Heat shock protein 90 interacts with vitamin D receptor in human leukemia cells

• Published in: Journal of steroid biochemistry and molecular biology Vol. 121; no. 1; pp. 114 - 116
• Main Authors: Marcinkowska, Ewa, Gocek, Elżbieta
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Kidlington Elsevier Ltd 01.07.2010; Elsevier
• Subjects: 1α,25-Dihydroxyvitamin D 3; Acute myeloid leukemia; Antineoplastic Agents - pharmacology; Benzoquinones - pharmacology; Biological and medical sciences; Cell Differentiation; Cell Line, Tumor; Cell Nucleus - metabolism; Co-immunoprecipitation; Cytosol - metabolism; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation, Neoplastic; Heat shock protein 90; Hematologic and hematopoietic diseases; HL-60 Cells; HL60; HSP90 Heat-Shock Proteins - metabolism; Humans; Immunoprecipitation; Lactams, Macrocyclic - pharmacology; Leukemia - metabolism; Leukemias. Malignant lymphomas. Malignant reticulosis. Myelofibrosis; Medical sciences; Models, Biological; Nucleus; Receptors, Calcitriol - metabolism; THP-1; Vertebrates: endocrinology; Vertebrates: reproduction; Vitamin D - metabolism; Vitamin D receptor; THP-1; Nucleus; Co-immunoprecipitation; Vitamin D receptor; Acute myeloid leukemia; 1α,25-Dihydroxyvitamin D 3; Heat shock protein 90; HL60; Human; Acute myelogenous leukemia; Malignant hemopathy; Heat shock protein; 1α,25-Dihydroxyvitamin D; Cancer
• ISSN: 0960-0760; 1879-1220
• DOI: 10.1016/j.jsbmb.2010.01.013

The active form of vitamin D, 1α,25-dihydroxyvitamin D 3 (1,25D), has a broad range of effects which are mediated by nuclear vitamin D receptor (VDR). Many experiments that investigate the role of VDR can be done in human acute myeloid leukemia (AML) cells, since these cells are responsive to 1,25D and express VDR in a 1,25D-regulated manner. In this paper we show that in HL60 and in THP-1 cells VDR protein interacts with heat shock protein 90 (Hsp90) and that Hsp90 is important for differentiation of AML cells. Geldanamycin (GA), an Hsp90 inhibitor, is able to suppress 1,25-induced differentiation of HL60 cells.