies specific for the neuronal calcium channel α(1E) subunit (anti-CNE1 and anti-CNE2) were produced to study the biochemical properties and subcellular distribution of the α(1E) polypeptide from rat brain. Immunoblotting identified a single size form of 245-255 kDa which was a substrate for phosphorylation by cAMP-dependent protein kinase, protein kinase C, cGMP-dependent protein kinase, and calcium/calmodulin-dependent protein kinase II. Ligand-binding studies of α(1E) indicate that it is not a high affinity receptor for the dihydropyridine isradipine or the peptide toxins ω-conotoxin GVIA or ω-conotoxin MVIIC at concentrations which elicit high affinity binding to other channel types in the same membrane preparation. The α(1E) subunit is widely distributed in the brain with the most prominent immunocytochemical staining in deep midline structures such as caudate-putamen, thalamus, hypothalamus, amygdala, cerebellum, and a variety of nuclei in the ventral midbrain and brainstem. Staining is primarily in the cell soma but is also prominent in the dendritic field of a discrete subset of neurons including the mitral cells of the olfactory bulb and the distal dendritic branches of the cerebellar Purkinje cells. Our observations indicate that the 245-255 kDa α(1E) subunit is localized in cell bodies, and in some cases in dendrites, of a broad range of central neurons and is potentially modulated by multiple second messenger-activated protein kinases.

KW - calcium channel

KW - immunocytochemistry

KW - ion channel

KW - peptide toxin

KW - phosphorylation

KW - Purkinje cell

UR - http://www.scopus.com/inward/record.url?scp=0028829634&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028829634&partnerID=8YFLogxK

M3 - Article

C2 - 7472405

AN - SCOPUS:0028829634

VL - 15

SP - 6419

EP - 6432

JO - Journal of Neuroscience

JF - Journal of Neuroscience

SN - 0270-6474

IS - 10

ER -