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Protein‐DNA Array‐based identification of transcription factor activities following dehydration in the hypothalomo‐neurohypophyseal system
Author(s) -
Qiu Jing,
Gouraud Sabine Sandra,
Yao Song,
Paton Julian F.R.,
Murphy David
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a354-d
Subject(s) - transcription factor , dehydration , biology , microbiology and biotechnology , gene , dna , creb , homeostasis , transcription (linguistics) , chemistry , genetics , biochemistry , linguistics , philosophy
The hypothalamo‐neurohypophyseal system (HNS) of mammals controls the homeostatic function of water balance and salt excretion. Physiological activation of the HNS by dehydration results in the release of vasopressin into the circulation, which promotes water conservation at the level of the kidney. Concomitantly, fully differentiated neurons of the HNS undergo phenotypic changes, a property known as function‐related plasticity, which may serve as an adaptive response to functional demand. These changes are associated with alterations in gene expression, presumably, at least in part, mediated by transcription factors. Since little is known about which transcription factors mediate these gene changes, the DNA binding capacity of nuclear extracts of supraoptic nuclei (SON) to 345 consensus sequences was analyzed in samples prepared from normal and dehydrated rats using Panomics Protein/DNA Array. Following statistical analysis, the binding capacity of AP‐1, CREB, Myc‐max and other 8 transcription factors were shown to be significantly up‐regulated in the SON following dehydration and PEBP2, EGR1, and MTB‐Zf were shown to be significantly down‐regulated. We are currently using electrophortic mobility shift assays (EMSA) to validate the results of the Protein‐DNA array. In addition, we are using a real‐time biomolecular interaction analysis (BIA) coupled with Mass Spectrometry to identify the components of the protein complexes that bind to these consensus sequences. Supported by British Heart Foundation and BBSRC.