1. The relative increase in ORP150 mRNA observed in hypoxia, compared with normoxia, may support its cytoprotective role in oxygendeprived conditions PMID: 27748851
2. Here we show that Grp170 can bind directly to a variety of incompletely folded protein substrates in the endoplasmic reticulum, and as expected for a bona fide chaperone, it does not interact with folded secretory proteins. PMID: 24327659
3. These results suggest that although ORP150 is protective against bleomycin-induced lung injury, this protein could stimulate bleomycin-induced pulmonary fibrosis by increasing pulmonary levels of TGF-beta1 and myofibroblasts. PMID: 22892132
4. Results reveal a previously unrecognized attribute of Grp170 as a superior DNA-binding chaperone capable of amplifying TLR9 activation on pathogen recognition. PMID: 22207611
5. AICAR infusion enhanced ORP150 expression, resulting in the marked amelioration of hepatic ER stress and apoptosis PMID: 21296878
6. Secreted grp170 can bind to and co-transport out of tumour cells a full length tumour antigen that may play a role in the anti-tumour immune response. PMID: 20210603
7. Grp170 displays multiple peptide binding domains; the presence of two strong peptide binding regions in such a large protein may facilitate the interactions and assembly of two substate proteins. PMID: 14674765
8. demonstrated that expression of ORP150 in developing brain most likely serves a cytoprotective function in Purkinje cells PMID: 14960622
9. The 150-kDa oxygen-regulated protein may be cytoprotective against ischemia/reperfusion injury via reduction of endoplasmic reticulum stress and probably also inhibition of apoptosis. PMID: 15223375
10. ORP150 exerts cytoprotective effects in renal tubular epithelia subjected to I/R injury and suggest a key role for ER stress in the renal tubular response to acute renal failure PMID: 15240565
11. Systemic expression of ORP150 in Akita mice improves insulin intolerance, whereas the exclusive overexpression of ORP150 in pancreatic beta-cells of Akita mice did not change their glucose tolerance. PMID: 15734840
12. involvement of ORP150 in insulin secretion in MIN6 cells PMID: 15841037
13. molecular chaperoning is involved in stress protein interactions with APCs, antigen binding, and in eliciting antitumor immunity, thus bridging this ancient function of stress proteins in prokaryotes to their ability to elicit immunity in higher organisms PMID: 16424054
14. Grp170 depleted of endoplasmic reticulum retention sequence "KNDEL," when secreted by B16 melanoma cells, maintains its highly efficient chaperoning activities and is significantly superior to both hsp70 and gp96. PMID: 16849461
15. Our observations led to the hypothesis that ORP150 protects against MPTP/MPP(+)-induced neurotoxicity, and indicate the importance of the ER environment in maintaining the nigrostriatal pathways. PMID: 17330988
16. Overexpression of ORP150 in mice leads to abetalipoproteinemia with alteration of glucose and lipid metabolism. PMID: 17605339
17. These findings suggest that overexpression of ORP150 causes accumulation of ORP150 in the rough-surfaced endoplasmic reticula, resulting in vacuolar degeneration in the skeletal muscle of ORP-Tg mice. PMID: 18250584
18. Grp170 enhances therapeutic activity of a novel tumor suppressor, mda-7/IL-24 PMID: 18483274
19. grp170 elicits systemic tumor immunity and may be used to improve treatment outcomes for prostate cancer. PMID: 19142636

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KEGG: mmu:12282

STRING: 10090.ENSMUSP00000068594

UniGene: Mm.116721