ISOLATION AND RECONSTITUTION OF NEURONAL ION TRANSPORT PROTEINS

Autor: S M Goldin, D M Papazian, E G Moczydlowski
Rok vydání: 1983
Předmět:
Zdroj: Annual Review of Neuroscience. 6:419-446
ISSN: 1545-4126
0147-006X
DOI: 10.1146/annurev.ne.06.030183.002223
Popis: Introduction The electrical activity of nerve cells is produced by the coordinated gating and pumping of ions across the neuronal membrane. It is axiomatic that regulation of neuronal electrical activity is due to regulation of these ion transport proteins. Examples of primary regulatory mechanisms are (0) the depolarization of the nerve cell membrane that induces the opening of the voltage-sensitive action potential Na+ channel and (b) the conductance change directly induced by the binding of neurotransmitters to postsynaptic receptor sites. More indirect and in some cases simultaneous secondary mechanisms of regulation are postulated to occur, e.g. via phosphorylation of ion transport proteins resulting from a cyclic nucleotide-mediated series of events (reviewed by Kennedy 1983). Identifying these neuronal ion transport proteins and reconstituting them in a purified, biologically active form can help answer a variety of questions. The mechanisms of gene replication (DePampbilis & Wassarman 1980) and muscle contraction (Adelstein & Eisenberg 1980) are studied by isolating the enzymes and other components involved and determining how they function and interact with each other in vitro. Studying the mechanism and regulation of purified, reconstituted ion transport proteins could provide similar information about the molecular basis of neuronal electrical activity. If one can then proceed immunocytochemically to localize specific classes of these transport proteins in the eNS (together with using information provided by neuroanatomical techniques), one could in principle obtain a functional map of their distribution in neuronal pathways that might help
Databáze: OpenAIRE