Disease relevance of Tgfb1i1

• Finally, a colony formation assay using an hic-5 expression vector driven by the cytomegalovirus promoter suggested that hic-5 overexpression had a cytostatic effect on cellular growth, depending upon the cell type [1].

High impact information on Tgfb1i1

• Hic-5 and PPARgamma colocalize to the villus epithelium of the small intestine, and their expression during embryonic gut development correlates with the transition from endoderm to a specialized epithelium; expression of both these factors is reduced in tumors [2].
• We show here that PPARgamma interacts with Hic-5, a coactivator protein expressed in gut epithelial cells [2].
• Taken together, these data suggest that DALP and Hic-5 act upstream of MyoD and function as phylogenetically conserved "switches" to block muscle differentiation and induce death [3].
• Hic-5 expression is specifically and dramatically induced in normal myoblasts that die after removal of trophic support [3].
• Ectopic expression of DALP, or its mammalian ortholog Hic-5, blocks differentiation and induces apoptosis in mouse C(2)C(12) myoblasts [3].

Biological context of Tgfb1i1

• The ability of Hic-5/ARA55 to shuttle between the nuclear and cytoplasmic compartments was revealed on inhibition of nuclear export with leptomycin B [4].
• From in vitro binding experiments using deletion and point mutations, it was demonstrated that the essential domain in Hic-5 for the binding was LIM 3 [5].
• Finally, forced expression of Hic-5 during 3T3-L1 preadipocyte differentiation inhibits adipogenesis while inducing inappropriate expression of several mRNAs characteristic of gut epithelium in these mesenchymal cells [2].
• We conclude that hic-5 is a true hsp27 binding protein and inhibits the ability of hsp27 to provide protection against heat shock in an interaction-dependent manner [6].
• Characterization of the TGF beta 1-inducible hic-5 gene that encodes a putative novel zinc finger protein and its possible involvement in cellular senescence [1].

Anatomical context of Tgfb1i1

• Furthermore, a prostate stromal cell line, WPMY-1 cells, expresses Hic-5/ARA55, which is localized both at focal adhesion complexes and within the soluble cytoplasmic compartment [4].
• Hic-5/ARA55, a LIM domain-containing nuclear receptor coactivator expressed in prostate stromal cells [4].
• Like paxillin, Hic-5 is localized in focal adhesion plaques in association with focal adhesion kinase in cultured fibroblasts [5].
• The expression of hic-5 mRNA was repressed in Ki-ras-transformed mouse fibroblasts and in several cell lines established from human tumor [1].
• Uni-axial stretching regulates intracellular localization of Hic-5 expressed in smooth-muscle cells in vivo [7].

Associations of Tgfb1i1 with chemical compounds

• Finally, the mechanism of Hic-5/ARA55 coactivator activity in WPMY-1 cells was revealed by chromatin immunoprecipitation analysis that showed its androgen-dependent recruitment to the promoter of the stromal androgen-responsive keratinocyte growth factor gene [4].
• In conclusion, Hic-5 may participate in the regulation of signaling cascade through its interaction with distinct tyrosine kinases and phosphatases [5].
• In this study, we found that Hic-5 accumulated in the nucleus in response to oxidants such as H(2)O(2) [8].
• Identification and analysis of Hic-5/ARA55 isoforms: Implications for integrin signaling and steroid hormone action [9].

Regulatory relationships of Tgfb1i1

• Our previous study suggested that Hic-5 participates in the transcriptional control of several genes such as the c-fos and p21 genes [10].

Other interactions of Tgfb1i1

• However, this interaction was not essential for recruitment of Hic-5 to focal adhesions, since its subcellular localization was similar in FAK(-/-) cells [11].
• The Hic-5 level was markedly decreased when cells became immortalized, whereas that of paxillin was increased [11].
• The steady-state levels of TSC-36, TSC-128 and TSC-160 increased almost tenfold, whereas those of TSC-5, TSC-115 and TSC-161 were elevated at most threefold [12].
• Two of these genes, Hic-5, a possible negative regulator of muscle differentiation, and the transcription enhancing factor TEF-5 were selected and shown by in situ hybridizations to be expressed in the early developing heart [13].
• Thus, Hic-5 was suggested to have a potential function as a cofactor in the transcriptional complex that contains Sp1, playing a role in gene transcription in the nucleus as well as in integrin signaling at focal adhesion sites [10].

Analytical, diagnostic and therapeutic context of Tgfb1i1

• In the present study, we examined the expression of Hic-5 among mouse tissues by immunohistochemistry and found its expression only in smooth-muscle cells in several tissues [7].
• Physical mapping and fluorescent in situ hybridization analysis indicated that the hic-5 gene is located on mouse chromosome 7, 60 [14].

References