High impact information on CHD9

• Characterization and functional analysis of CReMM, a novel chromodomain helicase DNA-binding protein [1].
• In silico translation defined CReMM as a multiple domains protein including two chromodomains, SNF2/ATPase, helicase C domain and an A/T-DNA-binding domain (DBD) [1].
• CReMM protein structural motifs and proven biochemical activities highlight its role in chromatin remodeling [1].
• MBA-15 cells were challenged with dexamethasone (Dex) or 17beta-estradiol and quantification of CReMM at the protein (ELISA) and mRNA (RT-PCR) levels had shown that Dex upregulated CReMM levels [2].
• CReMM appears transiently during mesenchymal cell differentiation, being detected first in osteoprogenitors and declining in mature cells [3].

Biological context of CHD9

• The identification of CReMM and its tissue distribution and function provides an attractive clue for the study of transcriptional regulation of osteogenic cells' maturation [3].
• In this study, we analyzed CReMM expression on RNA and protein levels during embryonic development in mouse skeletal tissues [3].
• We used bone marrow derived osteogenic cell line (MBA-15) to elaborate on the regulation of CReMM expression in correlation with cell proliferation and co-expression with alkaline phosphatase (ALK) [2].

Anatomical context of CHD9

• PRIC320, a transcription coactivator, isolated from peroxisome proliferator-binding protein complex [4].
• Analysis in ex vivo cultured marrow stromal cells (MSC) from rats revealed higher level of CReMM in cells from young (3 months), when compared to cells from old (15 months) rats [2].
• In summary, CReMM is a CHD protein expressed by osteoprogenitors, and we suggest it plays a role in mediating transcriptional response to hormones that coordinate osteoblast function [2].
• A novel aspect of the study elaborates on in vivo association of CReMM with promoters in cells obtained by laser capture micro-dissection (LCM) technique from periosteum and endochondreal ossification regions [3].

Associations of CHD9 with chemical compounds

• We conclude that ciprofibrate, a PPARalpha ligand, binds a multiprotein complex and PRIC320 cloned from this complex functions as a nuclear receptor coactivator [4].
• Treatment with 17beta-estradiol enhanced the binding to estrogen receptor and abolished binding to the prolactin receptor promoters; CReMM interaction with osteocalcin promoter was identified constantly [5].

Other interactions of CHD9

• CReMM interaction with BMP4 and biglycan promoters in the marrow stromal cells was challenged with transforming growth factor-beta [5].
• Within the MSC population, osteogenic clones showed higher levels of CReMM then non-osteogenic ones [2].

Analytical, diagnostic and therapeutic context of CHD9

• Electrophoresis mobility-shift assay (EMSA) validated that CReMM binds to A/T-rich DNA [1].
• SDS-PAGE and matrix-assisted laser desorption/ionization reflection time-of-flight mass spectrometric analyses of ciprofibrate-binding proteins from liver nuclear extracts obtained using ciprofibrate-Sepharose affinity matrix resulted in the identification of a new high molecular weight nuclear receptor coactivator, which we designated PRIC320 [4].
• Chromatin immunoprecipitation assay was applied to follow the dynamics of CReMM binding to A/T-rich regions on promoters of genes that play a role in osteoblast maturation [5].

References