Alterations in the activity of phospholipases A2 in postmortem white matter from patients with multiple sclerosis.

Abstract:

:Activities toward arachidonyl-labelled phospholipase A2 substrates were assayed in fractions of white matter and cerebral cortex from control subjects and in fractions of demyelinated plaque, normal-appearing white matter and cerebral cortex from subjects who died with multiple sclerosis. Membranous activity at pH 8.6 in the presence of Ca2+, characteristic of 14 kDa "secretory" phospholipase A2, in either multiple sclerosis white matter or cortex did not differ from controls, whereas membranous activity at pH 4.5 in the absence of added Ca2+, characteristic of lysosomal enzymes was increased over controls in both plaque and normal-appearing white matter but not cerebral cortex. Activity in the cytosol fraction, at pH 8.6 in the presence of Ca2+ and glycerol characteristic of the "cytosolic" 85 kDa enzyme was decreased by greater than 50% in both white matter and cortex samples from multiple sclerosis subjects. Immuno-precipitation and -blotting confirmed that the deficient activity was largely attributable to the 85 kDa enzyme although the enzyme protein was not similarly reduced.

journal_name

Neurochem Res

journal_title

Neurochemical research

authors

Huterer SJ,Tourtellotte WW,Wherrett JR

doi

10.1007/BF00992509

subject

Has Abstract

pub_date

1995-11-01 00:00:00

pages

1335-43

issue

11

eissn

0364-3190

issn

1573-6903

journal_volume

20

pub_type

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