The thioredoxin system and cancer therapy: a review

被引：94

作者：

Mohammadi, Fariba ^{[1
,2
]}

Soltani, Arash ^{[1
,2
]}

Ghahremanloo, Atefeh ^{[1
]}

Javid, Hossein ^{[1
]}

Hashemy, Seyed Isaac ^{[1
,3
]}

机构：

[1] Mashhad Univ Med Sci, Dept Clin Biochem, Fac Med, Mashhad, Razavi Khorasan, Iran

[2] Mashhad Univ Med Sci, Student Res Comm, Fac Med, Mashhad, Razavi Khorasan, Iran

[3] Mashhad Univ Med Sci, Surg Oncol Res Ctr, Mashhad, Razavi Khorasan, Iran

来源：

CANCER CHEMOTHERAPY AND PHARMACOLOGY | 2019年 / 84卷 / 05期

关键词：

Thioredoxin; Thioredoxin reductase; Cancer; Cancer therapy; Oxidative stress; HISTONE DEACETYLASE INHIBITORS; 1-METHYLPROPYL 2-IMIDAZOLYL DISULFIDE; HUMAN HEPATOCELLULAR-CARCINOMA; AUTOCRINE GROWTH-FACTOR; MAMMALIAN THIOREDOXIN; REDOX REGULATION; REACTIVE OXYGEN; PERMEABILITY TRANSITION; ASK1-MEDIATED APOPTOSIS; GLUTATHIONE-REDUCTASE;

D O I：

10.1007/s00280-019-03912-4

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

Thioredoxin (Trx), thioredoxin reductase (TrxR), and NADPH are key members of the Trx system that is involved in redox regulation and antioxidant defense. In recent years, several researchers have provided information about the roles of the Trx system in cancer development and progression. These reports indicated that many tumor cells express high levels of Trx and TrxR, which can be responsible for drug resistance in tumorigenesis. Inhibition of the Trx system may thus contribute to cancer therapy and improving chemotherapeutic agents. There are now a number of effective natural and synthetic inhibitors with chemotherapy applications possessing antitumor activity ranging from oxidative stress induction to apoptosis. In this article, we first described the features and functions of the Trx system and then reviewed briefly its correlations with cancer. Finally, we summarized the present knowledge about the Trx/TrxR inhibitors as anticancer drugs.

引用

页码：925 / 935

页数：11

共 138 条

[71] Thioredoxin-1 binds to the C2 domain of PTEN inhibiting PTEN's lipid phosphatase activity and membrane binding: a mechanism for the functional loss of PTEN's tumor suppressor activity [J].