ArticleMolecular & cellular proteomics : MCP2009
MMP-9 sheds the beta2 integrin subunit (CD18) from macrophages.
Article in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed.
- Changes in Soluble CD18 in Murine Autoimmune Arthritis and Rheumatoid Arthritis Reflect Disease Establishment and Treatment Response.PloS one · 2016Trial
- Adipose-Derived Stem Cell Exosomes in Diabetic Wound Repair: Molecular Crosstalk, Bioengineering Strategies, and Translational Challenges.Stem cells international · 2026Review
- 1-Deoxynojirimycin Combined with Theaflavins Targets PTGS2/MMP9 to Exert a Synergistic Hypoglycemic Effect.Nutrients · 2025Article
- Large soluble CD18 complexes with exclusive ICAM-1-binding properties are shed during immune cell migration in inflammation.Journal of translational autoimmunity · 2025Article
- Identification of circulating T-cell immunoglobulin and mucin domain 4 as a potential biomarker for coronary heart disease.MedComm · 2023Article
- Novel Matrix Metalloproteinase-9 (MMP-9) Inhibitors in Cancer Treatment.International journal of molecular sciences · 2023Review
- MMP-9 reinforces radiation-induced delayed invasion and metastasis of neuroblastoma cells through second-signaling positive feedback with NFκB via both ERK and IKK activation.Cell biology and toxicology · 2023Article
- Review
- MMP9: A Tough Target for Targeted Therapy for Cancer.Cancers · 2022Review
- Global Proteomic Analyses Reveals Abnormal Immune Regulation in Patients With New Onset Ankylosing Spondylitis.Frontiers in immunology · 2022Article
- Whole patient knowledge modeling of COVID-19 symptomatology reveals common molecular mechanisms.Frontiers in molecular medicine · 2022Article
- Computational study of effective matrix metalloproteinase 9 (MMP9) targeting natural inhibitors.Aging · 2021Article
- Modulation of Microenvironment Signals by Proteolytic Shedding of Cell Surface Extracellular Matrix Receptors.Frontiers in cell and developmental biology · 2021Review
- Intravascular Crawling of Patrolling Monocytes: A Lèvy-Like Motility for Unique Search Functions?Frontiers in immunology · 2021Review
- Innate Immunity Effector Cells as Inflammatory Drivers of Cardiac Fibrosis.International journal of molecular sciences · 2020Review
- The Impact of Matrix Metalloproteinase-9 on the Sequential Steps of the Metastatic Process.International journal of molecular sciences · 2020Review
- Matrix Metalloproteases as Influencers of the Cells' Social Media.International journal of molecular sciences · 2019Review
- Matrix metalloproteinases in the CNS: interferons get nervous.Cellular and molecular life sciences : CMLS · 2019Review
- Matrix metalloproteinases in emphysema.Matrix biology : journal of the International Society for Matrix Biology · 2018Review
- Matrix Metalloproteinase-9 (MMP-9) as a Cancer Biomarker and MMP-9 Biosensors: Recent Advances.Sensors (Basel, Switzerland) · 2018Review
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Activated macrophages are essential effectors of immunity and a rich source of matrix metalloproteinase-9 (MMP-9; gelatinase B). To search for cellular substrates of the enzyme, we subjected wild-type macrophages and macrophages expressing an autoactivating form of pro-MMP-9 (M9A macrophages) to proteomics analysis. Two-dimensional liquid chromatography together with tandem mass spectrometry identified 467 proteins in medium conditioned by M9A and/or wild-type macrophages. Subtractive proteomics identified 18 candidate MMP-9 substrates. Biochemical studies confirmed that two transmembrane proteins, beta(2) integrin subunit (CD18) and amyloid protein precursor (APP), were enriched in the medium of M9A macrophages. To identify potential cleavage sites, we synthesized an overlapping library of peptides that spanned 60 residues of the ectodomain and transmembrane domain of beta(2) integrin. Active MMP-9 cleaved a single peptide, ECVKGPNVAAIVGGT, at residues corresponding to Ala(705) and Ile(706) of the beta(2) integrin. Peptides corresponding to this cleavage site were detected by tandem mass spectrometric analysis only in medium from M9A macrophages, strongly supporting the proposal that beta(2) integrin is shed by autoactivating MMP-9. Our observations indicate that subtractive proteomics in concert with peptide substrate mapping is a powerful approach for identifying proteolytic substrates and suggest that MMP-9 plays previously unsuspected roles in the regulation and shedding of beta(2) integrin.
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Registered trials
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