Effect of reactive oxygen species on myelin membrane proteins.

Abstract:

:Fresh myelin, isolated from brainstems of adult rats, was incubated in the presence of Cu2+ and H2O2. Electrophoretic analysis of the reisolated myelin membrane revealed a gradual loss of the protein moiety from the characteristic pattern and an increase in aggregated material appearing at the origin of the gel. The aggregation of proteins was time-dependent and was concomitant with the accumulation of lipid peroxidation products reactive with thiobarbituric acid. Furthermore, during the course of incubation, there was a gradual decrease in the amount of recovered light myelin and a quantitatively similar increase in heavier myelin subfractions. The aggregation of proteins seems not to be directly related to the buoyant densities of myelin fragments. The peroxidative damage to the myelin proteins may be an important contributor to pathochemistry of myelin sheath, in particular, and in general it implies the susceptibility of the protein moiety of cell membranes to oxygen-induced deterioration.

journal_name

J Neurochem

authors

Konat GW,Wiggins RC

doi

10.1111/j.1471-4159.1985.tb05530.x

subject

Has Abstract

pub_date

1985-10-01 00:00:00

pages

1113-8

issue

4

eissn

0022-3042

issn

1471-4159

journal_volume

45

pub_type

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