http://www.cnr.it/ontology/cnr/individuo/prodotto/ID4293
Inhibition of ERalpha-mediated trans-activation of human coagulation factor XII gene by heteromeric transcription factor NF-Y. (Articolo in rivista)
- Type
- Label
- Inhibition of ERalpha-mediated trans-activation of human coagulation factor XII gene by heteromeric transcription factor NF-Y. (Articolo in rivista) (literal)
- Anno
- 2001-01-01T00:00:00+01:00 (literal)
- Alternative label
Farsetti A., Narducci M., Moretti F., Nanni S., Mantovani R., Sacchi A., Pontecorvi A. (2001)
Inhibition of ERalpha-mediated trans-activation of human coagulation factor XII gene by heteromeric transcription factor NF-Y.
in Endocrinology (Philadelphia)
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- Farsetti A., Narducci M., Moretti F., Nanni S., Mantovani R., Sacchi A., Pontecorvi A. (literal)
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- Istituto di Neurobiologia e Medicina Molecolare, Consiglio Nazionale delle Ricerche (A.F., F.M.); Cattedra di Endocrinologia, Università di Roma La Sapienza (M.N.); Dipartimento Biologia Animale, Università di Modena e Reggio (R.M.); Istituto di Patologia Medica, Università Cattolica del Sacro Cuore (A.P.); and Laboratorio di Oncogenesi Molecolare, Istituto Tumori Regina Elena (A.F., M.N., F.M., S.N., A.S., A.P.) (literal)
- Titolo
- Inhibition of ERalpha-mediated trans-activation of human coagulation factor XII gene by heteromeric transcription factor NF-Y. (literal)
- Abstract
- Human coagulation factor XII promoter contains an estrogen response element that mediates ligand-activated ERalpha induction of coagulation factor XII gene expression. The 3'-half of coagulation factor XII-estrogen response element overlaps a putative CCAAT box, the widespread regulatory element specifically recognized by the heteromeric transcription factor NF-Y. Transient cotransfection of NF-Y and ERalpha results in strong inhibition of estrogen stimulation of coagulation factor XII promoter activity. NF-Y antagonism is primarily exerted by the NF-YA subunit and does not require binding to the CCAAT element, as NF-YA mutants with impaired DNA binding capacity retain the ability to inhibit ERalpha trans-activation. EMSAs with increasing concentrations of recombinant NF-Y do not detect the formation of NF-Y-DNA complexes or show impairment of ERalpha binding to estrogen response element. Immunoprecipitation of whole cell extracts with anti-ERalpha antibody reveals an in vivo association between the two transcription factors, which is abolished by deletion of the NF-YA carboxyl-terminus. In functional experiments with sequential NF-YA deletion mutants the HAP2-homology region appears essential in eliciting NF-YA antagonistic activity. In conclusion, our results demonstrate that heteromeric transcription factor NF-Y inhibits estrogen induction of coagulation factor XII promoter in a DNA binding-independent fashion and suggest a novel role for NF-Y as a partner for the ERalpha transcription complex. (literal)
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