Secretion of acetylcholinesterase: Relation to acetylcholine receptor metabolism

Richard L Rotundo, D. M. Fambrough

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Acetylcholinesterase (AChE) and acetylcholine receptors (AChR) are muscle-specific glycoproteins present in cultured chick embryo muscle cells. The first is found as both a secreted and a membrane-bound enzyme whereas the ACh receptor is strictly an integral membrane protein. We have studied the transport and externalization of these two proteins in the same cells using several compounds known to affect secretory processes: colchicine, tunicamycin and the ionophores X-537A, Nigericin and Monensin. Under all experimental conditions, any change in the rate of AChE secretion was accompanied by an identical change in the rate of ACh receptor incorporation into the plasma membrane. These studies were designed to test directly the hypothesis that secreted and integral membrane proteins are transported together to the plasma membrane. Our results are consistent with a single transport pathway in muscle cells for the externalization of membrane and secreted proteins.

Original languageEnglish
Title of host publicationCell
Pages594-602
Number of pages9
Volume22
Edition2 II
StatePublished - Dec 1 1980
Externally publishedYes

Fingerprint

Cholinergic Receptors
Acetylcholinesterase
Membrane Proteins
Cell Membrane
Muscle Cells
Lasalocid
Nigericin
Tunicamycin
Monensin
Secretory Pathway
Ionophores
Colchicine
Chick Embryo
Glycoproteins
Muscles
Membranes
Enzymes
Proteins

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Rotundo, R. L., & Fambrough, D. M. (1980). Secretion of acetylcholinesterase: Relation to acetylcholine receptor metabolism. In Cell (2 II ed., Vol. 22, pp. 594-602)

Secretion of acetylcholinesterase : Relation to acetylcholine receptor metabolism. / Rotundo, Richard L; Fambrough, D. M.

Cell. Vol. 22 2 II. ed. 1980. p. 594-602.

Research output: Chapter in Book/Report/Conference proceedingChapter

Rotundo, RL & Fambrough, DM 1980, Secretion of acetylcholinesterase: Relation to acetylcholine receptor metabolism. in Cell. 2 II edn, vol. 22, pp. 594-602.
Rotundo RL, Fambrough DM. Secretion of acetylcholinesterase: Relation to acetylcholine receptor metabolism. In Cell. 2 II ed. Vol. 22. 1980. p. 594-602
@inbook{35127f6a77f94d0099bcc5a62059ec78,
title = "Secretion of acetylcholinesterase: Relation to acetylcholine receptor metabolism",
abstract = "Acetylcholinesterase (AChE) and acetylcholine receptors (AChR) are muscle-specific glycoproteins present in cultured chick embryo muscle cells. The first is found as both a secreted and a membrane-bound enzyme whereas the ACh receptor is strictly an integral membrane protein. We have studied the transport and externalization of these two proteins in the same cells using several compounds known to affect secretory processes: colchicine, tunicamycin and the ionophores X-537A, Nigericin and Monensin. Under all experimental conditions, any change in the rate of AChE secretion was accompanied by an identical change in the rate of ACh receptor incorporation into the plasma membrane. These studies were designed to test directly the hypothesis that secreted and integral membrane proteins are transported together to the plasma membrane. Our results are consistent with a single transport pathway in muscle cells for the externalization of membrane and secreted proteins.",
author = "Rotundo, {Richard L} and Fambrough, {D. M.}",
year = "1980",
month = "12",
day = "1",
language = "English",
volume = "22",
pages = "594--602",
booktitle = "Cell",
edition = "2 II",

}

TY - CHAP

T1 - Secretion of acetylcholinesterase

T2 - Relation to acetylcholine receptor metabolism

AU - Rotundo, Richard L

AU - Fambrough, D. M.

PY - 1980/12/1

Y1 - 1980/12/1

N2 - Acetylcholinesterase (AChE) and acetylcholine receptors (AChR) are muscle-specific glycoproteins present in cultured chick embryo muscle cells. The first is found as both a secreted and a membrane-bound enzyme whereas the ACh receptor is strictly an integral membrane protein. We have studied the transport and externalization of these two proteins in the same cells using several compounds known to affect secretory processes: colchicine, tunicamycin and the ionophores X-537A, Nigericin and Monensin. Under all experimental conditions, any change in the rate of AChE secretion was accompanied by an identical change in the rate of ACh receptor incorporation into the plasma membrane. These studies were designed to test directly the hypothesis that secreted and integral membrane proteins are transported together to the plasma membrane. Our results are consistent with a single transport pathway in muscle cells for the externalization of membrane and secreted proteins.

AB - Acetylcholinesterase (AChE) and acetylcholine receptors (AChR) are muscle-specific glycoproteins present in cultured chick embryo muscle cells. The first is found as both a secreted and a membrane-bound enzyme whereas the ACh receptor is strictly an integral membrane protein. We have studied the transport and externalization of these two proteins in the same cells using several compounds known to affect secretory processes: colchicine, tunicamycin and the ionophores X-537A, Nigericin and Monensin. Under all experimental conditions, any change in the rate of AChE secretion was accompanied by an identical change in the rate of ACh receptor incorporation into the plasma membrane. These studies were designed to test directly the hypothesis that secreted and integral membrane proteins are transported together to the plasma membrane. Our results are consistent with a single transport pathway in muscle cells for the externalization of membrane and secreted proteins.

UR - http://www.scopus.com/inward/record.url?scp=0019132559&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0019132559&partnerID=8YFLogxK

M3 - Chapter

C2 - 7448874

VL - 22

SP - 594

EP - 602

BT - Cell

ER -