Subcellular targeting analysis of SDR-type hydroxysteroid dehydrogenases

被引:9
作者
Filling, C [1 ]
Wu, XQ [1 ]
Shafqat, N [1 ]
Hult, M [1 ]
Mårtensson, E [1 ]
Shafqat, J [1 ]
Oppermann, UCT [1 ]
机构
[1] Karolinska Inst, Dept Med Biochem & Biophys, S-17177 Stockholm, Sweden
关键词
short-chain dehydrogenases/reductases; aldo-keto reductases; hydroxysteroid dehydrogenase; subcellular localization; ERAB;
D O I
10.1016/S0303-7207(00)00419-6
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Most mammalian hydroxysteroid dehydrogenases known thus far belong to the protein superfamilies of short-chain dehydrogenases/reductases (SDR) and aldo-keto reductases (AKR). Whereas members of the AKR family are soluble, cytoplasmic enzymes, SDR-type hydroxysteroid dehydrogenases are also located to other subcellular compartments, i.e. endoplasmic reticulum, mitochondria or peroxisomes. Differential localization might play an important role in influencing the reaction direction of hydroxy dehydrogenase/oxo reductase pathways by determining the available nucleotide cofactor pool. Targeting signals for different subcellular organelles in human hydroxysteroid dehydrogenases have been identified, however, in several enzymes localization signals remain to be determined. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.
引用
收藏
页码:99 / 101
页数:3
相关论文
共 12 条
[1]   Steroid dehydrogenase structures, mechanism of action, and disease [J].
Duax, WL ;
Ghosh, D ;
Pletnev, V .
VITAMINS AND HORMONES - ADVANCES IN RESEARCH AND APPLICATIONS, VOL 58, 2000, 58 :121-+
[2]   Cloning and expression of cDNA for a newly identified isozyme of bovine liver 3-hydroxyacyl-CoA dehydrogenase and its import into mitochondria [J].
Furuta, S ;
Kobayashi, A ;
Miyazawa, S ;
Hashimoto, T .
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION, 1997, 1350 (03) :317-324
[3]  
GABRIELLI F, 1995, EUR J BIOCHEM, V232, P473, DOI 10.1111/j.1432-1033.1995.473zz.x
[4]   Function of human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase in androgen metabolism [J].
He, XY ;
Merz, G ;
Yang, YZ ;
Pullakart, R ;
Mehta, P ;
Schulz, H ;
Yang, SY .
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS, 2000, 1484 (2-3) :267-277
[5]   A new nomenclature for the aldo-keto reductase superfamily [J].
Jez, JM ;
Flynn, TG ;
Penning, TM .
BIOCHEMICAL PHARMACOLOGY, 1997, 54 (06) :639-647
[6]   SHORT-CHAIN DEHYDROGENASES REDUCTASES (SDR) [J].
JORNVALL, H ;
PERSSON, B ;
KROOK, M ;
ATRIAN, S ;
GONZALEZDUARTE, R ;
JEFFERY, J ;
GHOSH, D .
BIOCHEMISTRY, 1995, 34 (18) :6003-6013
[7]   The subcellular localization of 17 beta-hydroxysteroid dehydrogenase type 4 and its interaction with actin [J].
Markus, M ;
Husen, B ;
Adamski, J .
JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY, 1995, 55 (5-6) :617-621
[8]   Truncation of the N- and C-terminal regions of the human 11 beta-hydroxysteroid dehydrogenase type 2 enzyme and effects on solubility and bidirectional enzyme activity [J].
Obeyesekere, VR ;
Li, KXZ ;
Ferrari, P ;
Krozowski, Z .
MOLECULAR AND CELLULAR ENDOCRINOLOGY, 1997, 131 (02) :173-182
[9]   The 11 beta-hydroxysteroid dehydrogenase system, a determinant of glucocorticoid and mineralocorticoid action - Function, gene organization and protein structures of 11 beta-hydroxysteroid dehydrogenase isoforms [J].
Oppermann, UCT ;
Persson, B ;
Jornvall, H .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1997, 249 (02) :355-360
[10]   17β-Hydroxysteroid dehydrogenase (HSD)/17-ketosteroid reductase (KSR) family;: nomenclature and main characteristics of the 17HSD/KSR enzymes [J].
Peltoketo, H ;
Luu-The, V ;
Simard, J ;
Adamski, J .
JOURNAL OF MOLECULAR ENDOCRINOLOGY, 1999, 23 (01) :1-11