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Biochemical evidence for a novel low molecular weight 2-5A-dependent RNase L in Chronic Fatigue Syndrome (CFS)

  [ 32 votes ]   [ Discuss This Article ]
By Suhadolnik RJ, Peterson DL, O'Brien K, Cheney PR, Herst CV, Reichenbach NL, KonN, Horvath SE, Iacono KT, Adelson ME, De Meirleir K, De Becker P, Charubala R, Pfleiderer W • www.ProHealth.com • July 10, 1997


Previous studies from this laboratory have demonstrated a
statistically significant dysregulation in several key
components of the 2',5'-oligoadenylate (2-5A) synthetase/RNase
L and PKR antiviral pathways in chronic fatigue syndrome (CFS)
(Suhadolnik et al. Clin Infect Dis 18, S96-104, 1994;
Suhadolnik et al. In Vivo 8, 599-604, 1994). Two methodologies
have been developed to further examine the upregulated RNase L
activity in CFS. First, photoaffinity labeling of extracts of
peripheral blood mononuclear cells (PBMC) with the azido 2-5A
photoaffinity probe, [32P]pApAp(8-azidoA), followed by
immunoprecipitation with a polyclonal antibody against
recombinant, human 80-kDa RNase L and analysis under
denaturing conditions. A subset of individuals with CFS was
identified with only one 2-5A binding protein at 37 kDa,
whereas in extracts of PBMC from a second subset of CFS PBMC
and from healthy controls, photolabeled/immunoreactive 2-5A
binding proteins were detected at 80, 42, and 37 kDa. Second,
analytic gel permeation HPLC was completed under native
conditions. Extracts of healthy control PBMC revealed 2-5A
binding and 2-5A-dependent RNase L enzyme activity at 80 and
42 kDa as determined by hydrolysis of poly(U)-3'-[32P]pCp. A
subset of CFS PBMC contained 2-5A binding proteins with
2-5A-dependent RNase L enzyme activity at 80, 42, and 30 kDa.
However, a second subset of CFS PBMC contained 2-5A binding
and 2-5A-dependent RNase L enzyme activity only at 30 kDa.
Evidence is provided indicating that the RNase L enzyme
dysfunction in CFS is more complex than previously reported.




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