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Cited by 263Protease and Inhibitor MechanismsBone and Dental Protein StudiesWound Healing and Treatments

MMP generated matrikines

Open access
Wells, J. Michael, Gaggar, Amit, Blalock, J. Edwin·2015·Matrix Biology
DOI 10.1016/j.matbio.2015.01.016PMC PMC4838901
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Abstract

Matrikines originate from the fragmentation of extracellular matrix proteins and regulate cellular activities by interacting with specific receptors. Matrikines are implicated in inflammation, immune responses, organ development, wound repair, angiogenesis, atherosclerosis, tumor progression and metastasis due to their ability to alter cellular migration, chemotaxis, and mitogenesis. Matrix metalloproteinases (MMPs) degrade extracellular matrix components under normal circumstances and in disease processes. Of the 20 MMPs identified, MMP-1, MMP-2, MMP-8, MMP-9, and MMP-12 have been implicated in regulating the matrikines Val-Gly-Val-Ala-Pro-Gly (elastin peptide) and proline-glycine-proline (PGP). Elastin peptide fragments are generated by elastolytic enzymes and have implications in atherosclerosis, neovascularization, chronic obstructive pulmonary disease, skin disease, as well as tumor invasion and spread. PGP is produced through a multistep pathway that liberates the tripeptide fragment from extracellular collagen. PGP is best described for its role in neutrophil chemotaxis and is implicated in the pathogenesis of corneal ulcers and in chronic lung conditions. In chronic cigarette smoke related lung disease, the PGP pathway can become a self-propagating cycle of inflammation through cigarette-smoke mediated inhibition of leukotriene A4 hydrolase, the enzyme responsible for degrading PGP and halting acute inflammation. This review highlights the roles of MMPs in generating these important matrikines.

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  • Unrestricted release of PGP motives in the transplantation of organs such as heart and lung mediates chronic inflammation and rejection.

    “Unrestricted release of PGP motives in the transplantation of organs such as heart and lung mediate chronic inflammation and rejection [102, 103].”

    From Immunogenicity of decellularized extracellular matrix scaffolds: a bottleneck in tissue engineering and regenerative medicine (2023) · cites this paper as [102]

    The “PGP as a matrikine” section reports a pathway generating PGP in chronic lung-transplant rejection and describes PGP-mediated neutrophil chemotaxis. It does not address heart transplantation or establish that unrestricted PGP release causes transplant rejection. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • MMPs degrade collagens and expose cryptic three-peptide motives PGP, which trigger CXCR2 receptors of neutrophils and orchestrate their chemotaxis and interplay with adaptive immunity.

    “MMPs per se degrade collagens and expose cryptic three-peptide motives PGP (Pro-Gly-Pro), which trigger CXCR2 receptors of neutrophils and orchestrate their chemotaxis and interplay with adaptive immunity.”

    From Immunogenicity of decellularized extracellular matrix scaffolds: a bottleneck in tissue engineering and regenerative medicine (2023) · cites this paper as [102]

    The ‘PGP as a matrikine’ section (page not provided) says collagen-derived PGP is generated through a pathway involving MMP-8, MMP-9 and prolyl endopeptidase, and that PGP/AcPGP stimulates neutrophil chemotaxis through CXCR2. The cited passages do not establish that PGP orchestrates an interplay with adaptive immunity; they also describe its release as a multistep process, rather than MMP action alone. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • Some cryptic laminin motives induce macrophage and neutrophil chemotaxis and upregulate MMPs activity.

    “Besides, some cryptic laminin motives induce macrophage and neutrophil chemotaxis and upregulate MMPs activity [102].”

    From Immunogenicity of decellularized extracellular matrix scaffolds: a bottleneck in tissue engineering and regenerative medicine (2023) · cites this paper as [102]

    In “Other bioactive ECM fragments generated by MMPs” (page not provided), the review says a cryptic laminin α5 peptide recruits PMNs (neutrophils) and macrophages. It also says the peptide induces MMP-9 release from immune cells, but does not establish increased MMP activity or the same effect for multiple laminin motifs. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

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Authors
Wells, J. M., Gaggar, A., & Blalock, J. E.
Affiliations
University of Alabama at Birmingham (US)
Corresponding author
Wells, J. Michael
ORCID
Venue
Matrix Biology
Publisher
Elsevier BV
Published
2015-05
Volume
44-46
Pages
122-129
ISSN
0945-053X (ISSN-L)
DOI
10.1016/j.matbio.2015.01.016
PMC
PMC4838901
OpenAlex
W2035683946
Cited by
263
References
75
Citations by year
2026: 19 · 2025: 15 · 2024: 25 · 2023: 35 · 2022: 15 · 2021: 30 · 2020: 33 · 2019: 23 · 2018: 20 · 2017: 21 · 2016: 17 · 2015: 10
FWCI
2.21
Type
journal article
Language
en
Open access
Licence
Locations
  • Matrix Biology (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Heart, Lung, and Blood Institute
  • National Institutes of Health
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
  • Health Sciences › Medicine › Rheumatology › Bone and Dental Protein Studies
  • Health Sciences › Medicine › Rehabilitation › Wound Healing and Treatments
Keywords
matrikines, matrix metalloproteinases, elastin peptides, extracellular matrix degradation, MMP-1, MMP-2, MMP-8, MMP-9, MMP-12, neutrophil chemotaxis, cigarette smoke, leukotriene A4 hydrolase, corneal ulcer, atherosclerosis, tumor invasion, chronic obstructive pulmonary disease, inflammation
MeSH terms
Animals, Inflammation, Oligopeptides, Peptides, Extracellular Matrix Proteins, Matrix Metalloproteinases

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