Disease relevance of ARL6IP5

• For the notable performance achieved by ATRA in the differentiation induction therapy, we investigated the role of JWA in the induction of differentiation of human myeloid leukemia cells [1].

High impact information on ARL6IP5

• Moreover, the introduction of a di-acidic motif to the COOH-terminal domain of PRA2 resulted in partial localization to the Golgi complex [2].
• The two PRA isoforms showed distinct intracellular localization with PRA1 localized primarily to the Golgi complex and PRA2 to the endoplasmic reticulum (ER) compartment [2].
• Using phytochrome-deficient mutants, we showed that the pra2 protein level in seedlings was also regulated by these photoreceptors [3].
• Using this construct in a transient assay, we determined a pra2 cis-regulatory region sufficient to direct the light down-regulation of the luciferase reporter gene [4].
• Furthermore, JM4, JWA, and GTRAP3-18 co-localise and heterodimerise indicating a functional relationship [5].

Chemical compound and disease context of ARL6IP5

• Our results showed that JWA was not only regulated by ATRA but also by several other differentiation inducers such as phorbol-12-myristate-13-acetate (TPA), arabinoside (Ara-C), and hemin, involved in the mechanisms of differentiation along different lineages of myeloid leukemia cells arrested at different stages of development [1].

Biological context of ARL6IP5

• Inhibition of JWA by RNA interference decreased the induced cellular differentiation [1].
• Our recent data showed that JWA, initially being cloned as a novel cell differentiation-associated gene, was also actively responsive to environmental stressors, such as heat-shock, oxidative stress and so on [6].
• In the present study, we have applied a modified comet assay and bacterial repair endonucleases system (endonuclease III and formamidopyrimidine glycosylase) to investigate if JWA is involved in hydrogen peroxide (H2O2)-induced DNA damage and repair in K562 and MCF-7 cells, and to demonstrate if the damage is associated with 8-oxo-dG [6].
• In addition, the data have clearly demonstrated that JWA gene expression is actively induced by H2O2 treatment in K562 and MCF-7 cells [6].
• 5. These data indicate that the inhibition of proliferation and the induction of apoptosis by ATRA are dependent on JWA expression in HeLa cells [7].

Anatomical context of ARL6IP5

• JM4 and GTRAP3-18 harbor a Rab-acceptor motif, indicating a function in vesicle formation at the Golgi complex [5].
• JWA (AF070523) is a novel all-trans retinoic acid (ATRA) responsible gene that initially isolated from ATRA-treated primary human tracheal bronchial epithelial cells [1].
• In NB4 cells, JWA may function as a lineage-restricted gene during differentiation along the monocyte/macrophage-like or granulocytic pathway [1].
• In JWA-overexpressing HeLa cells, ATRA showed more significant antiproliferative effects and induced more apoptosis [7].
• JWA may be a novel molecular marker for ATRA-induced HL-60 cell differentiation [8].

Associations of ARL6IP5 with chemical compounds

• PRA2 was found to form a large sodium dodecyl sulfate (SDS)-insoluble complex upon heat denaturation, resulting in significant reduction in the Western immunoblot signal [9].
• In this study, the potential role of JWA was further investigated in hydrogen peroxide (H2O2) induced DNA damage and cell apoptosis in K562 cells [10].
• In the present study, the influence of both fenvalerate and phoxim was examined on the expression of JWA in MCF-7 (ER+) and MDA-MB-231 (ER-) human breast carcinoma cell lines [11].
• In both H and N furosemide caused a significant rise of PRA1 (p less than 0.001 in H and p less than 0.01 in N) and PRA2 (p less than 0.001 in H and p less than 0.05 in N) [12].

Analytical, diagnostic and therapeutic context of ARL6IP5

• The changes in the immunoblotting pattern of the pra2 protein in these mutants were correlated with the changes in epicotyl elongation [3].
• Northern blot analysis showed mRNA corresponding to hp22 to be expressed in all tissues examined [13].
• We also found that protein interaction with PRA2 is highly sensitive to detergent and describe a covalent cross-linking procedure for mammalian cell extracts to stabilize the PRA2-containing complex prior to membrane solubilization and immunoprecipitation [9].

References