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Matrix metalloproteinase 7 promoted Schwann cell migration and myelination after rat sciatic nerve injury

Wang, Hongkui, Zhang, Ping, Yu, Jun, Zhang, Fuchao, Dai, Wenzhao, Yi, Sheng·2019·Molecular Brain
DOI 10.1186/s13041-019-0516-6PMC PMC6889483
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Abstract

Schwann cells experience de-differentiation, proliferation, migration, re-differentiation and myelination, and participate in the repair and regeneration of injured peripheral nerves. Our previous sequencing analysis suggested that the gene expression level of matrix metalloproteinase 7 (MMP7), a Schwann cell-secreted proteolytic enzyme, was robustly elevated in rat sciatic nerve segments after nerve injury. However, the biological roles of MMP7 are poorly understood. Here, we exposed primary cultured Schwann cells with MMP7 recombinant protein and transfected siRNA against MMP7 into Schwann cells to examine the effect of exogenous and endogenous MMP7. Meanwhile, the effects of MMP7 in nerve regeneration after sciatic nerve crush in vivo were observed. Furthermore, RNA sequencing and bioinformatic analysis of Schwann cells were conducted to show the molecular mechanism behind the phenomenon. In vitro studies showed that MMP7 significantly elevated the migration rate of Schwann cells but did not affect the proliferation rate of Schwann cells. In vivo studies demonstrated that increased level of MMP7 contributed to Schwann cell migration and myelin sheaths formation after peripheral nerve injury. MMP7-mediated genetic changes were revealed by sequencing and bioinformatic analysis. Taken together, our current study demonstrated the promoting effect of MMP7 on Schwann cell migration and peripheral nerve regeneration, benefited the understanding of cellular and molecular mechanisms underlying peripheral nerve injury, and thus might facilitate the treatment of peripheral nerve regeneration in clinic.

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  1. Gu X, Ding F, Yang Y, Liu J. Construction of tissue engineered nerve grafts and their application in peripheral nerve regeneration. Prog Neurobiol. 2011;93(2):204–30. https://doi.org/10.1016/j.pneurobio.2010.11.002. · DOI
  2. Li R, Liu Z, Pan Y, Chen L, Zhang Z, Lu L. Peripheral nerve injuries treatment: a systematic review. Cell Biochem Biophys. 2014;68(3):449–54. https://doi.org/10.1007/s12013-013-9742-1. · DOI
  3. Yi S, Xu L, Gu X. Scaffolds for peripheral nerve repair and reconstruction. Exp Neurol. 2018. https://doi.org/10.1016/j.expneurol.2018.05.016. · DOI
  4. Lee SK, Wolfe SW. Peripheral nerve injury and repair. J Am Acad Orthop Surg. 2000;8(4):243–52. · DOI · Paper page
  5. Wong KM, Babetto E, Beirowski B. Axon degeneration: make the Schwann cell great again. Neural Regen Res. 2017;12(4):518–24. https://doi.org/10.4103/1673-5374.205000. · DOI
  6. Chen ZL, Yu WM, Strickland S. Peripheral regeneration. Annu Rev Neurosci. 2007;30:209–33. https://doi.org/10.1146/annurev.neuro.30.051606.094337. · DOI
  7. Dubovy P. Schwann cells and endoneurial extracellular matrix molecules as potential cues for sorting of regenerated axons: a review. Anat Sci Int. 2004;79(4):198–208. https://doi.org/10.1111/j.1447-073x.2004.00090.x. · DOI
  8. Hill R. Extracellular matrix remodelling in human diabetic neuropathy. J Anat. 2009;214(2):219–25. https://doi.org/10.1111/j.1469-7580.2008.01026.x. · DOI
  9. Lamarca A, Gella A, Martianez T, Segura M, Figueiro-Silva J, Grijota-Martinez C, Trullas R, Casals N. Uridine 5′-triphosphate promotes in vitro Schwannoma cell migration through matrix metalloproteinase-2 activation. PLoS One. 2014;9(6):e98998. https://doi.org/10.1371/journal.pone.0098998. · DOI
  10. Page-McCaw A, Ewald AJ, Werb Z. Matrix metalloproteinases and the regulation of tissue remodelling. Nat Rev Mol Cell Biol. 2007;8(3):221–33. https://doi.org/10.1038/nrm2125. · DOI · Paper page
  11. Verma RP, Hansch C. Matrix metalloproteinases (MMPs): chemical-biological functions and (Q)SARs. Bioorg Med Chem. 2007;15(6):2223–68. https://doi.org/10.1016/j.bmc.2007.01.011. · DOI
  12. Nagase H, Visse R, Murphy G. Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res. 2006;69(3):562–73. https://doi.org/10.1016/j.cardiores.2005.12.002. · DOI
  13. Sternlicht MD, Werb Z. How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol. 2001;17:463–516. https://doi.org/10.1146/annurev.cellbio.17.1.463. · DOI · Paper page
  14. Krekoski CA, Neubauer D, Graham JB, Muir D. Metalloproteinase-dependent predegeneration in vitro enhances axonal regeneration within acellular peripheral nerve grafts. J Neurosci. 2002;22(23):10408–15. · DOI
  15. Remacle AG, Hullugundi SK, Dolkas J, Angert M, Chernov AV, Strongin AY, Shubayev VI. Acute- and late-phase matrix metalloproteinase (MMP)-9 activity is comparable in female and male rats after peripheral nerve injury. J Neuroinflammation. 2018;15(1):89. https://doi.org/10.1186/s12974-018-1123-7. · DOI
  16. La Fleur M, Underwood JL, Rappolee DA, Werb Z. Basement membrane and repair of injury to peripheral nerve: defining a potential role for macrophages, matrix metalloproteinases, and tissue inhibitor of metalloproteinases-1. J Exp Med. 1996;184(6):2311–26. · DOI
  17. Ferguson TA, Muir D. MMP-2 and MMP-9 increase the neurite-promoting potential of schwann cell basal laminae and are upregulated in degenerated nerve. Mol Cell Neurosci. 2000;16(2):157–67. https://doi.org/10.1006/mcne.2000.0859. · DOI
  18. Kobayashi H, Chattopadhyay S, Kato K, Dolkas J, Kikuchi S, Myers RR, Shubayev VI. MMPs initiate Schwann cell-mediated MBP degradation and mechanical nociception after nerve damage. Mol Cell Neurosci. 2008;39(4):619–27. https://doi.org/10.1016/j.mcn.2008.08.008. · DOI
  19. Mantuano E, Inoue G, Li X, Takahashi K, Gaultier A, Gonias SL, Campana WM. The hemopexin domain of matrix metalloproteinase-9 activates cell signaling and promotes migration of schwann cells by binding to low-density lipoprotein receptor-related protein. J Neurosci. 2008;28(45):11571–82. https://doi.org/10.1523/JNEUROSCI.3053-08.2008. · DOI
  20. Qin J, Zha GB, Yu J, Zhang HH, Yi S. Differential temporal expression of matrix metalloproteinases following sciatic nerve crush. Neural Regen Res. 2016;11(7):1165–71. https://doi.org/10.4103/1673-5374.187059. · DOI · Paper page
  21. Yi S, Yuan Y, Chen Q, Wang X, Gong L, Liu J, Gu X, Li S. Regulation of Schwann cell proliferation and migration by miR-1 targeting brain-derived neurotrophic factor after peripheral nerve injury. Sci Rep. 2016;6:29121. https://doi.org/10.1038/srep29121. · DOI
  22. Kim D, Pertea G, Trapnell C, Pimentel H, Kelley R, Salzberg SL. TopHat2: accurate alignment of transcriptomes in the presence of insertions, deletions and gene fusions. Genome Biol. 2013;14(4):R36. https://doi.org/10.1186/gb-2013-14-4-r36. · DOI · Paper page
  23. Li B, Dewey CN. RSEM: accurate transcript quantification from RNA-Seq data with or without a reference genome. BMC Bioinformatics. 2011;12:323. https://doi.org/10.1186/1471-2105-12-323. · DOI · Paper page
  24. Yong VW. Metalloproteinases: mediators of pathology and regeneration in the CNS. Nat Rev Neurosci. 2005;6(12):931–44. https://doi.org/10.1038/nrn1807. · DOI · Paper page
  25. Yong VW, Power C, Forsyth P, Edwards DR. Metalloproteinases in biology and pathology of the nervous system. Nat Rev Neurosci. 2001;2(7):502–11. https://doi.org/10.1038/35081571. · DOI
  26. Nishihara T, Remacle AG, Angert M, Shubayev I, Shiryaev SA, Liu H, Dolkas J, Chernov AV, Strongin AY, Shubayev VI. Matrix metalloproteinase-14 both sheds cell surface neuronal glial antigen 2 (NG2) proteoglycan on macrophages and governs the response to peripheral nerve injury. J Biol Chem. 2015;290(6):3693–707. https://doi.org/10.1074/jbc.M114.603431. · DOI
  27. Hsu JY, McKeon R, Goussev S, Werb Z, Lee JU, Trivedi A, Noble-Haeusslein LJ. Matrix metalloproteinase-2 facilitates wound healing events that promote functional recovery after spinal cord injury. J Neurosci. 2006;26(39):9841–50. https://doi.org/10.1523/JNEUROSCI.1993-06.2006. · DOI
  28. Shubayev VI, Myers RR. Matrix metalloproteinase-9 promotes nerve growth factor-induced neurite elongation but not new sprout formation in vitro. J Neurosci Res. 2004;77(2):229–39. https://doi.org/10.1002/jnr.20160. · DOI
  29. Larsen PH, Wells JE, Stallcup WB, Opdenakker G, Yong VW. Matrix metalloproteinase-9 facilitates remyelination in part by processing the inhibitory NG2 proteoglycan. J Neurosci. 2003;23(35):11127–35. · DOI
  30. Liu H, Kim Y, Chattopadhyay S, Shubayev I, Dolkas J, Shubayev VI. Matrix metalloproteinase inhibition enhances the rate of nerve regeneration in vivo by promoting dedifferentiation and mitosis of supporting schwann cells. J Neuropathol Exp Neurol. 2010;69(4):386–95. https://doi.org/10.1097/NEN.0b013e3181d68d12. · DOI
  31. Spinale FG. Myocardial matrix remodeling and the matrix metalloproteinases: influence on cardiac form and function. Physiol Rev. 2007;87(4):1285–342. https://doi.org/10.1152/physrev.00012.2007. · DOI
  32. Kessenbrock K, Plaks V, Werb Z. Matrix metalloproteinases: regulators of the tumor microenvironment. Cell. 2010;141(1):52–67. https://doi.org/10.1016/j.cell.2010.03.015. · DOI · Paper page

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Metadata

Authors
Wang, H., Zhang, P., Yu, J., Zhang, F., Dai, W., & Yi, S.
ORCID
Yi, Sheng
Venue
Molecular Brain
Publisher
Springer Science and Business Media LLC
Published
2019-12
Volume
12
Issue
1
ISSN
1756-6606
DOI
10.1186/s13041-019-0516-6
PMC
PMC6889483
Cited by
25
References
1
Language
en
Licence
Funders
National Natural Science Foundation of China (31700926)

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