Poly(rC) Binding Protein 1 (PCBP1) ELISA Kits

Human Poly(rC) Binding Protein 1 (PCBP1) interaction partners

1. Knockdown of PCBP1 promoted both tumorigenesis and metastatic progression in prostate cancer, suggestive of PCBP1 functioning as a tumor suppressor in normal prostate epithelial cells and potentiates tumor formation by up-regulation of MAPK1 expression.

2. PCBP1 binds to more severely oxidized RNA to activate apoptosis-related reactions. PCBP1 does not bind to such oligoribonucleotides but instead binds firmly to oligoribonucleotides in which two 8-oxoG residues are located nearby. The structure-function relationship of PCBP1 was established with the use of PCBP1 mutant proteins with defective conserved KH domains. PCBP1 operates when RNA is more severely damaged.

3. High HNRPE1 expression is associated with pancreatic cancer metastasis.

4. UBE4A targets PCBP1 for proteasomal degradation and that UBE4A expression can serve as a novel biomarker in thyroid cancer patients.

5. Study report a novel interaction between mutant HSPB1-P182L and the RNA binding protein PCBP1, leading to a reduction in its translational repression activity. Identifying PCBP1 mRNA targets revealed a marked prevalence for an RNA recognition motif, preferably seen in their 5' and 3'UTRs. Findings further support a role for mutant HSPB1 in neurodegenerative diseases.

6. It is reported here that TGF-beta directly regulates alternative splicing of cancer stem cell marker CD44 through a phosphorylated threonine179 of SMAD3-mediated interaction with RNA-binding protein PCBP1.

7. our findings suggest that PCBP1 is a molecular marker of oxaliplatin resistance in colorectal cancer

8. Data suggest a 216-nucleotide proximal cis-element in LIF mRNA exhibits mRNA destabilizing potential; on exposure to carcinogen PMA (phorbol-12-myristate-13-acetate), this cis-element exhibits mRNA stabilizing activity. PMA induces nucleo-cytoplasmic translocation of both nucleolin and PCBP1, 2 trans-acting factors that bind to and stabilize LIF mRNA. [LIF = leukemia inhibitory factor; PCBP1 = poly(rC) binding protein 1]

9. It was concluded that a novel positive feedback loop amplifies hnRNP-E1 during prolonged folate deficiency and thereby maximizes upregulation of folate receptors in order to restore folate homeostasis toward normalcy in placental cells.

10. TGF-beta signaling through Akt2 induces phosphorylation of heterogeneous nuclear ribonucleoprotein E1 (hnRNP E1) at serine-43 (p-hnRNP E1), driving epithelial to mesenchymal transition and metastasis.

11. These results establish the role of hnRNP K and PCPB1 in the translational control of morphine-induced MOR expression in human neuroblastoma (NMB) cells as well as cells stably expressing MOR (NMB1).

12. The results provide a mechanism for exon 16 3' splice site activation in which a coordinated effort among TIA1, Pcbp1, and RBM39 stabilizes or increases U2 snRNP recruitment, enhances spliceosome A complex formation, and facilitates exon definition through RBM39-mediated splicing regulation.

13. BC200 RNA interacts with hnRNP E1 and E2 mainly through its unique 3' C-rich domain.

14. Low expression of PCBP1 is associated with lung cancer metastasis.

15. We found a C-rich element (CRE) in mu-opioid receptor (MOR) 3'-untranslated region (UTR) to which poly (rC) binding protein 1 (PCBP1) binds, resulting in MOR mRNA stabilization. AUF1 phosphorylation also led to an increased interaction with PCBP1.

16. miR-7977 in extracellular vesicles may be a critical factor that induces failure of normal hematopoiesis via poly(rC) binding protein 1 suppression in myeloid neoplasms.

17. Poly C binding protein 1 represses autophagy through downregulation of LC3B to promote tumor cell apoptosis in starvation

18. Inhibin betaA is translationally regulated by TGFbeta via hnRNP E1.

19. alphaCP1/ alphaCP2 binding to a cytosine-rich subset of polypyrimidine tracts drives a novel pathway of cassette exon splicing in the mammalian transcriptome.

20. Suggest that PCBP1 might play an important role in preventing the process of epithelial mesenchymal transformation in NSCLC.

Mouse (Murine) Poly(rC) Binding Protein 1 (PCBP1) interaction partners

1. Study report a novel interaction between mutant HSPB1-P182L and the RNA binding protein PCBP1, leading to a reduction in its translational repression activity. Identifying PCBP1 mRNA targets revealed a marked prevalence for an RNA recognition motif, preferably seen in their 5' and 3'UTRs. Findings further support a role for mutant HSPB1 in neurodegenerative diseases.

2. These studies demonstrate the importance of ferritin for the vectorial transfer of imported iron to mitochondria in developing red cells and of PCBP1 and NCOA4 in mediating iron flux through ferritin.

3. Pcbp1 modulated the processing of muscle-enriched miR-1, miR-133, and miR-206 by physically interacting with argonaute 2 (AGO2) and other miRNA pathway components.

4. These data reveal that Pcbp1 and Pcbp2 are individually essential for mouse embryonic development and have distinct impacts on embryonic viability and that Pcpb2 has a nonredundant in vivo role in hematopoiesis.

5. PCBP1 may serve as a novel maternal factor.

6. Our analysis of PCBP1 and PCBP2 expression demonstrates robust expression of these two proteins within the gastric epithelium with high concordance for both proteins in their cell-type specificities and intracellular distributions.

7. knockdown of PCBP1 led to a reversal effect on the transcriptional inactivation during oocyte growth, which highlights the important role of PCBP1 in maintaining the gobal transcriptional silencing when the growth phase is completed

8. TGF-beta modulates the expression of Dab2 and ILEI mRNA required for epithelial-mesenchymal transdifferentiation by inducing phosphorylation of hnRNP E1, resulting in its release from a structural, 33-nucleotide BAT element in the 3'UTR of Dab2 and ILEI.

9. To define the mechanism of STAT3C suppression of transcript. and/or translational activity of NF-kappaB we found that a alphaCP-1 interacted with STAT3C. alphaCP-1 is a K-homol. domain-containing RNA-binding prot with specific for C-rich pyrimidine tracts