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

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MMP generated matrikines

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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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The Role of Extracellular Matrix in Corneal Wound Healing
Yamanaka, O., Sumioka, T., & Saika, S. (2013) · Cornea · doi:10.1097/ico.0b013e3182a4786b · Cited by 15
Retracted
Molecular Mechanisms of Stress-Responsive Changes in Collagen and Elastin Networks in Skin
Aziz, J., Shezali, H., Radzi, Z., Yahya, N. A., Abu Kassim, N. H., Czernuszka, J., & Rahman, M. T. (2016) · Skin Pharmacology and Physiology · doi:10.1159/000447017 · Cited by 7,323
Requirement for Macrophage Elastase for Cigarette Smoke-Induced Emphysema in Mice
Hautamaki, R. D., Kobayashi, D. K., Senior, R. M., & Shapiro, S. D. (1997) · Science · doi:10.1126/science.277.5334.2002 · Cited by 1,470
Angiostatin induces and sustains dormancy of human primary tumors in mice
O’Reilly, M. S., Holmgren, L., Chen, C., & Folkman, J. (1996) · Nature Medicine · doi:10.1038/nm0696-689 · Cited by 1,170
Effects of Angiogenesis Inhibitors on Multistage Carcinogenesis in Mice
Bergers, G., Javaherian, K., Lo, K.-M., Folkman, J., & Hanahan, D. (1999) · Science · doi:10.1126/science.284.5415.808 · Cited by 988
Control of matrix metalloproteinase catalytic activity
Ra, H.-J., & Parks, W. C. (2007) · Matrix Biology · doi:10.1016/j.matbio.2007.07.001 · Cited by 669
Antielastin autoimmunity in tobacco smoking–induced emphysema
Lee, S., Goswami, S., Grudo, A., Song, L., Bandi, V., Goodnight-White, S., Green, L., Hacken, J. B., Huh, J., Bakaeen, F. G., et al. (2007) · Nature Medicine · doi:10.1038/nm1583 · Cited by 595
Physiological levels of tumstatin, a fragment of collagen IV α3 chain, are generated by MMP-9 proteolysis and suppress angiogenesis via αVβ3 integrin
Hamano, Y., Zeisberg, M., Sugimoto, H., Lively, J. C., Maeshima, Y., Yang, C., Hynes, R. O., Werb, Z., Sudhakar, A., & Kalluri, R. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00133-8 · Cited by 566
Biochemistry of tropoelastin
Vrhovski, B., & Weiss, A. S. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2580001.x · Cited by 544
Chemotactic activity of elastin-derived peptides.
Senior, R. M., Griffin, G. L., & Mecham, R. P. (1980) · Journal of Clinical Investigation · doi:10.1172/jci109926 · Cited by 534

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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: Wells, J. Michael
Gaggar, Amit
Blalock, J. Edwin
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: hybrid
doi.org
Licence: cc-by-nc-nd
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by-nc-nd/4.0/ (vor)
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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Bone and Dental Protein Studies
Health Sciences › Medicine › Surgery › 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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