Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1988-4-6
pubmed:databankReference
pubmed:abstractText
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.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3240-4
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:3343244-8-Bromo Cyclic Adenosine Monophosphate, pubmed-meshheading:3343244-Adrenal Glands, pubmed-meshheading:3343244-Adrenodoxin, pubmed-meshheading:3343244-Amino Acid Sequence, pubmed-meshheading:3343244-Base Sequence, pubmed-meshheading:3343244-Cell Line, Transformed, pubmed-meshheading:3343244-Cholesterol Side-Chain Cleavage Enzyme, pubmed-meshheading:3343244-Cloning, Molecular, pubmed-meshheading:3343244-Cycloheximide, pubmed-meshheading:3343244-DNA, pubmed-meshheading:3343244-DNA, Recombinant, pubmed-meshheading:3343244-Female, pubmed-meshheading:3343244-Fetus, pubmed-meshheading:3343244-Gene Expression Regulation, pubmed-meshheading:3343244-Humans, pubmed-meshheading:3343244-Male, pubmed-meshheading:3343244-Molecular Sequence Data, pubmed-meshheading:3343244-Nucleic Acid Hybridization, pubmed-meshheading:3343244-Placenta, pubmed-meshheading:3343244-Pregnancy, pubmed-meshheading:3343244-RNA, Messenger, pubmed-meshheading:3343244-Testis, pubmed-meshheading:3343244-Tissue Distribution
pubmed:year
1988
pubmed:articleTitle
Human adrenodoxin: cloning of three cDNAs and cycloheximide enhancement in JEG-3 cells.
pubmed:affiliation
Department of Pediatrics, University of California, San Francisco 94143.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't