D
Dong Lin
Researcher at University of California, San Francisco
Publications - 18
Citations - 2519
Dong Lin is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Pregnenolone & Cholesterol side-chain cleavage enzyme. The author has an hindex of 13, co-authored 17 publications receiving 2462 citations. Previous affiliations of Dong Lin include Albert Einstein College of Medicine & University of California.
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Journal ArticleDOI
Role of steroidogenic acute regulatory protein in adrenal and gonadal steroidogenesis.
Dong Lin,Teruo Sugawara,Jerome F. Strauss,Barbara J. Clark,Douglas M. Stocco,Paul Saenger,Alan D. Rogol,Walter L. Miller +7 more
TL;DR: In three unrelated individuals with this disorder, steroidogenic acute regulatory protein, which enhances the mitochondrial conversion of cholesterol into pregnenolone, was mutated and nonfunctional, providing genetic evidence that this protein is indispensable normal adrenal and gonadal steroidogenesis.
Journal ArticleDOI
Human steroidogenic acute regulatory protein: functional activity in COS-1 cells, tissue-specific expression, and mapping of the structural gene to 8p11.2 and a pseudogene to chromosome 13
Teruo Sugawara,John A. Holt,Deborah A. Driscoll,Jerome F. Strauss,Dong Lin,Walter L. Miller,David A. Patterson,K P Clancy,Iris Hart,Barbara J. Clark +9 more
TL;DR: Steroidogenic acute regulatory protein (StAR) appears to mediate the rapid increase in pregnenolone synthesis stimulated by tropic hormones and StAR mRNA levels are regulated by cAMP.
Journal ArticleDOI
Structure of the human steroidogenic acute regulatory protein (StAR) gene: StAR stimulates mitochondrial cholesterol 27-hydroxylase activity.
Teruo Sugawara,Dong Lin,John A. Holt,Kumiko O. Martin,Norman B. Javitt,Walter L. Miller,Jerome F. Strauss +6 more
TL;DR: expression of StAR in COS-1 cells cotransfected with cholesterol 27-hydroxylase and adrenodoxin resulted in a 6-fold increase in formation of 3 beta-hydroxy-5-cholestenoic acid, demonstrating that StAR's actions are not specific to steroidogenesis but extend to other mitochondrial cholesterol-metabolizing enzymes.
Journal ArticleDOI
Steroid 17 alpha-hydroxylase and 17,20-lyase activities of P450c17: contributions of serine106 and P450 reductase.
TL;DR: The data suggest that the essential role of Ser106 is in the active site, rather than in interacting with P450 reductase, and that electron transfer may play an important role in regulating the 17,20-lyase activity of P450c17.
Journal ArticleDOI
Missense mutation serine106----proline causes 17 alpha-hydroxylase deficiency.
TL;DR: This work uses site-directed mutagenesis of the normal P450c17 cDNA to construct the Pro106 mutant, and expressed both the normal and mutant sequences in monkey COS-1 cells and in yeast, proving that the Ser106----Pro mutation abolished the 17 alpha-hydroxylase and 17,20-lyase activities.