Recombinant Mouse Protein disulfide-isomerase A3 (Pdia3)

1. Role of the ERp57 protein (1,25D3-MARRS receptor) in murine mammary gland growth and development PMID: 29477346
2. PDI knockout inhibits the inflammatory function of macrophages by decreasing ROS production and inactivating NF-kappaB pathway. PMID: 29294242
3. Thiol isomerase ERp57 is mobilized to the surface of activated platelets via a process that requires actin polymerization. PMID: 27079884
4. These data indicate a synergistic crosstalk between 1alpha,25(OH)2D3 and BMP2 toward osteogenesis and mineral deposition, involving both VDR and Pdia3. PMID: 23784946
5. ERp57 deficiency causes neuromuscular defects PMID: 26869642
6. ERp57 levels are increased in the airway epithelium of asthmatic patients and in mice with allergic airways disease. PMID: 26435004
7. Data suggest that regulation of Pdia3 (protein disulfide isomerase associated 3 protein) expression by microRNA-330-5p is important in maintaining hair cycle through regulation of proliferation and migration capability of keratinocytes. PMID: 26402295
8. All the growth plate and bone abnormalities, however, become attenuated after the pubertal growth spurt, when protein synthesis is decelerated and, hence, ERp57 function is less essential. PMID: 25704664
9. ERp57 regulates thrombosis via multiple targets. PMID: 25156521
10. These data suggest the 25D3 -MARRS receptor/PDIA3/ERp57 may contribute to the length of lifespan in mammals. PMID: 25283641
11. Pdia3+/- mice exhibit a mild skeletal phenotype characterized by enlarged growth plates, reduced tether and trabecular bone formation, and impaired osteogenic potential of calvarial osteoblasts in vitro. PMID: 25405762
12. Maternal PDIA3 plays a crucial role in sperm decondensation by reducing protamine disulfide bonds in porcine oocytes, supporting its utility as a potential tool for oocyte selection in assisted reproduction techniques. PMID: 25030891
13. Cell cycle analyses demonstrated that the suppressed expression of ERp57 increased the sub-G1 population. These data reveal that increased expression of ERp57 may contribute to the protection from beta cell death caused by autophagic failure. PMID: 25241190
14. The current study implicates PDIA3 to be an important cellular neuroprotective mechanism against a toxic drug PMID: 22715419
15. Pdia3 co-localizes with vitamin D receptor and caveolin-1 on the surface of MC3T3-E1 osteoblasts. In response to 1alpha,25(OH)2D3, receptors translocate and change interactions. PMID: 23896121
16. These data indicate that both the chaperone functional domains and the subcellular location of Pdia3 control rapid membrane responses to 1alpha,25-dihydroxyvitamin d3. PMID: 23660595
17. Platelets lacking ERp57 have defective activation of the alphaIIbbeta3 integrin and platelet aggregation. The defect in aggregation was corrected by the addition of exogenous ERp57, implicating surface ERp57 in platelet aggregation. PMID: 24030382
18. Knockout of the Pdia3 protein in mice eliminates the rapid response to calcitriol in intestinal epithial cells. PMID: 22546984
19. Phospholipase A2 activating protein is required for 1alpha,25-dihydroxyvitamin D3 dependent rapid activation of protein kinase C via Pdia3 PMID: 22484374
20. ERp57 has roles in multiple components of platelet function and arterial thrombus formation. PMID: 22168334
21. ERp57 is required for platelet aggregation, hemostasis, and thrombosis. PMID: 22207737
22. ERp57, by ER luminal interaction with STIM1, has a modulatory role in capacitative Ca(2+) entry. PMID: 21941299
23. ERp57 participates in signal transduction from the cell surface, in regulatory processes taking place in the nucleus, and in multimeric protein complexes involved in DNA repair. (Review) PMID: 21837552
24. 1,25D(3)-MARRS receptor is of central importance to steroid hormone-stimulated calcium uptake in mammalian intestinal cells. PMID: 20682787
25. Pdia3 plays a crucial role in 1alpha,25(OH)2D3-regulated bone formation and the Pdia3-PKC signalling pathway might be involved in this process PMID: 20576531
26. ERp57 effects on STAT3 signaling are enhanced by ER luminal complex formation between ERp57 and calreticulin PMID: 20022947
27. The thiol oxidoreductase endoplasmic reticulum (ER)p57 interacts with newly synthesized glycoproteins through ternary complexes with the chaperones/lectins calnexin or calreticulin. PMID: 14978212
28. ERp57 plays an important role during the post-translational phases of glycoprotein folding, when the primary requirement for promotion of glycoprotein maturation is an isomerase/reductase activity PMID: 16407314
29. ERp57 is involved in disulfide formation in vivo but not in peptide loading of class I molecules PMID: 16567808
30. Overall, these results suggest that protein folding and other activities mediated through PDI and BiP are diminished during aging. PMID: 17996725
31. the function of ERp57 in peptide loading is likely caused by other ERp57 functional domains or a combinatorial feature of the tapasin-ERp57 conjugate PMID: 18650385
32. ERP57 is a key protein that controls immunogenicity by controlling calreticulin exposure and serves as a molecular marker of immunogenicity. PMID: 18684944
33. ERp57 must be physically associated with the calnexin cycle to catalyze isomerization reactions with most of its substrates PMID: 19054761

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KEGG: mmu:14827

STRING: 10090.ENSMUSP00000028683

UniGene: Mm.263177