PCBP2 Antibody

1. PCBP2 expression was markedly increased in higher stages of glioblastoma compared with those in lower stages; further research suggested that PCBP2 upregulation was connected with poorer prognosis in patients with glioblastoma PMID: 28787701
2. Double immunofluorescence for hnRNP E2 and TDP-43 showed most TDP-43 immunopositive dystrophic neuritis within frontal and temporal cortex, and the neuronal cytoplasmic inclusions seen in dentate gyrus granule cells, to contain hnRNP E2. Present findings indicate an association between TDP-43 and hnRNP E2 which might underlie the pathogenetic mechanism of Semantic Dementia Frontotemporal Lobar Degeneration. PMID: 28666471
3. Data suggest that the interaction between PCBP2 and the 3'UTR of the ARHGDIA mRNA may induce a local change in RNA structure that favors subsequent binding of miR-151-5p and miR-16, thus leading to the suppression of ARHGDIA expression. PMID: 26761212
4. To promote intracellular iron flux, an iron chaperone appears to be essential for receiving iron from heme catabolism. Data suggest that PCBP2 competes with CPR for binding HO1; PCBP2 K homology 3 domain is important for HO1/PCBP2 interaction; heme prompts HO1/CPR multimer and decreases HO1/PCBP2 multimer. [PCBP2 = poly(rC) binding protein 2; CPR = cytochrome P450 reductase; HO1 = heme oxidase 1] PMID: 28655775
5. Study determined that PCBP2 specifically associates with components of this kinase cascade and regulates the activities of its downstream transcriptional coactivators. PMID: 27215387
6. These results suggest that FPN1 exports iron received from the iron chaperone PCBP2. Therefore, it was found that PCBP2 modulates cellular iron export, which is an important physiological process. PMID: 27302059
7. PCBP2 was overexpressed in esophageal squamous cell carcinoma tissues and cell lines. PCBP2 expression promoted proliferation of ESCC cells. We also found that reduced PCBP2 expression might induce ESCC cell apoptosis with increased cleaved caspase3 expression. Overall, our findings indicated that PCBP2 might be involved in the ESCC progression and be considered as a new treatment target in ESCC. PMID: 27461833
8. High expression of PCBP2 may contribute to sorafenib resistance in hepatocellular carcinoma cells. PMID: 27748915
9. our data indicate that miR-214 may function as tumor suppressor in glioma by targeting PCBP2 PMID: 26722446
10. PCBP2 knockdown promoted angiotensin II-induced hypertrophy (increase in cell size, protein synthesis and activation of fetal genes) of cardiomyocytes, while PCBP2 overexpression obtained oppose effects. PMID: 26116532
11. Protein and mRNA levels of PCBP2 were down-regulated under insulin-resistant conditions. Over-expression of PCBP2 inhibits HIF1alpha and STAT3 pathway. PMID: 26002461
12. STAT3 functions via cellular PCBP2 to regulate B-cell lytic susceptibility by restraining Epstein-Barr Virus lytic activation. PMID: 25717101
13. PCBP2-depletion induces apoptosis in gastric cancer cells via up-regulating expression of pro-apoptotic proteins and down-regulating anti-apoptotic proteins. miR-34a is a target of PCBP2, and miR-34a is critically essential for the function of PCBP2. PMID: 24796666
14. SIRT6 inhibits glioma cell proliferation and colony formation in vitro and glioma cell growth in vivo in a PCBP2 dependent manner. SIRT6 inhibits PCBP2 expression through deacetylating H3K9ac and SIRT6 acts as a tumor suppressor in glioma. PMID: 24607900
15. Inhibition of poliovirus-induced cleavage of cellular PCBP2 protein reduces the viral RNA replication. PMID: 24371074
16. PCBP2 and PTB are differentially cleaved by human rhinovirus proteinase in infected cells. PMID: 24418535
17. PCBP2 controls the 3' processing of its own transcript. PMID: 23629627
18. PCBP2 is an RNA-binding protein that modulates glioma growth by regulating FHL3 PMID: 23585479
19. Cytosolic iron may modulate the association between PCBP2 and Dicer, as well as the multimerization of PCBP2 and its ability to bind to miRNA precursors PMID: 22633452
20. PCBP2 specifically and selectively interacts with rabies virus glycoprotein mRNA and this interaction may contribute to the post-transcriptional regulation of glycoprotein expression PMID: 22438951
21. PCBP2 stabilizes the mRNA of STAT1 and STAT2 through binding the 3'Untranslated Region (UTR) of these two molecules. PMID: 22022391
22. SRp75 inhibits splicing of tau exon 10 by binding to the CA repeat in the intronic splicing silencer downstream of the exon, and requires hnRNPG to exert its full regulatory effect on tau exon 10. PMID: 21723381
23. study demonstrates the mechanism of the participation of PCBP2 in hepatitis C virus translation and replication PMID: 21632751
24. Study reports that loss of miR-328 occurs in blast crisis chronic myelogenous leukemia (CML-BC) in a BCR/ABL dose- and kinase-dependent manner through the MAPK-hnRNP E2 pathway. PMID: 20211135
25. The authors established that the 5'CL-PCBP complex is required for optimal poliovirus viral RNA translation and identified the KH3 domain of PCBP2 as the functional region. PMID: 19945132
26. specific PCBP2 domains may have distinct roles for differential picornavirus template utilization during viral translation and RNA replication PMID: 12414943
27. Data suggest that poly(C)-binding protein 2 KH domain 1 interactions with telomeric DNA and telomerase RNA may be involved in the regulation of telomere/telomerase functions. PMID: 15331611
28. PCBP2 KH1 binds to C-rich strand of human telomeric DNA, indicating that that PCBPs may participate in mechanisms involved in the regulation of telomere/telomerase functions PMID: 16186123
29. 2',5'-oligoadenylate synthetase activation may occur in prostate cancer cells stimulated by cellular mRNAs for PCBP2. PMID: 17145707
30. Downregulation of HnRNP E2 is associated with oral cancer PMID: 17219427
31. molecular model of the interaction of the third KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA. PMID: 17426136
32. Crystal structures of PCBP2 KH1 domain in complex with a 12-nucleotide DNA corresponding to two repeats of the human C-rich strand telomeric DNA and its RNA equivalent. PMID: 17526645
33. Study shows that through the loss of the KH3 domain, and therefore loss of its ability to function in translation, PCBP2 can mediate the switch from viral translation to RNA replication. PMID: 17581994
34. The interaction of PCBP2 with RNA target sequences at the 5' end of the coxsackievirus B3 genome was investigated. PMID: 18086560
35. PCBP2 may be involved in stress-induced remodeling of mRNP complexes and that it may also play a role in the rapid transition of certain silenced mRNAs into a translationally active state. PMID: 18174314
36. Using a novel protein-RNA tethering system, We establish PCBP2 as an essential co-factor in the initiation of poliovirus negative-strand synthesis. PMID: 18252259
37. The authors showed that the PCBP2 linker domain modulates binding to poliovirus stem-loop IV RNA via a mechanism that is not inhibited by the antibody. PMID: 18656221
38. SIN1 and PCBP2 are generally coregulated with large numbers of genes implicated in both cell survival and death and in cellular stress responses, including RNA translation and processing PMID: 18687895
39. analysis of the human poly(C)-binding protein containing the first and second KH domains reveals insights into its regulatory mechanisms PMID: 18701464
40. The data demonstrate interaction of isolated PCBP2 KH1 and KH3 domains to four distinct target sites within the 5'-nontranslated region of the CVB3 genomic RNA. PMID: 18929541
41. Results establish the compositional diversity among P-bodies, and that PCBP2, probably in complex with other mRNP factors, may dynamically recognize such differences and accumulate to specific P-bodies. PMID: 19230839
42. PCBP2-AIP4 axis defines a new signaling cascade for MAVS degradation and 'fine tuning' of antiviral innate immunity. PMID: 19881509
43. validated occurrence of an unusual TG 3' splice site in intron 7 PMID: 17672918

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HGNC: 8648

OMIM: 601210

KEGG: hsa:5094

STRING: 9606.ENSP00000352438

UniGene: Hs.546271