INTERPLAY BETWEEN POLYCYSTIN-1 AND EXTRACELLULAR MATRIX: INVESTIGATING THE REJ DOMAIN'S SIGNIFICANCE IN ADPKD PATHOGENESIS
Main Article Content
Keywords
Polycystin-1, Receptor of the egg jelly (REJ) domain, Pull-down technique, MALDI-TOF MS, Extracellular matrix (ECM)
Abstract
Polycystin 1 (PC1) plays a crucial role in the progression of autosomal dominant polycystic kidney disease (ADPKD), a potentially life-threatening monogenic disorder marked by the gradual formation of fluid-filled cysts that compromise renal function and may lead to end-stage renal disease. Polycystin 1 is a protein of structural complexity, featuring numerous domains and engaging in diverse functions such as cellular adhesion, signal transduction, and ion channel activity. Our goal was to unravel its interactions with other proteins and its involvement in the onset of cystic diseases, ADPKD. This exploration seeks to enhance our grasp of the intricate interplay between its structure and functions, offering valuable insights into potential therapeutic targets. Our focus in this study is to study and characterize a REJ domain located at the N-terminal extracellular region of PC-1 and study its interaction with various components of the extracellular matrix. By exploring these interactions, we can better understand their potential significance in both the healthy development of the kidneys and the underlying mechanisms of ADPKD. In vitro, pull-down assays were used to assess the binding of the REJ fusion to several ECM components. The results showed that the REJ fusion protein binds to collagen VI, integrin, and fibronectin. The addition of the REJ fusion protein to HEK293 embryonic kidney epithelial cells in culture resulted in a significant reduction in the rate of cell proliferation. These findings indicated that the REJ region serves as a mediator for the interaction between polycystin-1 and the ECM and highlights the functional role of polycystin-1 in cell-matrix and cell-cell interactions.
References
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2. Lanktree MB, Chapman AB. New treatment paradigms for ADPKD: moving towards precision medicine. Nat Rev Nephrol. 2017;13(12):750-768. doi:10.1038/nrneph.2017.127
3. Hogan MC, Norby SM. Evaluation and management of pain in autosomal dominant polycystic kidney disease. Adv Chronic Kidney Dis. 2010;17(3):e1-e16. doi:10.1053/j.ackd.2010.01.005
4. Zhang Y, Reif G, Wallace DP. Extracellular matrix, integrins, and focal adhesion signaling in polycystic kidney disease. Cell Signal. 2020;72:109646. doi:10.1016/j.cellsig.2020.109646
5. Sharma M, Reif GA, Wallace DP. In vitro cyst formation of ADPKD cells. Methods Cell Biol. 2019;153:93-111. doi:10.1016/bs.mcb.2019.05.008
6. Malhas AN, Abuknesha RA, Price RG. Interaction of the leucine-rich repeats of polycystin-1 with extracellular matrix proteins: possible role in cell proliferation. J Am Soc Nephrol. 2002;13(1):19-26. doi:10.1681/ASN.V13119
7. Zhang C, Balbo B, Ma M, Zhao J, Tian X, Kluger Y, Somlo S. Cyclin-Dependent Kinase 1 Activity Is a Driver of Cyst Growth in Polycystic Kidney Disease. J Am Soc Nephrol. 2021 Jan;32(1):41-51. doi: 10.1681/ASN.2020040511. Epub 2020 Oct 12. PMID: 33046531; PMCID: PMC7894654.
8. Schröder S, Fraternali F, Quan X, Scott D, Qian F, Pfuhl M. When a module is not a domain: the case of the REJ module and the redefinition of the architecture of polycystin-1. Biochem J. 2011 May 1;435(3):651-60. doi: 10.1042/BJ20101810. PMID: 21314639; PMCID: PMC4979573.
9. Maser RL, Calvet JP. Adhesion GPCRs as a paradigm for understanding polycystin-1 G protein regulation. Cell Signal. 2020;72:109637. doi:10.1016/j.cellsig.2020.109637
10. Xu M, Ma L, Bujalowski PJ, Qian F, Sutton RB, Oberhauser AF. Analysis of the REJ Module of Polycystin-1 Using Molecular Modeling and Force-Spectroscopy Techniques. J Biophys. 2013;2013:525231. doi:10.1155/2013/525231
11. Weston BS, Malhas AN, Price RG. Structure-function relationships of the extracellular domain of the autosomal dominant polycystic kidney disease-associated protein, polycystin-1. FEBS Lett. 2003;538(1-3):8-13. doi:10.1016/s0014-5793(03)00130-3
12. Orhi Esarte Palomero, Megan Larmore, and Paul G.DeCaen, Polycystin Channel Complexes Esarte Palomero O, Larmore M, DeCaen PG. Polycystin Channel Complexes. Annu Rev Physiol. 2023;85:425-448. doi:10.1146/annurev-physiol-031522-084334
13. Sonbol HS, AlRashidi AA. Cloning and Expression of Receptor of Egg Jelly Protein of Polycystic Kidney Disease 1 Gene in Human Receptor of Egg Jelly Protein. Pharmacophore. 2022;13(6):97-105. https://doi.org/10.51847/vqgHaBLLgJ
14. Bandzerewicz A, Gadomska-Gajadhur A. Into the Tissues: Extracellular Matrix and Its Artificial Substitutes: Cell Signalling Mechanisms. Cells. 2022;11(5):914. Published 2022 Mar 7. doi:10.3390/cells11050914
15. Pastor-Pareja JC. Atypical basement membranes and basement membrane diversity - what is normal anyway?. J Cell Sci. 2020;133(8):jcs241794. Published 2020 Apr 21. doi:10.1242/jcs.241794.
16. Naylor RW, Morais MRPT, Lennon R. Complexities of the glomerular basement membrane. Nat Rev Nephrol. 2021;17(2):112-127. doi:10.1038/s41581-020-0329-y
17. Regoli M, Tosi GM, Neri G, Altera A, Orazioli D, Bertelli E. The Peculiar Pattern of Type IV Collagen Deposition in Epiretinal Membranes. J Histochem Cytochem. 2020 Feb;68(2):149-162. doi: 10.1369/0022155419897258. Epub 2019 Dec 20. PMID: 31858878; PMCID: PMC7003493.
18. Boudko SP, Danylevych N, Hudson BG, Pedchenko VK. Basement membrane collagen IV: Isolation of functional domains. Methods Cell Biol. 2018;143:171-185. doi:10.1016/bs.mcb.2017.08.010
19. Elango J, Hou C, Bao B, Wang S, Maté Sánchez de Val JE, Wenhui W. The Molecular Interaction of Collagen with Cell Receptors for Biological Function. Polymers (Basel). 2022;14(5):876. Published 2022 Feb 23. doi:10.3390/polym14050876
20. Bonche R, Smolen P, Chessel A, Boisivon S, Pisano S, Voigt A, Schaub S, Thérond P, Pizette S. Regulation of the collagen IV network by the basement membrane protein perlecan is crucial for squamous epithelial cell morphogenesis and organ architecture. Matrix Biol. 2022;114: 35-66. https://doi.org/10.1016/j.matbio.2022.10.004.
21. Hansen NUB, Gudmann NS, Karsdal MA. Type VIII collagen. In Biochemistry of Collagens, Laminins and Elastin (pp. 75-81). Academic Press,2019.
22. Hohenester E. Structural biology of laminins. Essays Biochemi. 2019;63(3):285-295.
23. Stafman LL, Aye J, Beierle EA. Role of Stemness factors in neuroblastoma: neuroblastoma stem cells, tumor microenvironment, and chemoresistance. Neuroblastoma. 2019;187-202.
24. McEver RP, Luscinskas, F.W. Cell adhesion. Hematology. 2018: 127-134).
25. Wilson PD. Polycystic kidney disease. N Engl J Med.2004;350(2): 151-164.
26. Weston BS, Bagnéris C, Price RG, Stirling JL. The polycystin-1 C-type lectin domain binds carbohydrate in a calcium-dependent manner, and interacts with extracellular matrix proteins in vitro. Biochim Biophys Acta. 2001;1536(2-3):161-176. doi:10.1016/s0925-4439(01)00046-1
27. Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays, J Immunol Methods. 1984:65: 55-63.
28. Choudhury B, Kandimalla R, Bharali R, Monisha J, Kunnumakara AB, Kalita K, Kotoky J. Anticancer Activity of Garcinia morella on T-Cell Murine Lymphoma Via Apoptotic Induction. Front Pharmacol. 2016 Jan 29;7:3. doi: 10.3389/fphar.2016.00003.
29. Marvin LF, Roberts MA, Fay LB. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry in clinical chemistry. Clin Chim Acta. 2003;337(1-2):11-21. doi:10.1016/j.cccn.2003.08.008
30. Krappitz M, Pioppini C, Bhardwaj R, Duygu E, Hollmann T, Somlo S, Fedeles S. WCN23-1242 Genetic interaction between XBP1 and Pkd1 modulates ADPKD progression. Kidney Int Rep. 2023;8(3):S250..
31. Al-Hamed MH, Alsahan N, Rice SJ, et al. Bialleleic PKD1 mutations underlie early-onset autosomal dominant polycystic kidney disease in Saudi Arabian families. Pediatr Nephrol. 2019;34(9):1615-1623. doi:10.1007/s00467-019-04267-x
32. Al-Muhanna FA, Al-Rubaish AM, Vatte C, Mohiuddin SS, Cyrus C, Ahmad A, Shakil Akhtar M, Albezra MA, Alali RA, Almuhanna AF, Huang K, Wang L, Al-Kuwaiti F, Elsalamouni TSA, Al Hwiesh A, Huang X, Keating B, Li J, Lanktree MB, Al-Ali AK. Exome sequencing of Saudi Arabian patients with ADPKD. Ren Fail. 2019 Nov;41(1):842-849. doi: 10.1080/0886022X.2019.1655453. PMID: 31488014; PMCID: PMC6735335.
33. Jerry X, Herbert W. The mechanics involved in ADPKD and nephrolithiasis interaction. Second Int Conf Biol Eng Med Sci (ICBioMed). 2022;12611: 521-526.
34. Rroji M, Figurek A, Spasovski G. Proteomic Approaches and Potential Applications in Autosomal Dominant Polycystic Kidney Disease and Fabry Disease. Diagnostics (Basel). 2023 Mar 17;13(6):1152. doi: 10.3390/diagnostics13061152. PMID: 36980460; PMCID: PMC10047122.
35. Guo Y, Yu M, Jing N, Zhang S. Production of soluble bioactive mouse leukemia inhibitory factor from Escherichia coli using MBP tag. Protein Expr Purif. 2018 Oct;150:86-91. doi: 10.1016/j.pep.2018.05.006. Epub 2018 May 26. PMID: 29758321.
36. Tan E, Chin CSH, Lim ZFS, Ng SK. HEK293 Cell Line as a Platform to Produce Recombinant Proteins and Viral Vectors. Front Bioeng Biotechnol. 2021 Dec 13;9:796991. doi: 10.3389/fbioe.2021.796991. PMID: 34966729; PMCID: PMC8711270.
37. Malm M, Saghaleyni R, Lundqvist M, Giudici M, Chotteau V, Field R, Rockberg J. Evolution from adherent to suspension: systems biology of HEK293 cell line development. Sci Rep., 2020;10(1):18996.
38. Naseri K, Khademi E, Mortazavi-Derazkola S. Introducing a new pharmaceutical agent: Facile synthesis of CuFe12O19@ HAp-APTES magnetic nanocomposites and its cytotoxic effect on HEK-293 cell as an efficient in vitro drug delivery system for atenolol. Arab J Chem. 2023;16(1): 104404.
39. Ahmadi R, Hemmateenejad B, Safavi A, Shojaeifard Z, Mohabbati M, Firuzi O. Assessment of cytotoxicity of choline chloride-based natural deep eutectic solvents against human HEK-293 cells: A QSAR analysis. Chemosphere. 2018 Oct;209:831-838. doi: 10.1016/j.chemosphere.2018.06.103. Epub 2018 Jun 15. PMID: 30114731.
40. Olsen S. Effects of ultra-high dilutions of sodium butyrate on viability and gene expression in HEK 293 cells. Homeopathy. 2017 Feb;106(1):32-36. doi: 10.1016/j.homp.2017.01.003. Epub 2017 Feb 22. PMID: 28325222.
41. Reshma VG, Mohanan PV. Cellular interactions of zinc oxide nanoparticles with human embryonic kidney (HEK 293) cells. Colloids and Surfaces B: Biointerfaces, 2017;157: 182-190.
42. Dong K, Zhang C, Tian X, Coman D, Hyder F, Ma M, Somlo S. Renal plasticity revealed through reversal of polycystic kidney disease in mice. Nat Genet. 2021 Dec;53(12):1649-1663. doi: 10.1038/s41588-021-00946-4. Epub 2021 Oct 11. PMID: 34635846; PMCID: PMC9278957.
43. Gargalionis AN, Basdra EK, Papavassiliou AG. Polycystins and Mechanotransduction in Human Disease. Int J Mol Sci. 2019 May 2;20(9):2182. doi: 10.3390/ijms20092182. PMID: 31052533; PMCID: PMC6539061.
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May 12, 2024
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Hala Salim Sonbol, Aljazi Abdullah Alrashidi. (2024). INTERPLAY BETWEEN POLYCYSTIN-1 AND EXTRACELLULAR MATRIX: INVESTIGATING THE REJ DOMAIN’S SIGNIFICANCE IN ADPKD PATHOGENESIS. Journal of Population Therapeutics and Clinical Pharmacology, 31(5), 245-256. https://doi.org/10.53555/jptcp.v31i5.6205
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All articles published in JPTCP are licensed under Copyright Creative Commons Attribution-NonCommercial 4.0 International License.
How to Cite
Hala Salim Sonbol, Aljazi Abdullah Alrashidi. (2024). INTERPLAY BETWEEN POLYCYSTIN-1 AND EXTRACELLULAR MATRIX: INVESTIGATING THE REJ DOMAIN’S SIGNIFICANCE IN ADPKD PATHOGENESIS. Journal of Population Therapeutics and Clinical Pharmacology, 31(5), 245-256. https://doi.org/10.53555/jptcp.v31i5.6205