This Article Full Text Full Text (PDF) All Versions of this Article: 146/8/3409    most recent Author Manuscript (PDF) Purchase Article View Shopping Cart Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Copyright Permission Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Alimov, A. P. Articles by Koszewski, N. J. Search for Related Content PubMed PubMed Citation Articles by Alimov, A. P. Articles by Koszewski, N. J.

Transactivation of the Parathyroid Hormone Promoter by Specificity Proteins and the Nuclear Factor Y Complex

Division of Nephrology, Bone and Mineral Metabolism (A.P.A., H.H.M., N.J.K.) and Departments of Physiology (O.-K.P.-S.) and Molecular and Cellular Biochemistry (K.D.S.), University of Kentucky Medical Center, Lexington, Kentucky 40536

Address all correspondence and requests for reprints to: N. J. Koszewski, University of Kentucky Medical Center, Division of Nephrology, Bone and Mineral Metabolism, Room MN562, 800 Rose Street, Lexington, Kentucky 40536-0298. E-mail: njhosz0{at}uky.edu.

We previously identified a highly conserved specificity protein 1 (Sp1) DNA element in mammalian PTH promoters that acted as an enhancer of gene transcription and bound Sp1 and Sp3 proteins present in parathyroid gland nuclear extracts. More recently, a nuclear factor (NF)-Y element (NF-Y_prox) was also described by our group, which was located approximately 30 bp downstream from the Sp1 site in the human PTH (hPTH) promoter and by itself acted as a weak enhancer of gene transcription. We now report that Sp proteins and NF-Y can synergistically enhance transcription of a minimal hPTH promoter construct. Positioning of the Sp1 DNA element appears to be critical for this synergism because deviations of one half of a helical turn caused an approximate 60% decrease in transactivation. Finally, examination of the bovine PTH (bPTH) promoter also revealed Sp1/NF-Y synergism, in conjunction with the identification of an analogous NF-Y binding site similarly positioned downstream from the bPTH Sp1 element. In summary, synergistic transactivation of the hPTH and bPTH promoters is observed by Sp proteins and the NF-Y complex. The conservation of this transactivation in the human and bovine promoters suggests that this may be a principle means of enhancing PTH gene transcription.

This article has been cited by other articles:

				M. C. Chia, A. Leung, T. Krushel, N. M. Alajez, K. W. Lo, P. Busson, H. J. Klamut, C. Bastianutto, and F.-F. Liu Nuclear Factor-Y and Epstein Barr Virus in Nasopharyngeal Cancer Clin. Cancer Res., February 15, 2008; 14(4): 984 - 994. [Abstract] [Full Text] [PDF]

				Y. Jiang and S. S Stojilkovic Molecular cloning and characterization of {alpha}1-soluble guanylyl cyclase gene promoter in rat pituitary cells J. Mol. Endocrinol., December 1, 2006; 37(3): 503 - 515. [Abstract] [Full Text] [PDF]

				L. J. Suva PTH Expression, Not Always where You Think ... J. Clin. Endocrinol. Metab., February 1, 2006; 91(2): 396 - 397. [Full Text] [PDF]

				J. N. VanHouten, N. Yu, D. Rimm, J. Dotto, A. Arnold, J. J. Wysolmerski, and R. Udelsman Hypercalcemia of Malignancy due to Ectopic Transactivation of the Parathyroid Hormone Gene J. Clin. Endocrinol. Metab., February 1, 2006; 91(2): 580 - 583. [Abstract] [Full Text] [PDF]