Disease relevance of Jafrac2

• In contrast, TPx overexpressing cells were more susceptible to copper and heat stress when compared with control cells and exhibited DNA fragmentation [1].

High impact information on Jafrac2

• Mature Jafrac2 interacts genetically and biochemically with DIAP1 and promotes cell death in tissue culture cells and the Drosophila developing eye [2].
• In healthy cells, Jafrac2 resides in the endoplasmic reticulum but is rapidly released into the cytosol following induction of apoptosis [2].
• Like other CysGPxs with thioredoxin peroxidase activity, Drosophila melanogaster (Dm)GPx oxidized by H(2)O(2) contained an intra-molecular disulfide bridge between the active-site cysteine (C45; C(P)) and C91 [3].
• Thioredoxin peroxidases can foster cytoprotection or cell death in response to different stressors: over- and under-expression of thioredoxin peroxidase in Drosophila cells [1].
• Furthermore, when cells were supplemented with N -acetyl-L-cysteine together with copper, there was a clear negative effect on cell survival, which was exacerbated by TPx overexpression [1].

Biological context of Jafrac2

• The other, Jafrac2, encodes a protein of 242 amino acids and mapped in the region 62F in the 3 L chromosome [4].
• The deduced amino acid sequence of the BmTPx cDNA showed 78% identity to Drosophila melanogaster (DmTPx-1), 73% to Aedes aegypti (AaTPx), and 54-48% to other insect 2-Cys TPx [5].

Associations of Jafrac2 with chemical compounds

• A thioredoxin peroxidase (TPx) that reduces H(2)O(2) was firstly characterized in the lepidopteran insect, silkworm Bombyx mori [5].

References