Morphologic Change and Elevation of Cortisol Secretion in Cultured Human Normal Adrenocortical Cells Caused by Mutant p21[sup K-ras] Protein

Wu, Chia-Hung; Lee, Su-Chen; Chiu, Hua-Hsien; Yang, Yuan-Chieh; Lian, Shen-Tsuen; Shin, Shyi-Jang; Lin, Shiu-Ru
January 2002
DNA & Cell Biology;Jan2002, Vol. 21 Issue 1, p21
Academic Journal
In our previous study on the tumorigenesis of human functional adrenal tumors, we observed a high frequency of K-ras point mutations in clinical specimens. Furthermore, we cloned the mutated K-ras gene from the tumors and inserted it into vectors to transfect normal bovine adrenocortical cells to express the mutated K-ras gene. The mRNA level of steroidogenic enzymes such as cholesterol sidechain cleavage enzyme (P450[sub SCC]), 17a-hydroxylase/17,20-lyase (P450[sub c17]), and 3�-hydroxysteroid dehydrogenase (3�HSD) in the mutant K-ras stably transfected cells were elevated. Cultured normal adrenocortical cells from donors and patients with adrenocortical tumors were then transfected with mutant K-ras expression plasmids constructed from human adrenal tumors. Stable transfectants grew faster than normal cells. Additionally, morphologic change was observed in the transfected cells. Moreover, when the synthesis of hormones was analyzed, the mRNA of P450[sub SCC], P450[sub C17], and 3�HSD was found to have increased, and the level of cortisol was 18 to 25 times that in control cells. The increased steroid hormone production in mutant K-ras-transfected cells was reversed by lovastatin, a pharmacologic inhibitor of p21[sup ras] function. These results, combined with previous reports of steroidogenic K-ras in bovine adrenocortical cells, suggest that the K-ras oncogene is involved in steroidogenesis in human adrenocortical cells.


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