Molecular cloning of cDNA for rat ovarian 20 α-hydroxysteroid dehydrogenase (HSD1)

Miura, Ryuichi; Shiota, Kunio; Noda, Katsuji; Yagi, Shusuke; Ogawa, Tomoya; Takahashi, Michio

doi:10.1042/bj2990561

Cited by 63 publications

(44 citation statements)

References 42 publications

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“…This report describes the cloning and the characterization of a human 20 -HSD that is highly homologous to rabbit (Lacy et al 1993), rat (Mao et al 1994, Miura et al 1994, and bovine (Warren et al 1993) 20 -HSDs. The clone has been identified previously as a bile acid-binding protein (Stolz et al 1993).…”

Section: Discussionmentioning

confidence: 99%

“…In the human placenta, 20 -HSD activities have been associated with type I (Strickler et al 1981) and type II (Wu et al 1993) 17 -HSDs. Recently, cDNAs encoding rat (Mao et al 1994, Miura et al 1994, rabbit (Lacy et al 1993) and bovine (Warren et al 1993) 20 -HSD have been cloned. They are highly homologous to the 3 -hydroxysteroid dehydrogenase family, and belong to the the aldoketo reductase superfamily.…”

Section: Introductionmentioning

confidence: 99%

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Characterization of a human 20alpha-hydroxysteroid dehydrogenase

Zhang

Dufort²,

Rheault³

et al. 2000

Journal of Molecular Endocrinology

100

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It has been suggested that 20 -hydroxysteroid dehydrogenase (20 -HSD) is a T-cell differentiation marker in mice. In the human, this enzyme has generally been associated with types 1 and 2 17 -HSDs, which belong to the short-chain alcohol dehydrogenase family, whereas the rat, rabbit, pig and bovine 20 -HSDs are members of the aldoketo reductase superfamily, which also includes the 3 -HSD family. In this study, we report the cloning, from a human skin cDNA library, of a cDNA that shows, after transfection into human embryonic kidney (HEK-293) cells, high 20 -HSD activity but negligible 3 -and 17 -hydroxysteroid dehydrogenase activities. A comparison of the amino acid sequence of the human 20 -HSD with those of other related 20 -and 3 -HSDs indicates that the human 20 -HSD shares 79·9, 68·7 and 52·3% identity with rabbit, rat and bovine 20 -HSDs, whereas it shows 97, 84 and 65% identity with human type 3, type 1 and rat 3 -HSDs. In contrast, the enzyme shares only 15·2 and 15·0% identity with type 1 and type 2 human 17 -HSDs. DNA analysis predicts a protein of 323 amino acids, with a calculated molecular weight of 36 767 Da. In intact transfected cells, the human 20 -HSD preferentially catalyzes the reduction of progesterone to 20 -hydroxyprogesterone with a K m value of 0·6 µM, the reverse reaction (oxidation) being negligible. In a cell cytosolic preparation, the enzyme could use both NADPH and NADH as cofactors, but NADPH, which gave 4-fold lower K m values, was preferred. We detected the expression of 20 -HSD mRNA in liver, prostate, testis, adrenal, brain, uterus and mammary-gland tissues and in human keratinocyte (HaCaT) cells. The present study clearly indicates that the genuine human 20 -HSD belongs to the aldoketo reductase family, like the 20 -HSDs from other species.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterization of a human 20alpha-hydroxysteroid dehydrogenase

Zhang

Dufort²,

Rheault³

et al. 2000

Journal of Molecular Endocrinology

100

View full text Add to dashboard Cite

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“…Before the initiation of parturition, the progesterone level decreases markedly due to 20a-HSD induction, which is a cytosolic enzyme that converts progesterone to the inactive form 20a-hydroxyprogesterone (20a-OHP), in the corpus luteum of rodents (Wiest 1959;Batra et al 1976). Recently, cDNAs encoding rabbit [AKR 1C5] (Lacy et al 1993) and rat [AKR 1C8] (Mao et al 1994;Miura et al 1994) 20a-HSDs were isolated, and 20a-HSD is classi®ed as an aldo-keto reductase (AKR) (1997b; Jez et al 1997a). The AKR superfamily consists of monomeric NAD(P)(H)-dependent oxido-reductases with a broad speci®city of substrates: endogenous substrates, such as steroid hormones and prostaglandins (PGs); and xenobiotics, such as drugs and carcinogens.…”

Section: Introductionmentioning

confidence: 99%

Close kinship of human 20α‐hydroxysteroid dehydrogenase gene with three aldo‐keto reductase genes

Nishizawa¹,

et al. 2000

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Background: 20a-Hydroxysteroid dehydrogenase (HSD) is a member of the aldo-keto reductase (AKR) superfamily and catalyses the reaction of progesterone to the inactive form 20a-hydroxyprogesterone. Progesterone plays an important role in the maintenance of pregnancy, and, in rodents, plasma progesterone levels decrease abruptly just before parturition. The induction of 20a-HSD is thought to be responsible for the decrease in plasma progesterone at term. High homology between human 20a-HSD [AKR 1C1] cDNA with other AKRs had caused dif®culty in gene isolation and expression analysis. Thus, the metabolism of progesterone in the human reproductive system remained unclear.

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“…PRL expresses its luteotropic action by inhibiting the enzyme activity of 20α-HSD, which converts progesterone to the inactive steroid, 20α-OHP [14,15]. As a result, it has been well documented that there is a reciprocal relationship between the secretion of progesterone and 20α-dihydroprogesterone (20α-OHP).…”

mentioning

confidence: 99%

“…We previously purified 20α-hydroxysteroid dehydrogenase (20α-HSD) from rat ovary [14] and cloned its cDNA [15]. PRL expresses its luteotropic action by inhibiting the enzyme activity of 20α-HSD, which converts progesterone to the inactive steroid, 20α-OHP [14,15].…”

mentioning

confidence: 99%

Characterization of Rat Mid-Pregnancy-Specific Placental Lactogen Produced by Baculovirus / Insect Cell Expression System

Hirosawa-Takamori

Matsruura

Tanaka

et al. 1999

Journal of Reproduction and Development

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Abstract. The placenta produces prolactin (PRL)-or growth hormone-like hormones known as placental lactogens (PLs) which play roles in the maternal endocrine system and fetal growth development. We previously cloned a cDNA encoding a novel rat PL, PL-I mosaic (PL-Im), which is specifically expressed at mid-pregnancy. In this study, the biological activity of PL-Im was evaluated by producing the recombinant protein (recPL-Im) by means of a baculovirus/insect cell expression system. RecPL-Im demonstrated binding activity for PRL receptor in a radioreceptor assay (RRA) system with rat liver membrane fraction and 125 I-ovine PRL (oPRL). In addition, the activity of recPL-Im is comparable to oPRL in the Nb2 cell proliferation assay. Interestingly, recPLIm stimulated progesterone secretion in a concentration-dependent manner in a primary culture of luteal cells from pregnant rat, whereas oPRL had no effect on luteal cells. The luteotropic function of recPL-Im was accompanied by suppression of the secretion of 20α-dihydroprogesterone (20α-OHP) in the culture. PL-Im therefore has ability to bind PRL-receptor and express PRL-like activity. In addition, recPL-Im has luteotropic hormone (LTH) activity and its activity is qualitatively different from that of PRL.

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Molecular cloning of cDNA for rat ovarian 20 α-hydroxysteroid dehydrogenase (HSD1)

Cited by 63 publications

References 42 publications

Characterization of a human 20alpha-hydroxysteroid dehydrogenase

Characterization of a human 20alpha-hydroxysteroid dehydrogenase

Close kinship of human 20α‐hydroxysteroid dehydrogenase gene with three aldo‐keto reductase genes

Characterization of Rat Mid-Pregnancy-Specific Placental Lactogen Produced by Baculovirus / Insect Cell Expression System

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