ADP-ribosyltransferase activity in myelin membranes isolated from human brain.
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 GTP gamma S and was specific for the beta-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.
Boulias
C
C
Division of Biochemistry Research, Hospital for Sick Children, Toronto, Ontario, Canada.
Mastronardi
F G
FG
Moscarello
M A
MA
D001921:Brain / Q000201:enzymology* / Q000648:ultrastructure; D005591:Chemical Fractionation; D016244:Guanosine 5'-O-(3-Thiotriphosphate) / Q000494:pharmacology; D006801:Humans; D004676:Myelin Basic Protein / Q000737:chemistry; D009186:Myelin Sheath / Q000201:enzymology*; D009243:NAD / Q000378:metabolism; D011065:Poly(ADP-ribose) Polymerases / Q000187:drug effects / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology; D013237:Stereoisomerism; D013379:Substrate Specificity
D004676:Myelin Basic Protein; D009243:NAD; D016244:Guanosine 5'-O-(3-Thiotriphosphate); D011065:Poly(ADP-ribose) Polymerases