Gelatinase B functions as regulator and effector in leukocyte biology
Abstract
Matrix metalloproteinases (MMPs) form a family of enzymes with major actions in the remodeling of extracellular matrix (ECM) components. Gelatinase B (MMP-9) is the most complex family member in terms of domain structure and regulation of its activity. Gelatinase B activity is under strict control at various levels: transcription of the gene by cytokines and cellular interactions; activation of the pro-enzyme by a cascade of enzymes comprising serine proteases and other MMPs; and regulation by specific tissue inhibitors of MMPs (TIMPs) or by unspecific inhibitors, such as α2-macroglobulin. Thus, remodeling ECM is the result of the local protease load, i.e., the net balance between enzymes and inhibitors. Glycosylation has a limited effect on the net activity of gelatinase B, and in contrast to the all-or-none effect of enzyme activation or inhibition, it results in a higher-level, fine-tuning effect on the ECM catalysis by proteases in mammalian species. Fast degranulation of considerable amounts of intracellularly stored gelatinase B from neutrophils, induced by various types of chemotactic factors, is another level of control of activity. Neutrophils are first-line defense leukocytes and do not produce gelatinase A or TIMP. Thus, neutrophils contrast sharply with mononuclear leukocytes, which produce gelatinase A constitutively, synthesize gelatinase B de novo after adequate triggering, and overproduce TIMP-1. Gelatinase B is also endowed with functions other than cleaving the ECM. It has been shown to generate autoimmune neo-epitopes and to activate pro-IL-1β into active IL-1β. Gelatinase B ablation in the mouse leads to altered bone remodeling and subfertility, results in resistance to several induced inflammatory or autoimmune pathologies, and indicates that the enzyme plays a crucial role in development and angiogenesis. The major human neutrophil chemoattractant, IL-8, stimulates fast degranulation of gelatinase B from neutrophils. Gelatinase B is also found to function as a regulator of neutrophil biology and to truncate IL-8 at the aminoterminus into a tenfold more potent chemokine, resulting in an important positive feedback loop for neutrophil activation and chemotaxis. The CXC chemokines GRO-α, CTAP-III, and PF-4 are degraded by gelatinase B, whereas the CC chemokines MCP-2 and RANTES are not cleaved.
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Removal of the ELR sequence by matrix metalloproteinase 9 proteolysis causes, in the case of CXCL8, a 10-fold increase in its activity.
“Removal of this sequence by matrix metalloproteinase 9 (MMP9) proteolysis causes, in the case of CXCL8, a 10-fold increase in its activity.49”
From The Innate Immune System in Acute and Chronic Wounds (2016) · cites this paper as [49]
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“Removal of this sequence by matrix metalloproteinase 9 (MMP9) proteolysis causes, in the case of CXCL8, a 10-fold increase in its activity.(49) This contrasts with the effect of proteolysis on later stages of wound healing, where MMP9 may cause breakdown of protein factors needed to orchestrate wound closure.”
BackgroundNeutrophils: important contributors to tumor progression and metastasis
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- Authors
- Opdenakker, G., Van den Steen, P. E., Dubois, B., Nelissen, I., Van Coillie, E., Masure, S., Proost, P., & Van Damme, J.
- Affiliations
- KU Leuven (BE)
- Laboratory of Molecular Immunology, Rega Institute, University of Leuven , Leuven, Belgium
- Corresponding author
- Opdenakker, Ghislain
- Venue
- Journal of Leukocyte Biology
- Publisher
- Oxford University Press (OUP)
- Published
- 2001-06-01
- Volume
- 69
- Issue
- 6
- Pages
- 851-859
- ISSN
- 0741-5400 (ISSN-L)
- 1938-3673
- OpenAlex
- W2135423586
- Cited by
- 553
- References
- 74
- Citations by year
- 2026: 4 · 2025: 9 · 2024: 11 · 2023: 15 · 2022: 12 · 2021: 14 · 2020: 14 · 2019: 15 · 2018: 8 · 2017: 16 · 2016: 20 · 2015: 16 · 2014: 23 · 2013: 21 · 2012: 39
- FWCI
- 10.83
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Leukocyte Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Scientific Research
- Charcot Foundation, Belgian Federation against Cancer
- Cancer Research Foundation of Fortis Insurances AB
- Foundation for Research on Multiple Sclerosis
- University of Oxford
- Deutsches Krebs for schungszentrum, Heidelberg
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
- Keywords
- MMP-9, matrix metalloproteinases, extracellular matrix remodeling, neutrophil degranulation, neutrophil activation, chemotaxis, interleukin-8, chemokine degradation, tissue inhibitors of metalloproteinases, TIMP-1, alpha2-macroglobulin, glycosylation, autoimmunity, bone remodeling, angiogenesis, leukocyte biology, MMP-8, MMP-14, MMP-1
- MeSH terms
- Autoimmune Diseases, Chromosomes, Human, Pair 20, Enzyme Activation, Enzyme Induction, Extracellular Matrix, Humans, Leukocytes, Leukocytes, Mononuclear, Neoplasms, Neutrophils, Organ Specificity, Phenotype, Protein Processing, Post-Translational, Cytokines, Protein Structure, Tertiary, Chemokines, Tissue Inhibitor of Metalloproteinase-1, Matrix Metalloproteinase 2, Matrix Metalloproteinase 9, Macromolecular Substances
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