Non-genomic stimulation of tyrosine phosphorylation cascades by 1,25(OH)2D3 by VDR-dependent and -independent mechanisms in muscle cells

Autor: Carolina Baldi, Daniela A. Capiati, Susana Morelli, Claudia Buitrago, Ricardo Boland, Guillermo Vazquez, Ana Russo de Boland, Graciela Santillán
Rok vydání: 2002
Předmět:
Otras Ciencias Biológicas
Clinical Biochemistry
Chick Embryo
Protein tyrosine phosphatase
Biology
TRP
Biochemistry
Calcitriol receptor
Receptor tyrosine kinase
Ciencias Biológicas
CSK Tyrosine-Protein Kinase
Proto-Oncogene Proteins c-myc
chemistry.chemical_compound
Endocrinology
Animals
NON-GENOMIC
Phosphorylation
Tyrosine
Muscle
Skeletal
Molecular Biology
Cells
Cultured
Protein Kinase C
VDR
Cell Nucleus
Pharmacology
TYROSINE PHOSPHORYLATION
Organic Chemistry
Tyrosine phosphorylation
MUSCLE
Protein-Tyrosine Kinases
Cell biology
Enzyme Activation
Protein Transport
Antisense Elements (Genetics)
src-Family Kinases
chemistry
Type C Phospholipases
Steroid Hydroxylases
biology.protein
1
25(OH)2D3
Receptors
Calcitriol
Calcium
Mitogen-Activated Protein Kinases
Tyrosine kinase
CIENCIAS NATURALES Y EXACTAS
Proto-oncogene tyrosine-protein kinase Src
Zdroj: Steroids. 67:477-482
ISSN: 0039-128X
DOI: 10.1016/s0039-128x(01)00182-9
Popis: Studies with different cell types have shown that modulation of various of the fast as well as long-term responses to 1,25(OH)2D3 depends on the activation of tyrosine kinase pathways. Recent investigations of our laboratory have demonstrated that 1,25(OH)2D3 rapidly stimulates in muscle cells tyrosine phosphorylation of PLC-γ and the growth-related proteins MAPK and c-myc. We have now obtained evidence using antisense technology indicating that VDR-dependent activation of Src mediates the fast stimulation of tyrosine phosphorylation of c-myc elicited by the hormone. This non-genomic action of 1,25(OH)2D3 requires tyrosine phosphorylation of the VDR. Immunoprecipitation under native conditions coupled to Western blot analysis revealed 1,25(OH)2D3-dependent formation of complexes between Src and the VDR and c-myc. However, the activation of MAPK by the hormone was only partially mediated by the VDR and required in addition increased PKC and intracellular Ca2+. Following its phosphorylation, MAPK translocates into the nucleus where it regulates c-myc transcription. Altogether these results indicate that tyrosine phosphorylation plays a role in the stimulation of muscle cell growth by 1,25(OH)2D3. Data were also obtained involving tyrosine kinases and the VDR in hormone regulation of the Ca2+ messenger system by mediating the stimulation of store-operated calcium (SOC; TRP) channels. Congruent with this action, 1,25(OH)2D3 induces a rapid translocation of the VDR to the plasma cell membrane which can be blocked by tyrosine kinase inhibitors. Of mechanistic relevance, an association between the VDR and TRP proteins with the participation of the scaffold protein INAD was shown. Fil: Boland, Ricardo Leopoldo. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; Argentina Fil: Russo de Boland, Ana. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina Fil: Buitrago, Claudia Graciela. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Bahía Blanca; Argentina Fil: Morelli, Susana Ana. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina Fil: Santillán, Graciela Edith. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina Fil: Vazquez, Guillermo. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina Fil: Capiati, Daniela Andrea. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Baldi, Carolina. Universidad Nacional del Sur. Departamento de Biología, Bioquímica y Farmacia; Argentina
Databáze: OpenAIRE
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