Clinical relevance of the 2′-5′-oligoadenylate synthetase/RNase L system for treatment response in chronic hepatitis C

被引：7

作者：

Mihm, Ulrike ^{[1
]}

Ackermann, Oliver ^{[1
]}

Welsch, Christoph ^{[1
,2
]}

Herrmann, Eva ^{[3
]}

Hofmann, Wolf Peter ^{[1
]}

Grigorian, Natalia ^{[4
]}

Welker, Martin Walter ^{[1
]}

Lengauer, Thomas ^{[2
]}

Zeuzem, Stefan ^{[1
]}

Sarrazin, Christoph ^{[1
]}

机构：

[1] Univ Frankfurt Klinikum, Med Klin 1, D-60590 Frankfurt, Germany

[2] Max Planck Inst Informat & Angew Algorithm, D-66123 Saarbrucken, Germany

[3] Univ Frankfurt, Fachbereich Med, D-60590 Frankfurt, Germany

[4] Uniu Klinikum Saarlandes, Klin Innere Med 2, D-66421 Homburg, Germany

来源：

JOURNAL OF HEPATOLOGY | 2009年 / 50卷 / 01期

关键词：

Treatment response; Genotype; RNase L; RNA secondary structure; PROTEASE INHIBITOR TELAPREVIR; INTERFERON-TREATED CELLS; ALPHA-2B PLUS RIBAVIRIN; AMINO-ACID VARIATIONS; VIRUS TYPE 3A; RNASE-L; COMBINATION THERAPY; PEGYLATED INTERFERON-ALPHA-2B; 2-5A-DEPENDENT RNASE; HCV GENOTYPE-2;

D O I：

10.1016/j.jhep.2008.08.024

中图分类号：

R57 [消化系及腹部疾病];

学科分类号：

摘要：

Background/Aims: Interferon-a induces 2'-5'-oligoadenylate synthetase which activates RNase L. Viral RNA is cleaved by RNase L at UU/-UA dinucleotides. The clinical relevance of RNase L cleavage for response to an interferon-alpha-based therapy in chronic hepatitis C is unknown. Methods: RNase L cleavage sites within pre-treatment sequences coding for structural and non-structural hepatitis C virus proteins were compared between non-responders and responders to an interferon-alpha-based therapy. Furthermore, RNase L cleavage sites were analyzed in full length and partial genome isolates of hepatitis C virus genotype 1b infected non-responders before and during treatment and in different hepatitis C virus genotypes (1b, 2a/b, 3a/b). Results: No differences in RNase L cleavage sites were observed between non-responders and responders within a given hepatitis C genotype. Non-responders with hepatitis C virus genotype 1b infection did not eliminate UA/UU dinucleotides during therapy. Hepatitis C virus genotype 1b isolates showed a lower number of UA/UU dinucleotides than hepatitis C virus genotypes 2/3 (p < 0.001). Conclusions: Response or non-response to an interferon-a-based therapy within a given hepatitis C virus genotype is not explained by differences for RNase L cleavage sites. General differences of interferon sensitivity between hepatitis C virus genotypes correlate significantly with frequencies of RNase L cleavage sites. (C) 2008 European Association for the Study of the Liver. Published by Elsevier B.V. All rights reserved.

引用

页码：49 / 58

页数：10

共 50 条

[41] 2′,5′-oligoadenylate-peptide nucleic acids (2-5A-PNAs) activate RNase L
Verheijen, JC
van der Marel, GA
van Boom, JH
Bayly, SF
Player, MR
Torrence, PF
BIOORGANIC & MEDICINAL CHEMISTRY, 1999, 7 (03) : 449 - 455
[42] RNASE-L, A (2'-5')-OLIGOADENYLATE-DEPENDENT ENDORIBONUCLEASE - ASSAYS AND PURIFICATION OF THE ENZYME - CROSS-LINKING TO A (2'-5')-OLIGOADENYLATE DERIVATIVE
FLOYDSMITH, G
LENGYEL, P
METHODS IN ENZYMOLOGY, 1986, 119 : 489 - 499
[43] The 2′-5′ oligoadenylate/RNase L/RNase L inhibitor pathway regulates both MyoD mRNA stability and muscle cell differentiation
Bisbal, C
Silhol, M
Laubenthal, K
Kaluza, T
Carnac, G
Milligan, L
Le Roy, F
Salehzada, T
MOLECULAR AND CELLULAR BIOLOGY, 2000, 20 (14) : 4959 - 4969
[44] STUDY OF THE ACTIVITY OF AN INTERFERON-DEPENDENT LYMPHOCYTIC ENZYME, 2'5'-OLIGOADENYLATE-SYNTHETASE IN CHRONIC HBSAG+ HEPATITIS
POITRINE, A
CHOUSTERMAN, S
THANG, MT
CHOUSTERMAN, M
CHAPUT, JC
GASTROENTEROLOGIE CLINIQUE ET BIOLOGIQUE, 1983, 7 : A94 - A94
[45] INTERFERON THERAPY OF HBEAG POSITIVE CHRONIC HEPATITIS - ITS EFFICACY EVALUATED BY LYMPHOCYTIC 2',5'-OLIGOADENYLATE SYNTHETASE-ACTIVITY
FUJISAWA, K
YAMAZAKI, K
KAWASE, H
KAMEDA, H
HEPATOLOGY, 1986, 6 (04) : 795 - 795
[46] INDOMETHACIN INCREASES 2',5'-OLIGOADENYLATE SYNTHETASE RELEASE BY CULTURED LIVER-TISSUE OF PATIENTS WITH HCV CHRONIC ACTIVE HEPATITIS
ANDREONE, P
CURSARO, C
GRAMENZI, A
BUZZI, A
MINIERO, R
BERNARDI, M
GASBARRINI, G
INTERNATIONAL HEPATOLOGY COMMUNICATIONS, 1994, 2 (05): : 289 - 294
[47] Alternative function of a protein kinase homology domain in 2′,5′-oligoadenylate dependent RNase L
Dong, BH
Silverman, RH
NUCLEIC ACIDS RESEARCH, 1999, 27 (02) : 439 - 445
[48] 2',5'-OLIGOADENYLATE-DEPENDENT RNASE-L IS A DIMER OF REGULATORY AND CATALYTIC SUBUNITS
SALEHZADA, T
SILHOL, M
STEFF, AM
LEBLEU, B
BISBAL, C
JOURNAL OF BIOLOGICAL CHEMISTRY, 1993, 268 (11) : 7733 - 7740
[49] Regulation of human immunodeficiency virus replication by 2′,5′-oligoadenylate-dependent RNase L
Maitra, RK
Silverman, RH
JOURNAL OF VIROLOGY, 1998, 72 (02) : 1146 - 1152
[50] Structural Basis for 2′-5′-Oligoadenylate Binding and Enzyme Activity of a Viral RNase L Antagonist
Ogden, Kristen M.
Hu, Liya
Jha, Babal K.
Sankaran, Banumathi
Weiss, Susan R.
Silverman, Robert H.
Patton, John T.
Prasad, B. V. Venkataram
JOURNAL OF VIROLOGY, 2015, 89 (13) : 6633 - 6645

← 1 2 3 4 5 →