Neurochemical Research

, Volume 20, Issue 11, pp 1269–1277 | Cite as

ADP-ribosyltransferase activity in myelin membranes isolated from human brain

  • Chris Boulias
  • Fabrizio G. Mastronardi
  • Mario A. Moscarello
Original Articles
Accepted:

Abstract

An ADP-ribosyltransferase has been identified in compact myelin and in several white matter fractions which contain less compact myelin, fractionated on the basis of increasing protein/lipid ratios. One fraction the P3A contained the greatest activity although the activity in compact myelin was only slightly less. The ADP-ribosyltransferase activity of solubilized myelin was stimulated by increasing amounts of GTPγS and was specific for the β-isomer of NAD. Although ADP-ribosylation was demonstrated with the heterotrimeric G proteins in the 40–50 kDa range, the substrate for the ADP-ribosyltransferase in the 20 kDa range was identified as MBP. ADP-ribosyltransferase; myelin basic protein; signal transduction.

Keywords

Signal Transduction White Matter Human Brain Myelin Basic Protein Basic Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Abbreviations

ADP-ribose

adenosine diphosphate ribose

APAD

3-acetylpyridine adenine dinucleotide

ATP

adenosine triphosphate

C-1, 2, 3 etc

MBP components isolated by CM52 chromatography

EDTA

ethylenediaminetetraacetic acid

GTP

guanosine triphosphate

GTPγS

guanosine 5′-(3-0-thio)triphosphate

INH

isonicotinic acid hydrazide

MBP

myelin basic protein

NAD

nicotinamide adenine dinucleotide

PMSF

phenylmethylsulfonyl fluoride

PLP

proteolipid protein

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Copyright information

© Plenum Publishing Corporation 1995

Authors and Affiliations

  • Chris Boulias
    • 1
  • Fabrizio G. Mastronardi
    • 1
  • Mario A. Moscarello
    • 1
  1. 1.Division of Biochemistry ResearchThe Hospital for Sick ChildrenTorontoCanada

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