Human adrenodoxin: Cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells

J. Picado-Leonard, R. Voutilainen, L. Kao, B. Chung, J. F. Strauss, W. L. Miller

研究成果: ジャーナルへの寄稿記事

121 引用 (Scopus)

抄録

Adrenodoxin is an iron-sulfur protein serving as an electron transport intermediate for two mitochondrial steroidogenic cytochromes P450. We have cloned and sequenced three human adrenal adrenodoxin cDNAs. The longest 5'-untranslated region was 131 bases long, and the coding sequences, identical in all three clones, predict a preprotein of 180 amino acids. The 3'-untranslated regions were 235, 596, and 776 bases long due to the presence of alternate polyadenylation sites. RNA transfer blots showed multiple size species of adrenodoxin mRNA consistent with finding multiple polyadenylation sites. Similar sized cross-hybridizing RNA species are found abundantly in the adrenal and testis and to a lesser degree in RNA from human fetal brain, spleen, placenta, kidney, liver, and intestine, as well as in cultured fibroblasts, suggesting the same or a very similar iron-sulfur protein is found in mitochondria of nonsteroidogenic tissues. JEG-3 cells, a transformed progesterone-producing line of trophoblastic origin, accumulate mRNAs for cytochrome P450scc (the mitochondrial cholesterol side-chain cleavage enzyme), adrenodoxin, and the fos oncogene when stimulated with 8-bromo-cyclic AMP. Addition of actinomycin D to such cultures blocked cAMP-induced accumulation of mRNAs for cytochrome P450scc and adrenodoxin. Addition of cycloheximide or puromycin to such cultures substantially reduced basal levels and markedly attenuated the cAMP-induced accumulation of cytochrome P450scc mRNA, but augmented the accumulation of adrenodoxin and fos mRNAs in additive and multiplicative fashions, respectively. These data indicate that the cAMP-induced synthesis of the steroidogenic machinery is not wholly dependent on cycloheximide-sensitive protein mediators.

元の言語英語
ページ(範囲)3240-3244
ページ数5
ジャーナルJournal of Biological Chemistry
263
発行部数7
出版物ステータス出版済み - 1 1 1988

Fingerprint

Adrenodoxin
Cloning
Cycloheximide
Cholesterol Side-Chain Cleavage Enzyme
Organism Cloning
Complementary DNA
Messenger RNA
Iron-Sulfur Proteins
Polyadenylation
RNA
8-Bromo Cyclic Adenosine Monophosphate
Puromycin
Mitochondria
5' Untranslated Regions
3' Untranslated Regions
Dactinomycin
Fibroblasts
Electron Transport
Transfer RNA
Oncogenes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Picado-Leonard, J., Voutilainen, R., Kao, L., Chung, B., Strauss, J. F., & Miller, W. L. (1988). Human adrenodoxin: Cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells. Journal of Biological Chemistry, 263(7), 3240-3244.

Human adrenodoxin : Cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells. / Picado-Leonard, J.; Voutilainen, R.; Kao, L.; Chung, B.; Strauss, J. F.; Miller, W. L.

:: Journal of Biological Chemistry, 巻 263, 番号 7, 01.01.1988, p. 3240-3244.

研究成果: ジャーナルへの寄稿記事

Picado-Leonard, J, Voutilainen, R, Kao, L, Chung, B, Strauss, JF & Miller, WL 1988, 'Human adrenodoxin: Cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells', Journal of Biological Chemistry, 巻. 263, 番号 7, pp. 3240-3244.
Picado-Leonard J, Voutilainen R, Kao L, Chung B, Strauss JF, Miller WL. Human adrenodoxin: Cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells. Journal of Biological Chemistry. 1988 1 1;263(7):3240-3244.
Picado-Leonard, J. ; Voutilainen, R. ; Kao, L. ; Chung, B. ; Strauss, J. F. ; Miller, W. L. / Human adrenodoxin : Cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells. :: Journal of Biological Chemistry. 1988 ; 巻 263, 番号 7. pp. 3240-3244.
@article{0f01f5c661124d3fa9dfb40e00c81186,
title = "Human adrenodoxin: Cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells",
abstract = "Adrenodoxin is an iron-sulfur protein serving as an electron transport intermediate for two mitochondrial steroidogenic cytochromes P450. We have cloned and sequenced three human adrenal adrenodoxin cDNAs. The longest 5'-untranslated region was 131 bases long, and the coding sequences, identical in all three clones, predict a preprotein of 180 amino acids. The 3'-untranslated regions were 235, 596, and 776 bases long due to the presence of alternate polyadenylation sites. RNA transfer blots showed multiple size species of adrenodoxin mRNA consistent with finding multiple polyadenylation sites. Similar sized cross-hybridizing RNA species are found abundantly in the adrenal and testis and to a lesser degree in RNA from human fetal brain, spleen, placenta, kidney, liver, and intestine, as well as in cultured fibroblasts, suggesting the same or a very similar iron-sulfur protein is found in mitochondria of nonsteroidogenic tissues. JEG-3 cells, a transformed progesterone-producing line of trophoblastic origin, accumulate mRNAs for cytochrome P450scc (the mitochondrial cholesterol side-chain cleavage enzyme), adrenodoxin, and the fos oncogene when stimulated with 8-bromo-cyclic AMP. Addition of actinomycin D to such cultures blocked cAMP-induced accumulation of mRNAs for cytochrome P450scc and adrenodoxin. Addition of cycloheximide or puromycin to such cultures substantially reduced basal levels and markedly attenuated the cAMP-induced accumulation of cytochrome P450scc mRNA, but augmented the accumulation of adrenodoxin and fos mRNAs in additive and multiplicative fashions, respectively. These data indicate that the cAMP-induced synthesis of the steroidogenic machinery is not wholly dependent on cycloheximide-sensitive protein mediators.",
author = "J. Picado-Leonard and R. Voutilainen and L. Kao and B. Chung and Strauss, {J. F.} and Miller, {W. L.}",
year = "1988",
month = "1",
day = "1",
language = "English",
volume = "263",
pages = "3240--3244",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "7",

}

TY - JOUR

T1 - Human adrenodoxin

T2 - Cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells

AU - Picado-Leonard, J.

AU - Voutilainen, R.

AU - Kao, L.

AU - Chung, B.

AU - Strauss, J. F.

AU - Miller, W. L.

PY - 1988/1/1

Y1 - 1988/1/1

N2 - Adrenodoxin is an iron-sulfur protein serving as an electron transport intermediate for two mitochondrial steroidogenic cytochromes P450. We have cloned and sequenced three human adrenal adrenodoxin cDNAs. The longest 5'-untranslated region was 131 bases long, and the coding sequences, identical in all three clones, predict a preprotein of 180 amino acids. The 3'-untranslated regions were 235, 596, and 776 bases long due to the presence of alternate polyadenylation sites. RNA transfer blots showed multiple size species of adrenodoxin mRNA consistent with finding multiple polyadenylation sites. Similar sized cross-hybridizing RNA species are found abundantly in the adrenal and testis and to a lesser degree in RNA from human fetal brain, spleen, placenta, kidney, liver, and intestine, as well as in cultured fibroblasts, suggesting the same or a very similar iron-sulfur protein is found in mitochondria of nonsteroidogenic tissues. JEG-3 cells, a transformed progesterone-producing line of trophoblastic origin, accumulate mRNAs for cytochrome P450scc (the mitochondrial cholesterol side-chain cleavage enzyme), adrenodoxin, and the fos oncogene when stimulated with 8-bromo-cyclic AMP. Addition of actinomycin D to such cultures blocked cAMP-induced accumulation of mRNAs for cytochrome P450scc and adrenodoxin. Addition of cycloheximide or puromycin to such cultures substantially reduced basal levels and markedly attenuated the cAMP-induced accumulation of cytochrome P450scc mRNA, but augmented the accumulation of adrenodoxin and fos mRNAs in additive and multiplicative fashions, respectively. These data indicate that the cAMP-induced synthesis of the steroidogenic machinery is not wholly dependent on cycloheximide-sensitive protein mediators.

AB - Adrenodoxin is an iron-sulfur protein serving as an electron transport intermediate for two mitochondrial steroidogenic cytochromes P450. We have cloned and sequenced three human adrenal adrenodoxin cDNAs. The longest 5'-untranslated region was 131 bases long, and the coding sequences, identical in all three clones, predict a preprotein of 180 amino acids. The 3'-untranslated regions were 235, 596, and 776 bases long due to the presence of alternate polyadenylation sites. RNA transfer blots showed multiple size species of adrenodoxin mRNA consistent with finding multiple polyadenylation sites. Similar sized cross-hybridizing RNA species are found abundantly in the adrenal and testis and to a lesser degree in RNA from human fetal brain, spleen, placenta, kidney, liver, and intestine, as well as in cultured fibroblasts, suggesting the same or a very similar iron-sulfur protein is found in mitochondria of nonsteroidogenic tissues. JEG-3 cells, a transformed progesterone-producing line of trophoblastic origin, accumulate mRNAs for cytochrome P450scc (the mitochondrial cholesterol side-chain cleavage enzyme), adrenodoxin, and the fos oncogene when stimulated with 8-bromo-cyclic AMP. Addition of actinomycin D to such cultures blocked cAMP-induced accumulation of mRNAs for cytochrome P450scc and adrenodoxin. Addition of cycloheximide or puromycin to such cultures substantially reduced basal levels and markedly attenuated the cAMP-induced accumulation of cytochrome P450scc mRNA, but augmented the accumulation of adrenodoxin and fos mRNAs in additive and multiplicative fashions, respectively. These data indicate that the cAMP-induced synthesis of the steroidogenic machinery is not wholly dependent on cycloheximide-sensitive protein mediators.

UR - http://www.scopus.com/inward/record.url?scp=0023850573&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023850573&partnerID=8YFLogxK

M3 - Article

C2 - 3343244

AN - SCOPUS:0023850573

VL - 263

SP - 3240

EP - 3244

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 7

ER -