Send to

Choose Destination
Biochem Biophys Res Commun. 2001 Dec 21;289(5):1150-6.

The vitamin D receptor mediates rapid changes in muscle protein tyrosine phosphorylation induced by 1,25(OH)(2)D(3).

Author information

Departamento de Biología, Bioquímica and Farmacia, Universidad Nacional del Sur., Bahía Blanca, San Juan 670, 8000, Argentina.


It has been recently shown that the fast non-genomic responses of 1,25(OH)(2)-vitamin D(3) [1,25(OH)(2)D(3)] in skeletal muscle cells involve tyrosine phosphorylation of MAP kinase (ERK1/2), c-Src kinase and the oncoprotein c-myc. In the present work, blockade of vitamin D receptor (VDR) expression (> or =80%) by preincubation of chick embryonic muscle cells with three different antisense oligonucleotides against the VDR mRNA (AS-VDR ODNs) significantly reduced (-94%) 1,25(OH)(2)D(3) stimulation of c-myc tyrosine phosphorylation and inhibited c-Src tyrosine dephosphorylation implying lack of c-Src activation by the hormone. Coimmunoprecipitation experiments revealed that 1,25(OH)(2)D(3) induces the formation of complexes between c-Src and c-myc, in agreement with the above results and previous studies showing hormone-dependent association between c-Src and tyrosine phosphorylated VDR and c-Src mediated c-myc tyrosine phosphorylation. MAPK tyrosine phosphorylation by 1,25(OH)(2)D(3) was affected to a lesser extent (-35%) by transfection with AS-VDR ODNs implying that both VDR-dependent and VDR-independent signalling mediate hormone stimulation of MAPK. These are the first results providing direct evidence on the participation of the VDR in non-genomic 1,25(OH)(2)D(3) signal transduction. Activation of tyrosine phosphorylation cascades through this mechanism may contribute to hormone regulation of muscle growth.

[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center