The vitamin D receptor mediates rapid changes in muscle protein tyrosine phosphorylation induced by 1,25(OH)2-vitamin D3

BUITRAGO C; VAZQUEZ G; BOLAND R; RUSSO DE BOLAND A

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

ACADEMIC PRESS INC ELSEVIER SCIENCE

Lugar: Amsterdam; Año: 2001 vol. 289 p. 1150 - 1156

0006-291X

It has been recently shown that the fast nongenomic responses of 1,25(OH)2-vitamin D3 [1,25(OH)2- D3] 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 (>80%) by preincubation of chick embryonic muscle cells with three different antisense oligonucleotides against the VDR mRNA (AS-VDR ODNs) significantly reduced (294%) 1,25(OH)2D3 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)2D3 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)2D32D3 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)2D3 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)2D32D3 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)2D32D3 was affected to a lesser extent (235%) by transfection with AS-VDR ODNs implying that both VDRdependent 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)2D3 signal transduction. Activation of tyrosine phosphorylation cascades through this mechanism may contribute to hormone regulation of muscle growth.2D3 signal transduction. Activation of tyrosine phosphorylation cascades through this mechanism may contribute to hormone regulation of muscle growth.2-vitamin D3 [1,25(OH)2- D3] 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 (>80%) by preincubation of chick embryonic muscle cells with three different antisense oligonucleotides against the VDR mRNA (AS-VDR ODNs) significantly reduced (294%) 1,25(OH)2D3 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)2D3 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)2D32D3 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)2D3 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)2D32D3 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)2D32D3 was affected to a lesser extent (235%) by transfection with AS-VDR ODNs implying that both VDRdependent 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)2D3 signal transduction. Activation of tyrosine phosphorylation cascades through this mechanism may contribute to hormone regulation of muscle growth.2D3 signal transduction. Activation of tyrosine phosphorylation cascades through this mechanism may contribute to hormone regulation of muscle growth.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 (>80%) by preincubation of chick embryonic muscle cells with three different antisense oligonucleotides against the VDR mRNA (AS-VDR ODNs) significantly reduced (294%) 1,25(OH)2D3 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)2D3 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)2D32D3 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)2D3 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)2D32D3 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)2D32D3 was affected to a lesser extent (235%) by transfection with AS-VDR ODNs implying that both VDRdependent 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)2D3 signal transduction. Activation of tyrosine phosphorylation cascades through this mechanism may contribute to hormone regulation of muscle growth.2D3 signal transduction. Activation of tyrosine phosphorylation cascades through this mechanism may contribute to hormone regulation of muscle growth.>80%) by preincubation of chick embryonic muscle cells with three different antisense oligonucleotides against the VDR mRNA (AS-VDR ODNs) significantly reduced (294%) 1,25(OH)2D3 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)2D3 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)2D32D3 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)2D3 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)2D32D3 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)2D32D3 was affected to a lesser extent (235%) by transfection with AS-VDR ODNs implying that both VDRdependent 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)2D3 signal transduction. Activation of tyrosine phosphorylation cascades through this mechanism may contribute to hormone regulation of muscle growth.2D3 signal transduction. Activation of tyrosine phosphorylation cascades through this mechanism may contribute to hormone regulation of muscle growth.294%) 1,25(OH)2D3 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)2D3 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)2D32D3 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)2D3 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)2D32D3 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)2D32D3 was affected to a lesser extent (235%) by transfection with AS-VDR ODNs implying that both VDRdependent 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)2D3 signal transduction. Activation of tyrosine phosphorylation cascades through this mechanism may contribute to hormone regulation of muscle growth.2D3 signal transduction. Activation of tyrosine phosphorylation cascades through this mechanism may contribute to hormone regulation of muscle growth.235%) by transfection with AS-VDR ODNs implying that both VDRdependent 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)2D3 signal transduction. Activation of tyrosine phosphorylation cascades through this mechanism may contribute to hormone regulation of muscle growth.2D3 signal transduction. Activation of tyrosine phosphorylation cascades through this mechanism may contribute to hormone regulation of muscle growth.