Disease relevance of Id2

• These findings are consistent with the hypothesis that Id2 and p53 are responsive to unloading-induced muscle atrophy [1].
• Differentiating Rcho-1 cells in hypoxia did not alter the expression of lineage-specific markers; however, hypoxia did inhibit the downregulation of the trophoblast stem cell marker Id2 [2].

Psychiatry related information on Id2

• We used real-time RT-PCR to examine the effects of these factors on the expression of mRNA encoding the Id proteins, demonstrating an increase in Id2 and Id3 expression in Sertoli cells treated with thyroid hormone, retinoic acid, or testosterone [3].

High impact information on Id2

• Excitation through this pathway acts to inhibit expression of the glial fate genes Hes1 and Id2 and increase expression of NeuroD, a positive regulator of neuronal differentiation [4].
• Adenoviral overexpression of Pax4 caused a 3.5-fold increase in beta-cell proliferation with a concomitant 1.9-, 4-, and 5-fold increase in Bcl-xL (antiapoptotic), c-myc, and Id2 mRNA levels, respectively [5].
• Thus, we investigated the role of Id2 in SMC growth and cell cycle regulation [6].
• Finally, in a rat carotid model of arterial injury, Id2 was expressed in a temporal pattern that parallels the kinetics of cellular proliferation [6].
• Contribution of the helix-loop-helix factor Id2 to regulation of vascular smooth muscle cell proliferation [6].

Biological context of Id2

• The results demonstrated that overexpression of Id2 resulted in a significant enhancement of SMC growth via increased S-phase entry [6].
• Commitment to giant cell differentiation is under developmental control, involving down-regulation of Id1 and Id2, concomitant with up-regulation of the basic helix-loop-helix factor Hxt and acquisition of increased adhesiveness [7].
• It has been noted that putative phosphorylation sites for various protein kinases exist in rat Id1, Id2 and Id3 [8].
• Denervation stimulates apoptosis but not Id2 expression in hindlimb muscles of aged rats [9].
• The fact that the molecular mechanisms of liver regeneration are not completely understood prompted us to study the fate of Id2 in proliferating liver [10].

Anatomical context of Id2

• Hindlimb unloading increases muscle content of cytosolic but not nuclear Id2 and p53 proteins in young adult and aged rats [1].
• Moreover, our data indicate that aging is accompanied with altered abundances of HSP70-1 and HSP70-2 mRNA, in addition to Id2, p53, HSP70, and HSP27 protein in rat gastrocnemius muscle [1].
• However, there was no significant difference in Id2 mRNA expression between serum-treated and control astrocyte cultures within 1 h of serum induction [11].
• The objectives of this study were to determine the mRNA expression and the immunocytolocalization of Id1, Id2, Id3, and Id4 in the epididymis of adult rats and to determine the Id3 protein expression profile in orchidectomized and in aged animals [12].
• The Id family of helix-loop-helix factors (Id1, Id2, and Id3) expressed in many types of cells has been reported to negatively regulate myoblast differentiation and is required for G1/S progression of arrested fibroblasts [11].

Associations of Id2 with chemical compounds

• The DNA methyltransferase inhibitor 5-azacytidine specifically alters the expression of helix-loop-helix proteins Id1, Id2 and Id3 during neuronal differentiation [13].

Physical interactions of Id2

• The time course of c-myc binding to the Id2 promoter, as determined by ChIP assays is compatible with a role of the oncoprotein as a transcriptional inducer of Id2 in liver regeneration [10].

Regulatory relationships of Id2

• On differentiation, Rcho-1 cells downregulated Id2 and upregulated Csh1, a marker of the trophoblast giant cell lineage [2].

Other interactions of Id2

• This study tested the hypothesis that inhibitor of differentiation-2 (Id2), p53, and heat shock proteins (HSP) are responsive to suspension-induced muscle atrophy [1].
• In contrast to Id1 and Id2, which do not form homodimers, the carboxyl-terminal sequence of this alternatively spliced Id1 transcript, termed Id1.25, permits homodimerization [14].
• In this case, the pattern of Id2 presence in the c-myc promoter parallels that found in regenerating liver [10].

Analytical, diagnostic and therapeutic context of Id2

• Although we did not find a difference in the inhibitor of DNA binding/differentiation-2 (Id2) and c-Myc protein contents between the denervated and control muscles, the protein content of tumour suppressor p53 was significantly increased in both the nuclear and the cytosolic fractions with denervation [15].
• Id2 increases in liver regeneration after partial hepatectomy, following the early induction of its gene [10].
• Immunohistochemical analysis shows that Id2 also increases in proliferating hepatocytes after bile duct ligation [10].
• Co-immunoprecipitation shows that Id2 forms a complex with E2F4, p130 and mSin3A in quiescent liver and all these components are present at the c-myc promoter as shown using ChIP (chromatin immunoprecipitation) [10].

References