Citations 7

Regulation of Cellular Growth by 1,25-Dihydroxyvitamin D3-Mediated Growth Factor Expression

Physiology | December 24, 2017 | Volume: 14 | Issue: 1 | Pages: 37-40

10.1152/physiologyonline.1999.14.1.37 | PMID 11390816

Although the primary function of 1,25-dihydroxyvitamin D3 [1,25(OH)2D3] is the regulation of calcium and phosphorus metabolism, it also regulates the growth and differentiation of several different cell types. Recent work suggests that 1,25(OH)2D3 regulates cellular growth by altering the synthesis of growth factors and growth factor responses.
Manganese Superoxide Dismutase Regulates a Metabolic Switch during the Mammalian Cell Cycle

Cancer Research | June 19, 2012 | Volume: 72 | Issue: 15 | Pages: 3807-3816

10.1158/0008-5472.can-11-1063 | PMID 22710435

Abstract Proliferating cells consume more glucose to cope with the bioenergetics and biosynthetic demands of rapidly dividing cells as well as to counter a shift in cellular redox environment. This study investigates the hypothesis that manganese superoxide dismutase (MnSOD) regulates cellular redox flux and glucose consumption during the cell cycle. A direct correlation was observed between glucose consumption and percentage of S-phase cells in MnSOD wild-type fibroblasts, which was absent in MnSOD homozygous knockout fibroblasts. Results from electron paramagnetic resonance spectroscopy and flow cytometric assays showed a significant increase in cellular superoxide levels in S-phase cells, which was associated with an increase in glucose and oxygen consumption, and a decrease in MnSOD activity. Mass spectrometry results showed a complex pattern of MnSOD-methylation at both lysine (68, 89, 122, and 202) and arginine (197 and 216) residues. MnSOD protein carrying a K89A mutation had significantly lower activity compared with wild-type MnSOD. Computational-based simulations indicate that lysine and arginine methylation of MnSOD during quiescence would allow greater accessibility to the enzyme active site as well as increase the positive electrostatic potential around and within the active site. Methylation-dependent changes in the MnSOD conformation and subsequent changes in the electrostatic potential around the active site during quiescence versus proliferation could increase the accessibility of superoxide, a negatively charged substrate. These results support the hypothesis that MnSOD regulates a “metabolic switch” during progression from quiescent through the proliferative cycle. We propose MnSOD as a new molecular player contributing to the Warburg effect. Cancer Res; 72(15); 3807–16. ©2012 AACR.
An AP-1 Site in the Nerve Growth Factor Promoter Is Essential for 1,25-Dihydroxyvitamin D3-Mediated Nerve Growth Factor Expression in Osteoblasts

Biochemistry | July 26, 2002 | Volume: 37 | Issue: 17 | Pages: 5988-5994

10.1021/bi972965+ | PMID 9558335

Zinc Binding Properties of the DNA Binding Domain of the 1,25-Dihydroxyvitamin D3 Receptor

Biochemistry | July 26, 2002 | Volume: 36 | Issue: 34 | Pages: 10482-10491

10.1021/bi970561b | PMID 9265628

Determination of Calcium-Binding Sites in Rat Brain Calbindin D28K by Electrospray Ionization Mass Spectrometry

Biochemistry | July 26, 2002 | Volume: 36 | Issue: 12 | Pages: 3535-3542

10.1021/bi9628329 | PMID 9132004

Low temperature aqueous electrospray ionization mass spectrometry of noncovalent complexes

Journal of the American Society for Mass Spectrometry | July 25, 2002 | Volume: 9 | Issue: 6 | Pages: 580-584

10.1016/s1044-0305(98)00019-1 | PMID 9879371

Zinc-induced conformational changes in the DNA-binding domain of the vitamin D receptor determined by electrospray ionization mass spectrometry

Journal of the American Society for Mass Spectrometry | July 25, 2002 | Volume: 9 | Issue: 1 | Pages: 8-14

10.1016/s1044-0305(97)00229-8 | PMID 9679591