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Development of Matrix Metalloproteinases-Mediated Extracellular Matrix Remodeling in Regenerative Medicine: A Mini Review

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Tissue Engineering and Regenerative Medicine Aims and scope

Abstract

Extracellular matrix (ECM) components confer biomechanical properties, maintain cell phenotype and mediate tissue homeostasis. ECM remodeling is complex and plays a key role in both physiological and pathological processes. Matrix metalloproteinases (MMPs) are a group of enzymes responsible for ECM degradation and have been accepted as a key regulator in ECM remodeling. In this mini-review, we summarize MMPs categories, functions and the targeted substrates. We then discuss current understanding of the role of MMPs-mediated events, including inflammation reaction, angiogenesis, cellular activities, etc., in ECM remodeling in the context of regenerative medicine.

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References

  1. Shih B, Garside E, McGrouther DA, Bayat A. Molecular dissection of abnormal wound healing processes resulting in keloid disease. Wound Repair Regen. 2010;18:139–53.

    PubMed  Google Scholar 

  2. Franz S, Rammelt S, Scharnweber D, Simon JC. Immune responses to implants—a review of the implications for the design of immunomodulatory biomaterials. Biomaterials. 2011;32:6692–709.

    CAS  PubMed  Google Scholar 

  3. Mouton AJ, Rivera OJ, Lindsey ML. Myocardial infarction remodeling that progresses to heart failure: a signaling misunderstanding. Am J Physiol Heart Circ Physiol. 2018;315:H71–9.

    CAS  PubMed  PubMed Central  Google Scholar 

  4. Khalili AA, Ahmad MR. A review of cell adhesion studies for biomedical and biological applications. Int J Mol Sci. 2015;16:18149–84.

    CAS  PubMed  Google Scholar 

  5. Berthiaume F, Maguire TJ, Yarmush ML. Tissue engineering and regenerative medicine: history, progress, and challenges. Annu Rev Chem Biomol Eng. 2011;2:403–30.

    PubMed  Google Scholar 

  6. Petrosyan A, Montali F, Peloso A, Citro A, Byers LN, La Pointe C, et al. Regenerative medicine technologies applied to transplant medicine. An update. Front Bioeng Biotechnol. 2022;10:1015628.

    PubMed  PubMed Central  Google Scholar 

  7. Wang Y, Jang YY. From cells to organs: the present and future of regenerative medicine. Adv Exp Med Biol. 2022;1376:135–49.

    CAS  PubMed  PubMed Central  Google Scholar 

  8. Brown M, Li J, Moraes C, Tabrizian M, Li-Jessen NYK. Decellularized extracellular matrix: new promising and challenging biomaterials for regenerative medicine. Biomaterials. 2022;289:121786.

    CAS  PubMed  Google Scholar 

  9. Huang Y, Miyamoto D, Hidaka M, Adachi T, Gu WL, Eguchi S. Regenerative medicine for the hepatobiliary system: A review. J Hepatobiliary Pancreat Sci. 2021;28:913–30.

    PubMed  Google Scholar 

  10. Ali S, Haque N, Azhar Z, Saeinasab M, Sefat F. Regenerative medicine of liver: promises, advances and challenges. Biomimetics (Basel). 2021;6:62.

    PubMed  Google Scholar 

  11. Pang C, Ibrahim A, Bulstrode NW, Ferretti P. An overview of the therapeutic potential of regenerative medicine in cutaneous wound healing. Int Wound J. 2017;14:450–9.

    PubMed  PubMed Central  Google Scholar 

  12. Woodrow T, Chant T, Chant H. Treatment of diabetic foot wounds with acellular fish skin graft rich in omega-3: a prospective evaluation. J Wound Care. 2019;28:76–80.

    PubMed  Google Scholar 

  13. Michael S, Winters C, Khan M. Acellular fish skin graft use for diabetic lower extremity wound healing: a retrospective study of 58 ulcerations and a literature review. Wounds. 2019;31:262–8.

    PubMed  Google Scholar 

  14. Al-Ghadban S, Artiles M, Bunnell BA. Adipose stem cells in regenerative medicine: looking forward. Front Bioeng Biotechnol. 2021;9:837464.

    PubMed  Google Scholar 

  15. Gross J, Lapiere CM. Collagenolytic activity in amphibian tissues: a tissue culture assay. Proc Natl Acad Sci U S A. 1962;48:1014–22.

    CAS  PubMed  PubMed Central  Google Scholar 

  16. Jabłońska-Trypuć A, Matejczyk M, Rosochacki S. Matrix metalloproteinases (MMPs), the main extracellular matrix (ECM) enzymes in collagen degradation, as a target for anticancer drugs. J Enzyme Inhib Med Chem. 2016;31:177–83.

    PubMed  Google Scholar 

  17. Page-McCaw A, Ewald AJ, Werb Z. Matrix metalloproteinases and the regulation of tissue remodelling. Nat Rev Mol Cell Biol. 2007;8:221–33.

    CAS  PubMed  PubMed Central  Google Scholar 

  18. Chung L, Dinakarpandian D, Yoshida N, Lauer-Fields JL, Fields GB, Visse R, et al. Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis. Embo J. 2004;23:3020–30.

    CAS  PubMed  PubMed Central  Google Scholar 

  19. Mittal R, Patel AP, Debs LH, Nguyen D, Patel K, Grati M, et al. Intricate functions of matrix metalloproteinases in physiological and pathological conditions. J Cell Physiol. 2016;231:2599–621.

    CAS  PubMed  Google Scholar 

  20. Keskin ES, Keskin ER, Öztürk MB, Çakan D. The effect of MMP-1 on wound healing and scar formation. Aesthetic Plast Surg. 2021;45:2973–9.

    PubMed  Google Scholar 

  21. Wu Y, Tang Y, Zhang X, Chu Z, Liu Y, Tang C. MMP-1 promotes osteogenic differentiation of human bone marrow mesenchymal stem cells via the JNK and ERK pathway. Int J Biochem Cell Biol. 2020;129:105880.

    CAS  PubMed  Google Scholar 

  22. Hu Q, Ecker M. Overview of MMP-13 as a promising target for the treatment of osteoarthritis. Int J Mol Sci. 2021;22:1742.

  23. Arai Y, Choi B, Kim BJ, Park S, Park H, Moon JJ, et al. Cryptic ligand on collagen matrix unveiled by MMP13 accelerates bone tissue regeneration via MMP13/Integrin α3/RUNX2 feedback loop. Acta Biomater. 2021;125:219–30.

    CAS  PubMed  Google Scholar 

  24. Zhao Y, Wang Q, Zeng Y, Xie Y, Zhou J. Gastrin/CCK-B receptor signaling promotes cell invasion and metastasis by upregulating MMP-2 and VEGF expression in gastric cancer. J Cancer. 2022;13:134–45.

    CAS  PubMed  PubMed Central  Google Scholar 

  25. Pramanik KK, Mishra R. ERK-mediated upregulation of matrix metalloproteinase-2 promotes the invasiveness in human oral squamous cell carcinoma (OSCC). Exp Cell Res. 2022;411:112984.

    CAS  PubMed  Google Scholar 

  26. Hung SY, Lin CY, Yu CC, Chen HT, Lien MY, Huang YW, et al. Visfatin promotes the metastatic potential of chondrosarcoma cells by stimulating AP-1-dependent MMP-2 production in the MAPK pathway. Int J Mol Sci. 2021;22:8642.

  27. Koutsouki E, Beeching CA, Slater SC, Blaschuk OW, Sala-Newby GB, George SJ. N-cadherin-dependent cell-cell contacts promote human saphenous vein smooth muscle cell survival. Arterioscler Thromb Vasc Biol. 2005;25:982–8.

    CAS  PubMed  Google Scholar 

  28. Uglow EB, Slater S, Sala-Newby GB, Aguilera-Garcia CM, Angelini GD, Newby AC, et al. Dismantling of cadherin-mediated cell-cell contacts modulates smooth muscle cell proliferation. Circ Res. 2003;92:1314–21.

    CAS  PubMed  Google Scholar 

  29. Newby AC. Matrix metalloproteinases regulate migration, proliferation, and death of vascular smooth muscle cells by degrading matrix and non-matrix substrates. Cardiovasc Res. 2006;69:614–24.

    CAS  PubMed  Google Scholar 

  30. George SJ, Dwivedi A. MMPs, cadherins, and cell proliferation. Trends Cardiovasc Med. 2004;14:100–5.

    CAS  PubMed  Google Scholar 

  31. Ikeda U, Shimada K. Matrix metalloproteinases and coronary artery diseases. Clin Cardiol. 2003;26:55–9.

    PubMed  Google Scholar 

  32. Seliktar D, Zisch AH, Lutolf MP, Wrana JL, Hubbell JA. MMP-2 sensitive, VEGF-bearing bioactive hydrogels for promotion of vascular healing. J Biomed Mater Res A. 2004;68:704–16.

    CAS  PubMed  Google Scholar 

  33. Opdenakker G, Van den Steen PE, Dubois B, Nelissen I, Van Coillie E, Masure S, et al. Gelatinase B functions as regulator and effector in leukocyte biology. J Leukoc Biol. 2001;69:851–9.

    CAS  PubMed  Google Scholar 

  34. Debret R, Le Naour RR, Sallenave JM, Deshorgue A, Hornebeck WG, Guenounou M, et al. Elastin fragments induce IL-1beta upregulation via NF-kappaB pathway in melanoma cells. J Invest Dermatol. 2006;126:1860–8.

    CAS  PubMed  Google Scholar 

  35. Rybakin V, Stas M, Ugarte-Berzal E, Noppen S, Vandooren J, Van Aelst I, et al. Gelatinase B/matrix metalloproteinase-9 and other neutrophil proteases switch off interleukin-2 activity. Biochem J. 2019;476:2191–208.

    CAS  PubMed  Google Scholar 

  36. Russo MV, Latour LL, McGavern DB. Distinct myeloid cell subsets promote meningeal remodeling and vascular repair after mild traumatic brain injury. Nat Immunol. 2018;19:442–52.

    CAS  PubMed  PubMed Central  Google Scholar 

  37. Rundhaug JE. Matrix metalloproteinases and angiogenesis. J Cell Mol Med. 2005;9:267–85.

    CAS  PubMed  PubMed Central  Google Scholar 

  38. Mathis KM, Sturgeon KM, Winkels RM, Wiskemann J, De Souza MJ, Schmitz KH. Bone resorption and bone metastasis risk. Med Hypotheses. 2018;118:36–41.

    PubMed  Google Scholar 

  39. Tu YA, Chou CH, Yang PK, Shun CT, Wen WF, Tsao PN, et al. Intentional endometrial injury enhances angiogenesis through increased production and activation of MMP-9 by TNF-α and MMP-3 in a mouse model. Mol Hum Reprod. 2021;27:gabb055.

  40. Parks WC, Wilson CL, López-Boado YS. Matrix metalloproteinases as modulators of inflammation and innate immunity. Nat Rev Immunol. 2004;4:617–29.

    CAS  PubMed  Google Scholar 

  41. Gurney KJ, Estrada EY, Rosenberg GA. Blood-brain barrier disruption by stromelysin-1 facilitates neutrophil infiltration in neuroinflammation. Neurobiol Dis. 2006;23:87–96.

    CAS  PubMed  Google Scholar 

  42. Rong S, Li C, Li S, Wu S, Sun F. Genetically modified adipose-derived stem cells with matrix metalloproteinase 3 promote scarless cutaneous repair. Dermatol Ther. 2020;33:e14112.

    CAS  PubMed  Google Scholar 

  43. Piskór BM, Przylipiak A, Dąbrowska E, Niczyporuk M, Ławicki S. Matrilysins and stromelysins in pathogenesis and diagnostics of cancers. Cancer Manag Res. 2020;12:10949–64.

    PubMed  PubMed Central  Google Scholar 

  44. Visse R, Nagase H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ Res. 2003;92:827–39.

    CAS  PubMed  Google Scholar 

  45. McGuire JK, Li Q, Parks WC. Matrilysin (matrix metalloproteinase-7) mediates E-cadherin ectodomain shedding in injured lung epithelium. Am J Pathol. 2003;162:1831–43.

    CAS  PubMed  PubMed Central  Google Scholar 

  46. Davies G, Jiang WG, Mason MD. Matrilysin mediates extracellular cleavage of E-cadherin from prostate cancer cells: a key mechanism in hepatocyte growth factor/scatter factor-induced cell–cell dissociation and in vitro invasion. Clin Cancer Res. 2001;7:3289–97.

    CAS  PubMed  Google Scholar 

  47. Noë V, Fingleton B, Jacobs K, Crawford HC, Vermeulen S, Steelant W, et al. Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1. J Cell Sci. 2001;114:111–8.

    PubMed  Google Scholar 

  48. Friedl P, Gilmour D. Collective cell migration in morphogenesis, regeneration and cancer. Nat Rev Mol Cell Biol. 2009;10:445–57.

    CAS  PubMed  Google Scholar 

  49. Chen P, Abacherli LE, Nadler ST, Wang Y, Li Q, Parks WC. MMP7 shedding of syndecan-1 facilitates re-epithelialization by affecting alpha(2)beta(1) integrin activation. PLoS One. 2009;4:e6565.

    PubMed  PubMed Central  Google Scholar 

  50. Stepp MA, Liu Y, Pal-Ghosh S, Jurjus RA, Tadvalkar G, Sekaran A, et al. Reduced migration, altered matrix and enhanced TGFbeta1 signaling are signatures of mouse keratinocytes lacking Sdc1. J Cell Sci. 2007;120:2851–63.

    CAS  PubMed  Google Scholar 

  51. Altemeier WA, Schlesinger SY, Buell CA, Brauer R, Rapraeger AC, Parks WC. Transmembrane and extracellular domains of syndecan-1 have distinct functions in regulating lung epithelial migration and adhesion. J Biol Chem. 2012;287:34927–35.

    CAS  PubMed  PubMed Central  Google Scholar 

  52. Altemeier WA, Schlesinger SY, Buell CA, Parks WC, Chen P. Syndecan-1 controls cell migration by activating Rap1 to regulate focal adhesion disassembly. J Cell Sci. 2012;125:5188–95.

    CAS  PubMed  PubMed Central  Google Scholar 

  53. Uría JA, López-Otín C. Matrilysin-2, a new matrix metalloproteinase expressed in human tumors and showing the minimal domain organization required for secretion, latency, and activity. Cancer Res. 2000;60:4745–51.

    PubMed  Google Scholar 

  54. de Coignac AB, Elson G, Delneste Y, Magistrelli G, Jeannin P, Aubry JP, et al. Cloning of MMP-26. A novel matrilysin-like proteinase. Eur J Biochem. 2000;267:3323–9.

    PubMed  Google Scholar 

  55. Marchenko GN, Ratnikov BI, Rozanov DV, Godzik A, Deryugina EI, Strongin AY. Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin. Biochem J. 2001;356:705–18.

    CAS  PubMed  PubMed Central  Google Scholar 

  56. Marchenko ND, Marchenko GN, Weinreb RN, Lindsey JD, Kyshtoobayeva A, Crawford HC, et al. Beta-catenin regulates the gene of MMP-26, a novel metalloproteinase expressed both in carcinomas and normal epithelial cells. Int J Biochem Cell Biol. 2004;36:942–56.

    CAS  PubMed  Google Scholar 

  57. Gutschalk CM, Yanamandra AK, Linde N, Meides A, Depner S, Mueller MM. GM-CSF enhances tumor invasion by elevated MMP-2, -9, and -26 expression. Cancer Med. 2013;2:117–29.

    CAS  PubMed  Google Scholar 

  58. Sabeh F, Shimizu-Hirota R, Weiss SJ. Protease-dependent versus -independent cancer cell invasion programs: three-dimensional amoeboid movement revisited. J Cell Biol. 2009;185:11–9.

    CAS  PubMed  PubMed Central  Google Scholar 

  59. Sabeh F, Ota I, Holmbeck K, Birkedal-Hansen H, Soloway P, Balbin M, et al. Tumor cell traffic through the extracellular matrix is controlled by the membrane-anchored collagenase MT1-MMP. J Cell Biol. 2004;167:769–81.

    CAS  PubMed  PubMed Central  Google Scholar 

  60. Feng Y, Cai H, Huang X, Li Z, Chi Z, Ge RL. Active MT1-MMP is tethered to collagen fibers in DDR2-containing remnants. Gene. 2021;788:145673.

    CAS  PubMed  Google Scholar 

  61. Gifford V, Itoh Y. MT1-MMP-dependent cell migration: proteolytic and non-proteolytic mechanisms. Biochem Soc Trans. 2019;47:811–26.

    CAS  PubMed  PubMed Central  Google Scholar 

  62. Sato H, Takino T, Okada Y, Cao J, Shinagawa A, Yamamoto E, et al. A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature. 1994;370:61–5.

    CAS  PubMed  Google Scholar 

  63. Kang H, Hong Z, Zhong M, Klomp J, Bayless KJ, Mehta D, et al. Piezo1 mediates angiogenesis through activation of MT1-MMP signaling. Am J Physiol Cell Physiol. 2019;316:C92-103.

  64. Itoh Y. Membrane-type matrix metalloproteinases: Their functions and regulations. Matrix Biol. 2015;44–46:207–23.

    PubMed  Google Scholar 

  65. Kajita M, Itoh Y, Chiba T, Mori H, Okada A, Kinoh H, et al. Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration. J Cell Biol. 2001;153:893–904.

    CAS  PubMed  PubMed Central  Google Scholar 

  66. Sakamoto T, Seiki M. A membrane protease regulates energy production in macrophages by activating hypoxia-inducible factor-1 via a non-proteolytic mechanism. J Biol Chem. 2010;285:29951–64.

    CAS  PubMed  PubMed Central  Google Scholar 

  67. Dumin JA, Dickeson SK, Stricker TP, Bhattacharyya-Pakrasi M, Roby JD, Santoro SA, et al. Pro-collagenase-1 (matrix metalloproteinase-1) binds the alpha(2)beta(1) integrin upon release from keratinocytes migrating on type I collagen. J Biol Chem. 2001;276:29368–74.

    CAS  PubMed  Google Scholar 

  68. Brooks PC, Strömblad S, Sanders LC, von Schalscha TL, Aimes RT, Stetler-Stevenson WG, et al. Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3. Cell. 1996;85:683–93.

    CAS  PubMed  Google Scholar 

  69. Peck BD, Murach KA, Walton RG, Simmons AJ, Long DE, Kosmac K, et al. A muscle cell-macrophage axis involving matrix metalloproteinase 14 facilitates extracellular matrix remodeling with mechanical loading. FASEB J. 2022;36:e22155.

    CAS  PubMed  Google Scholar 

  70. Nénan S, Boichot E, Lagente V, Bertrand CP. Macrophage elastase (MMP-12): a pro-inflammatory mediator? Mem Inst Oswaldo Cruz. 2005;100:167–72.

    PubMed  Google Scholar 

  71. Banda MJ, Werb Z. Mouse macrophage elastase. Purification and characterization as a metalloproteinase. Biochem J. 1981;193:589–605.

    CAS  PubMed  PubMed Central  Google Scholar 

  72. Heinz A. Elastases and elastokines: elastin degradation and its significance in health and disease. Crit Rev Biochem Mol Biol. 2020;55:252–73.

    CAS  PubMed  Google Scholar 

  73. Chen YE. MMP-12, an old enzyme plays a new role in the pathogenesis of rheumatoid arthritis? Am J Pathol. 2004;165:1069–70.

    CAS  PubMed  PubMed Central  Google Scholar 

  74. Gronski TJ Jr, Martin RL, Kobayashi DK, Walsh BC, Holman MC, Huber M, et al. Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase. J Biol Chem. 1997;272:12189–94.

    CAS  PubMed  Google Scholar 

  75. Ashworth JL, Murphy G, Rock MJ, Sherratt MJ, Shapiro SD, Shuttleworth CA, et al. Fibrillin degradation by matrix metalloproteinases: implications for connective tissue remodelling. Biochem J. 1999;340:171–81.

    CAS  PubMed  PubMed Central  Google Scholar 

  76. Jariwala N, Ozols M, Bell M, Bradley E, Gilmore A, Debelle L, et al. Matrikines as mediators of tissue remodelling. Adv Drug Deliv Rev. 2022;185:114240.

    CAS  PubMed  Google Scholar 

  77. Davis GE, Bayless KJ, Davis MJ, Meininger GA. Regulation of tissue injury responses by the exposure of matricryptic sites within extracellular matrix molecules. Am J Pathol. 2000;156:1489–98.

    CAS  PubMed  PubMed Central  Google Scholar 

  78. Wells JM, Gaggar A, Blalock JE. MMP generated matrikines. Matrix Biol. 2015;44–46:122–9.

    PubMed  PubMed Central  Google Scholar 

  79. Pfister RR, Haddox JL, Sommers CI. Injection of chemoattractants into normal cornea: a model of inflammation after alkali injury. Invest Ophthalmol Vis Sci. 1998;39:1744–50.

    CAS  PubMed  Google Scholar 

  80. Haddox JL, Pfister RR, Sommers CI, Blalock JE, Villain M. Inhibitory effect of a complementary peptide on ulceration in the alkali-injured rabbit cornea. Invest Ophthalmol Vis Sci. 2001;42:2769–75.

    CAS  PubMed  Google Scholar 

  81. Haddox JL, Pfister RR, Muccio DD, Villain M, Sommers CI, Chaddha M, et al. Bioactivity of peptide analogs of the neutrophil chemoattractant, N-acetyl-proline-glycine-proline. Invest Ophthalmol Vis Sci. 1999;40:2427–9.

    CAS  PubMed  Google Scholar 

  82. Patel DF, Snelgrove RJ. The multifaceted roles of the matrikine Pro-Gly-Pro in pulmonary health and disease. Eur Respir Rev. 2018;27:180017.

  83. Lindsey ML, Iyer RP, Zamilpa R, Yabluchanskiy A, DeLeon-Pennell KY, Hall ME, et al. A novel collagen matricryptin reduces left ventricular dilation post-myocardial infarction by promoting scar formation and angiogenesis. J Am Coll Cardiol. 2015;66:1364–74.

    PubMed  PubMed Central  Google Scholar 

  84. Ramazani Y, Knops N, Elmonem MA, Nguyen TQ, Arcolino FO, van den Heuvel L, et al. Connective tissue growth factor (CTGF) from basics to clinics. Matrix Biol. 2018;68–9:44–66.

    PubMed  Google Scholar 

  85. Mecham RP, Broekelmann TJ, Fliszar CJ, Shapiro SD, Welgus HG, Senior RM. Elastin degradation by matrix metalloproteinases. Cleavage site specificity and mechanisms of elastolysis. J Biol Chem. 1997;272:18071–6.

    CAS  PubMed  Google Scholar 

  86. Taddese S, Weiss AS, Jahreis G, Neubert RH, Schmelzer CE. In vitro degradation of human tropoelastin by MMP-12 and the generation of matrikines from domain 24. Matrix Biol. 2009;28:84–91.

    CAS  PubMed  Google Scholar 

  87. Guo G, Booms P, Halushka M, Dietz HC, Ney A, Stricker S, et al. Induction of macrophage chemotaxis by aortic extracts of the mgR Marfan mouse model and a GxxPG-containing fibrillin-1 fragment. Circulation. 2006;114:1855–62.

    CAS  PubMed  Google Scholar 

  88. Li F, Chen J, Leier A, Marquez-Lago T, Liu Q, Wang Y, et al. DeepCleave: a deep learning predictor for caspase and matrix metalloprotease substrates and cleavage sites. Bioinformatics. 2020;36:1057–65.

    CAS  PubMed  Google Scholar 

  89. Ozols M, Eckersley A, Platt CI, Stewart-McGuinness C, Hibbert SA, Revote J, et al. Predicting proteolysis in complex proteomes using deep learning. Int J Mol Sci. 2021;22:3071.

  90. Naba A, Clauser KR, Ding H, Whittaker CA, Carr SA, Hynes RO. The extracellular matrix: tools and insights for the “omics” era. Matrix Biol. 2016;49:10–24.

    CAS  PubMed  Google Scholar 

  91. Shao X, Taha IN, Clauser KR, Gao YT, Naba A. MatrisomeDB: the ECM-protein knowledge database. Nucleic Acids Res. 2020;48:D1136-44.

    CAS  PubMed  Google Scholar 

  92. Schilling O, auf dem Keller U, Overall CM. Protease specificity profiling by tandem mass spectrometry using proteome-derived peptide libraries. Methods Mol Biol. 2011;753:257–72.

    CAS  PubMed  Google Scholar 

  93. Argelaguet R, Cuomo ASE, Stegle O, Marioni JC. Computational principles and challenges in single-cell data integration. Nat Biotechnol. 2021;39:1202–15.

    CAS  PubMed  Google Scholar 

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Acknowledgements

This work was supported by the National Nature Science Foundation of China (81772101, 81801933), the Natural Science Foundation of Guangdong Province of China (2017A030313900), and the Administrator Foundation of Nanfang Hospital (2016Z010, 2017C008).

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  1. Kaiqi Chen and Mimi Xu contributed equally to this article.

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  1. Department of Plastic and Cosmetic Surgery, Nanfang Hospital, Southern Medical University, 1838 Guangzhou North Road, Guangzhou, 510515, Guangdong, People’s Republic of China

    Kaiqi Chen, Mimi Xu, Feng Lu & Yunfan He

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Chen, K., Xu, M., Lu, F. et al. Development of Matrix Metalloproteinases-Mediated Extracellular Matrix Remodeling in Regenerative Medicine: A Mini Review. Tissue Eng Regen Med 20, 661–670 (2023). https://doi.org/10.1007/s13770-023-00536-x

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