The roles of aldo-keto reductases in steroid hormone action

被引：65

作者：

Bauman, DR ^{[1
]}

Steckelbroeck, S ^{[1
]}

Penning, TM ^{[1
]}

机构：

[1] Univ Penn, Sch Med, Dept Pharmacol, Philadelphia, PA 19104 USA

来源：

DRUG NEWS & PERSPECTIVES | 2004年 / 17卷 / 09期

关键词：

D O I：

10.1358/dnp.2004.17.9.872570

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

dThe human aldo-keto reductase 1 C (AKR1C) isozymes are implicated in the pre-receptor regulation of steroid receptors, nuclear orphan receptors and membrane-bound ligand-gated ion channels. Human AKR members that may regulate the local concentration of steroid hormones include: AKR1C1, AKR1C2, AKR1C3, AKR1C4 and AKR1D1. Since, these enzymes are pluripotent, the physiological role for the human AKR1C isozymes is determined by their tissue-specific expression patterns and their substrate availability in target tissues. AKRs work in concert with short-chain dehydrogenases/reductases as switches to control ligand access to nuclear receptors. Consequently, they are potential targets in treating prostate cancer, breast cancer, endometriosis and endometrial cancer. (C) 2004 Prous Science. All rights reserved.

引用

页码：563 / 578

页数：16

共 170 条

[81]

MACDONALD PC, 1974, OBSTET GYNECOL, V44, P629

[82] Modulation of GABAA receptor function by neuroactive steroids:: evidence for heterogeneity of steroid sensitivity of recombinant GABAA receptor isoforms [J].

Maitra, R ;

Reynolds, JN .

CANADIAN JOURNAL OF PHYSIOLOGY AND PHARMACOLOGY, 1998, 76 (09) :909-920

[83] NEUROSTEROIDS - ENDOGENOUS BIMODAL MODULATORS OF THE GABA-A RECEPTOR - MECHANISM OF ACTION AND PHYSIOLOGICAL SIGNIFICANCE [J].

MAJEWSKA, MD .

PROGRESS IN NEUROBIOLOGY, 1992, 38 (04) :379-395

[84] Testosterone and progesterone metabolism in the central nervous system: Cellular localization and mechanism of control of the enzymes involved [J].

Martini, L ;

Celotti, F ;

Melcangi, RC .

CELLULAR AND MOLECULAR NEUROBIOLOGY, 1996, 16 (03) :271-282

[85] Identification of a principal mRNA species for human 3α-hydroxysteroid dehydrogenase isoform (AKR1C3) that exhibits high prostaglandin D2 11-ketoreductase activity [J].

Matsuura, K ;

Shiraishi, H ;

Hara, A ;

Sato, K ;

Deyashiki, Y ;

Ninomiya, M ;

Sakai, S .

JOURNAL OF BIOCHEMISTRY, 1998, 124 (05) :940-946

[86] Identification of amino acid residues responsible for differences in substrate specificity and inhibitor sensitivity between two human liver dihydrodiol dehydrogenase isoenzymes by site-directed mutagenesis [J].

Matsuura, K ;

Deyashiki, Y ;

Sato, K ;

Ishida, N ;

Miwa, G ;

Hara, A .

BIOCHEMICAL JOURNAL, 1997, 323 :61-64

[87] Combinatorial control of gene expression by nuclear receptors and coregulators [J].

McKenna, NJ ;

O'Malley, BW .

CELL, 2002, 108 (04) :465-474

[88] Neurosteroids: biochemistry and clinical significance [J].

Mellon, SH ;

Griffin, LD .

TRENDS IN ENDOCRINOLOGY AND METABOLISM, 2002, 13 (01) :35-43

[89] METABOLISM OF 4-C-14-PROGESTERONE AND 4-C-14-TESTOSTERONE IN BRAIN OF PREVIABLE HUMAN FETUS [J].

MICKAN, H .

STEROIDS, 1972, 19 (05) :659-&

[90] INITIATION OF HUMAN PARTURITION .9. PROGESTERONE METABOLISM BY PLACENTAS OF EARLY AND LATE HUMAN GESTATION [J].

MILEWICH, L ;

GANT, NF ;

SCHWARZ, BE ;

CHEN, GT ;

MACDONALD, PC .

OBSTETRICS AND GYNECOLOGY, 1978, 51 (03) :278-280

← 4 5 6 7 8 9 10 11 12 13 →