全部 标题 作者
关键词 摘要

OALib Journal期刊
ISSN: 2333-9721
费用:99美元

查看量下载量

相关文章

更多...

Poly (C)-Binding Protein 1: A Novel Function Attributed to the Nervous System Microenvironment

DOI: 10.4236/wjns.2021.111006, PP. 48-66

Keywords: PCBP1, Neurological Disorders, Inflammatory, Proliferation, Apoptotic

Full-Text   Cite this paper   Add to My Lib

Abstract:

Poly (C)-binding protein 1 (PCBP1), which acts as an RNA binding protein, has multiple functions and regulates gene expression by binding to polycytosine, poly (C). The aim of the present study was to investigate the novel function of PCBP1 in the nervous system microenvironmen. The overexpression of PCBP1 has a critical effect on the proliferation and anti-apoptosis of neuroblastoma and glial cells in the direct model, whereas the overexpression of PCBP1 in neuroblastoma or glial cells cannot affect the proliferation or apoptosis of neuroblastoma or glial cells through substances secreted extracellularly. Fur-thermore, through direct or indirect actions, PCBP1 suppressed the expression of nuclear factor kappa B (NF-κB) and the inflammatory cytokine interleukin (IL)-6 and increased the levels of the anti-inflammatory cytokine IL-10; addi-tionally, PCBP1 changed the expression of functional proteins, such as heat shock protein 70 (HSP70), glial cell line-derived neurotrophic factor (GDNF) and brain-derived neurotrophic factor (BDNF). The results suggest that PCBP1 can regulate the nervous system in proliferation, apoptosis, inflammatory re-sponse and expression of relevant functional proteins, and it could provide novel targets for gene treating human neurological disorders.

References

[1]  Makeyev, A.V. and Liebhaber, S.A. (2002) The Poly (C)-Binding Proteins: A Multiplicity of Functions and a Search for Mechanisms. RNA, 8, 265-278.
https://doi.org/10.1017/S1355838202024627
[2]  Ren, C., Cho, S.J., Jung, Y.S. and Chen, X. (2014) DNA Polymerase η Is Regulated by Poly (rC)-Binding Protein 1 via mRNA Stability. Biochemical Journal, 464, 377-386.
https://doi.org/10.1042/BJ20141164
[3]  Makeyev, A.V. and Liebhaber, S.A. (2000) Identification of Two Novel Mammalian Genes Establishes a Subfamily of KH-Domain RNA-Binding Proteins. Genomics, 67, 301-316.
https://doi.org/10.1006/geno.2000.6244
[4]  Choi, H.S., Hwang, C.K., Song, K.Y., Law, P.-Y., Wei, L.-N. and Loh, H.H. (2009) Poly (C)-Binding Proteins as Transcriptional Regulators of Gene Expression. Biochemical and Biophysical Research Communications, 380, 431-436.
https://doi.org/10.1016/j.bbrc.2009.01.136
[5]  Ji, X., Wan, J., Vishnu, M., Xing, Y. and Liebhaber, S.A. (2013) αCP Poly (C) Binding Proteins Act as Global Regulators of Alternative Polyadenylation. Molecular and Cellular Biology, 33, 2560-2573.
https://doi.org/10.1128/MCB.01380-12
[6]  Chaudhury, A., Chander, P. and Howe, P.H. (2010) Heterogeneous Nuclear Ribonucleoproteins (hnRNPs) in Cellular Processes: Focus on hnRNP E1’s Multifunctional Regulatory Roles. RNA, 16, 1449-1462.
https://doi.org/10.1261/rna.2254110
[7]  Ostareck-Lederer, A., Ostareck, D.H. and Hentze, M.W. (1998) Cytoplasmic Regulatory Functions of the KH-Domain Proteins hnRNPs K and E1/E2. Trends in Biochemical, 23, 409-411.
https://doi.org/10.1016/S0968-0004(98)01301-2
[8]  Waggoner, S.A., Johannes, G.J. and Liebhaber, S.A. (2009) Depletion of the Poly (C)-Binding Proteins alphaCP1 and alphaCP2 from K562 Cells Leads to p53-Indepen- dent Induction of Cyclin-Dependent Kinase Inhibitor (CDKN1A) and G1 Arrest. Journal of Biological Chemistry, 284, 9039-9049.
https://doi.org/10.1074/jbc.M806986200
[9]  Ostareck-Lederer, A. and Ostareck, D.H. (2004) Control of mRNA Translation and Stability in Haematopoietic Cells: The Function of hnRNPs K and E1/E2. Biology of the Cell, 96, 407-411.
https://doi.org/10.1016/j.biolcel.2004.03.010
[10]  Zhang, T., Huang, X.H., Dong, L., Hu, D.Q., Ge, C.H., Zhan, Y.-Q., et al. (2010) PCBP-1 Regulates Alternative Splicing of the CD44 Gene and Inhibits Invasion in Human Hepatoma Cell Line HepG2 Cells. Molecular Cancer, 9, Article No. 72.
https://doi.org/10.1186/1476-4598-9-72
[11]  Liu, Y., Gai, L., Liu, J., Cui, Y., Cui, Y., Zhang, Y. and Feng, J. (2015) Expression of Poly (C)-Binding Protein 1 (PCBP1) in NSCLC as a Negative Regulator of EMT and Its Clinical Value. International Journal of Clinical and Experimental Pathology, 8, 7165-7172.
[12]  Zhang, M.P., Zhang, W.S., Tan, J., Zhao, M.-H., Lian, L.-J. and Cai, J. (2017) Poly r (C) Binding Protein (PCBP)1 Expression Is Regulated by the E3 Ligase UBE4A in Thyroid Carcinoma. Bioscience Reports, 37, 708-725.
https://doi.org/10.1042/BSR20170114
[13]  Chen, Q., Cai, Z.K., Chen, Y.B., Zheng, D., Zhou, J. and Wang, Z. (2015) Poly r (C) Binding Protein-1 Is Central to Maintenance of Cancer Stem Cells in Prostate Cancer Cells. Cellular Physiology and Biochemistry, 35, 1052-1061.
https://doi.org/10.1159/000373931
[14]  Shi, H., Bencze, K.Z., Stemmler, T.L. and Philpott, C.C. (2008) A Cytosolic Iron Chaperone That Delivers Iron to Ferritin. Science, 320, 1207-1210.
https://doi.org/10.1126/science.1157643
[15]  Nandal, A., Ruiz, J.C., Subramanian, P., Sinnamon, R.A., Stemmler, T.L., Bruick, R.K., et al. (2011) Activation of the HIF Prolyl Hydroxylase by the Iron Chaperones PCBP1 and PCBP2. Cell Metabolism, 14, 647-657.
https://doi.org/10.1016/j.cmet.2011.08.015
[16]  Frey, A.G., Nandal, A., Park, J.H., Smith, P.M., Yabe, T., Ryu, M.-S., et al. (2014) Iron Chaperones PCBP1 and PCBP2 Mediate the Metallation of the Dinuclear Iron Enzyme Deoxyhypusine Hydroxylase. Proceedings of the National Academy of Sciences of the United States of America, 111, 8031-8036.
https://doi.org/10.1073/pnas.1402732111
[17]  Dinh, P.X., Beura, L.K., Panda, D., Das, A. and Pattnaik, A.K. (2011) Antagonistic Effects of Cellular Poly (C) Binding Proteins on Vesicular Stomatitis Virus Gene Expression. Journal of Virology, 85, 9459-9471.
https://doi.org/10.1128/JVI.05179-11
[18]  Makarov, S.S. (2000) NF-kappaB as a Therapeutic Target in Chronic Inflammation: Recent Advances. Trend in Molecular Medicine, 6, 441-448.
https://doi.org/10.1016/S1357-4310(00)01814-1
[19]  Mattson, M.P. and Camandola, S. (2001) NF-kappaB in Neuronal Plasticity and Neurodegenerative Disorders. The Journal of Clinical Investigation, 107, 247-254.
https://doi.org/10.1172/JCI11916
[20]  Hunot, S., Brugg, B., Ricard, D., Michel, P.P., Muriel, M.-P., Ruberg, M., et al. (1997) Nuclear Translocation of NF-kappaB Is Increased in Dopaminergic Neurons of Patients with Parkinson Disease. Proceedings of the National Academy of Sciences of the United States of America, 94, 7531-7536.
https://doi.org/10.1073/pnas.94.14.7531
[21]  Nishinakamura, H., Minoda, Y., Saeki, K., Koga, K., Takaesu, G., Onodera, M., et al. (2007) An RNA-Binding Protein alphaCP-1 Is Involved in the STAT3-Mediated Suppression of NF-kappaB Transcriptional Activity. International Immunology, 19, 609-619.
https://doi.org/10.1093/intimm/dxm026
[22]  Zhong, N., Radu, G., Ju, W. and Ted Brown, W. (2005) Novel Progerin-Interactive Partner Proteins hnRNP E1, EGF, Mel 18, and UBC9 Interact with Lamin A/C. Biochemical and Biophysical Research Communications, 338, 855-861.
https://doi.org/10.1016/j.bbrc.2005.10.020
[23]  Geuens, T., De Winter, V., Rajan, N., Achsel, T., Mateiu, L., Almeida-Souza, L., et al. (2017) Mutant HSPB1 Causes Loss of Translational Repression by Binding to PCBP1, an RNA Binding Protein with a Possible Role in Neurodegenerative Disease. Acta Neuropathologica Communications, 5, Article No. 5.
https://doi.org/10.1186/s40478-016-0407-3
[24]  Huo, L.R., Ju, W., Yan, M., Zou, J.-H., Yan, W., He, B., et al. (2010) Identification of Differentially Expressed Transcripts and Translatants Targeted by Knock-Down of Endogenous PCBP1. Biochimica et Biophysica Acta (BBA)—Proteins and Proteomics, 1804, 1954-1964.
https://doi.org/10.1016/j.bbapap.2010.07.002
[25]  Giles, K.M., Daly, J.M., Beveridge, D.J., Thomson, A.M., Voon, D.C., Furneaux, H.M., et al. (2003) The 3’-Untranslated Region of p21WAF1 mRNA Is a Composite Cis-Acting Sequence Bound by RNA-Binding Proteins from Breast Cancer Cells, Including HuR and Poly (C)-Binding Protein. Journal of Biological Chemistry, 278, 2937-2946.
https://doi.org/10.1074/jbc.M208439200
[26]  Wang, H., Vardy, L.A., Tan, C.P., Loo, J.M., Guo, K., Li, J., et al. (2010) PCBP1 Suppresses the Translation of Metastasis-Associated PRL-3 Phosphatase. Cancer Cell, 18, 52-62.
https://doi.org/10.1016/j.ccr.2010.04.028
[27]  Leidgens, S., Bullough, K.Z., Shi, H., Li, F.M., Shakoury-Elizeh, M., Yabe, T., et al. (2013) Each Member of the Poly-r (C)-Binding Protein 1 (PCBP) Family Exhibits Iron Chaperone Activity toward Ferritin. Journal of Biological Chemistry, 288, 17791-17802.
https://doi.org/10.1074/jbc.M113.460253
[28]  Zhou, X., You, F., Chen, H. and Jiang, Z. (2012) Poly (C)-Binding Protein 1 (PCBP1) Mediates Housekeeping Degradation of Mitochondrial Antiviral Signaling (MAVS). Cell Research, 22, 717-727.
https://doi.org/10.1038/cr.2011.184
[29]  Thyagarajan, A. and Szaro, B.G. (2004) Phylogenetically Conserved Binding of Specific K Homology Domain Proteins to the 3’-Untranslated Region of the Vertebrate Middle Neurofilament mRNA. Journal of Biological Chemistry, 279, 49680-49688.
https://doi.org/10.1074/jbc.M408915200
[30]  Thyagarajan, A. and Szaro, B.G. (2008) Dynamic Endogenous Association of Neurofilament mRNAs with K-Homology Domain Ribonucleoproteins in Developing Cerebral Cortex. Brain Research, 1189, 33-42.
https://doi.org/10.1016/j.brainres.2007.11.012
[31]  Shi, H., Li, H., Yuan, R., Guan, W., Zhang, X.M., Zhang, S.Y., et al. (2018) PCBP1 Depletion Promotes Tumorigenesis through Attenuation of p27Kip1 mRNA Stability and Translation. Journal of Experimental & Clinical Cancer Research, 37, Article No. 187.
https://doi.org/10.1186/s13046-018-0840-1
[32]  Huo, L.R. and Zhong, N. (2008) Identification of Transcripts and Translatants Targeted by Overexpressed PCBP1. Biochimica et Biophysica Acta (BBA)—Proteins and Proteomics, 1784, 1524-1533.
https://doi.org/10.1016/j.bbapap.2008.06.017
[33]  Lin, L.F., Doherty, D.H., Lile, J.D., Bektesh, S. and Collins, F. (1993) GDNF: A Glial Cell Line-Derived Neurotrophic Factor for Midbrain Dopaminergic Neurons. Science, 260, 1130-1132.
https://doi.org/10.1126/science.8493557
[34]  Park, H. and Poo, M.M. (2013) Neurotrophin Regulation of Neural Circuit Development and Function. Nature Reviews Neuroscience, 14, 7-23.
https://doi.org/10.1038/nrn3379
[35]  Kang, S.M., More, S.V., Park, J.Y., Kim, B.-W., Park, J.I. and Yoon, S.-H. (2014) A Novel Synthetic HTB Derivative, BECT Inhibits Lipopolysaccharide-Mediated Inflammatory Response by Suppressing the p38 MAPK/JNK and NF-κB Activation Pathways. Pharmacological Reports, 66, 471-479.
https://doi.org/10.1016/j.pharep.2013.08.015
[36]  Lynch, G., Kramar, E.A., Rex, C.S., Jia, Y.S., Chappas, D., Gall, C.M., et al. (2007) Brain-Derived Neurotrophic Factor Restores Synaptic Plasticity in a Knock-in Mouse Model of Huntington’s Disease. Journal of Neuroscience, 27, 4424-4434.
https://doi.org/10.1523/JNEUROSCI.5113-06.2007
[37]  Brito, V., Giralt, A., Enriquez-Barreto, L., Puigdellívol, M., Puigdellívol, M., Suelves, N., Zamora-Moratalla, A., et al. (2014) Neurotrophin Receptor p75 (NTR) Mediates Huntington’s Disease-Associated Synaptic and Memory Dysfunction. Journal of Clinical Investigation, 124, 4411-4428.
https://doi.org/10.1172/JCI74809
[38]  Mishchenko, T.A., Mitroshina, E.V., Shishkina, T.V. and Vedunova, M.B. (2018) Antioxidant Properties of Glial Cell-Derived Neurotrophic Factor (GDNF). Bulletin of Experimental Biology and Medicine, 166, 293-296.
https://doi.org/10.1007/s10517-018-4335-z
[39]  Saraiva, M. and O’Garra, A. (2010) The Regulation of IL-10 Production by Immune Cells. Nature Reviews Immunology, 10, 170-181.
https://doi.org/10.1038/nri2711
[40]  de Oca, M.M., Kumar, R., de Labastida Rivera, F., et al. (2016) Blimp-1-Dependent IL-10 Production by Tr1 Cells Regulates TNF-Mediated Tissue Pathology. PLoS Pathog, 12, e1005398.
https://doi.org/10.1371/journal.ppat.1005460
[41]  Rajasingh, J., Bord, E., Luedemann, C., Asai, J., Hamada, H., Thorne, T., et al. (2006) IL-10-Induced TNF-alpha mRNA Destabilization is Mediated via IL-10 Suppression of p38 MAP Kinase Activation and Inhibition of HuR Expression. The FASEB Journal, 20, 2112-2114.
https://doi.org/10.1096/fj.06-6084fje
[42]  Williams, L., Bradley, L., Smith, A. and Foxwell, B. (2004) Signal Transducer and Activator of Transcription 3 Is the Dominant Mediator of the Anti-Inflammatory Effects of IL-10 in Human Macrophages. The Journal of Immunology, 172, 567-576.
https://doi.org/10.4049/jimmunol.172.1.567
[43]  Lin, Y.C., Uang, H.W., Lin, R.J., Chen, I.-J. and Lo, Y.-C. (2007) Neuroprotective Effects of Glyceryl Nonivamide against Microglia-Like Cells and 6-Hydroxydopa- mine-Induced Neurotoxicity in SH-SY5Y Human Dopaminergic Neuroblastoma Cells. Journal of Pharmacology and Experimental Therapeutics, 323, 877-887.
https://doi.org/10.1124/jpet.107.125955

Full-Text

comments powered by Disqus

Contact Us

service@oalib.com

QQ:3279437679

WhatsApp +8615387084133

WeChat 1538708413