CBR1

Case study 1: Quinn A Best, 2016

Quinoneoxidoreductase isozyme-1 within human cells, based on results from an investigation of the stability of various rhodamines and seminaphthorhodamines toward the biological reductant NADH, present at ~100-200 μM within cells. While rhodamines are generally known for their chemical stability, the researchers observe that NADH causes significant and sometimes rapid modification of numerous rhodamine analogues, including those oftentimes used in imaging applications. A relationship between the structural features of the rhodamines and their reactivity with NADH is observed. Rhodamines with increased alkylation on the N3- and N6-nitrogens, as well as the xanthene core, react the least with NADH; whereas, nonalkylated variants or analogues with electron-withdrawing substituents have the fastest rates of reaction. These outcomes allowed us to judiciously construct a seminaphthorhodamine-based, turn-on fluorescent probe that is capable of selectively detecting the cancer-associated, NADH-dependent enzyme.

Fig1. Activation of 5 μM probe by hNQO1, in contrast to a lack thereof by other reductase enzymes (human).

Fig2. Inhibition of potential NQO2 and CBR1 probe activation in hNQO1-positive Cells.

Case study 2: Miyong Yun, 2018

Human carbonyl reductase 1 (CBR1) plays major roles in protecting cells against cellular damage resulting from oxidative stress. Although CBR1-mediated detoxification of oxidative materials increased by stressful conditions including hypoxia, neuronal degenerative disorders, and other circumstances generating reactive oxide is well documented, the role of CBR1 under ionising radiation (IR) is still unclear.

The formalin-fixed and paraffin-embedded tissues of 85 patients with head and neck squamous cell carcinoma (HNSCC) were used to determine if CBR1 expression effects on survival of patients with treatment of radiotherapy. Subsequently colony formation assays and xenograft tumor mouse model was used to verify the relationship between CBR1 expression and radiosensitivity in HNSCC cells. To verify CBR1-mediated molecular signalling pathways, cell survival, DNA damage/repair, reactive oxygen species (ROS), cell cycle distribution and mitotic catastrophe in HNSCC cells with modulated CBR1 expression by knockdown or overexpression were measured using by colony formation assays, flow cytometry, qRT-PCR and western blot analysis. CBR1 has a key role in DNA damage response through regulation of IR-mediated ROS generation. Consistently, CBR1 expression is highly correlated with patient survival after and susceptibility to radiation therapy.

Fig3. CBR1 protein expression was evaluated in FaDu and YD38 cells transfected with Mock and CBR1/WT vectors.

Fig4. CBR1 expression by western blot analysis 24 h after IR from 0 to 6 Gy in HNSCC cells (FaDu, YD10B, SNU-1041, YD8). α-tubulin was used as an internal loading control.

Fig1. When there is no substrate binding to CBR1, GSH protects the active site and NADPH from attacks of oxidative small molecules. (Sophia M Shi, 2017)

Fig2. A working model illustrating the effect of maternal VDD on MetS in their offspring. (Jianqiong Zheng, 2020)

CBR1 involved in several pathways and played different roles in them. We selected most pathways CBR1 participated on our site, such as Arachidonic acid metabolism, Metabolism of xenobiotics by cytochrome P, Metabolic pathways, which may be useful for your reference. Also, other proteins which involved in the same pathway with CBR1 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

CBR1 has several biochemical functions, for example, 15-hydroxyprostaglandin dehydrogenase (NADP+) activity, carbonyl reductase (NADPH) activity, oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor. Some of the functions are cooperated with other proteins, some of the functions could acted by CBR1 itself. We selected most functions CBR1 had, and list some proteins which have the same functions with CBR1. You can find most of the proteins on our site.

CBR1 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with CBR1 here. Most of them are supplied by our site. Hope this information will be useful for your research of CBR1.

PRKAB1; EIF1B; EPB41; VDAC1; NME2; MCC; HLA-B; HLA-C; EIF6; GABARAPL2; IKBKE; ATG101; DDA1; UBA5; FTSJ1; TNIK; TRAF6; EGFR; ERCC8