MMP8 Gene: Matrix Metallopeptidase 8 (Neutrophil Collagenase)
Genomic, functional, and clinical insights into MMP8, a key collagenase involved in inflammation, tissue remodeling, and cancer.
Gene Information Card
| Symbol | MMP8 |
|---|---|
| Full Name | Matrix metallopeptidase 8 |
| Gene Type | Protein-coding |
| Chromosomal Location | 11q22.2 |
| NCBI Gene ID | 4317 ncbi.nlm.nih.gov/gene/4317 |
| Ensembl ID | ENSG00000118113 |
| UniProt ID | P22894 |
| OMIM ID | 120251 |
| HGNC ID | 7175 |
| Aliases | CLG1, HNC, MMP-8, PMNL-CL, Collagenase 2 |
Description
MMP8 (Matrix Metallopeptidase 8), also known as neutrophil collagenase or collagenase 2, is a zinc-dependent endopeptidase that degrades fibrillar collagens (types I, II, III) and other extracellular matrix components. It is primarily stored in neutrophil granules and released upon inflammation. MMP8 plays a dual role in cancer, showing both pro- and anti-tumorigenic effects depending on the context. It is also involved in inflammatory diseases, wound healing, and tissue remodeling.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Periodontitis | MMP8 degrades collagen in periodontal tissue; elevated levels in gingival crevicular fluid correlate with disease severity. | Multiple clinical studies; OMIM 120251 |
| Cancer (e.g., breast, lung, oral) | MMP8 can promote tumor invasion by ECM degradation, but in some cancers it has anti-tumorigenic effects via immune modulation. | COSMIC; PubMed studies |
| Rheumatoid Arthritis | MMP8 contributes to cartilage and bone destruction in inflamed joints. | OMIM; PubMed |
| Coronary Artery Disease | MMP8 is involved in atherosclerotic plaque remodeling and instability. | PubMed |
| Liver Fibrosis | MMP8 degrades collagen in liver, potentially affecting fibrosis progression. | PubMed |
| Asthma | MMP8 may contribute to airway remodeling and inflammation. | PubMed |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Bone Marrow | High | High |
| Spleen | Medium | Medium |
| Lung | Low | Low |
| Liver | Low | Low |
| Kidney | Low | Low |
| Blood | High | High |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| Neutrophils | High | Primary source; stored in granules |
| Macrophages | Medium | Induced upon activation |
| Fibroblasts | Low | Induced by cytokines |
| Endothelial cells | Low | Induced under inflammatory conditions |
| Cancer cell lines (e.g., MDA-MB-231) | Variable | Expression correlates with invasiveness |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| rs1940475 (K87E) | Missense | ~30% (global) | Alters enzyme activity; associated with periodontitis and cancer risk |
| rs11225395 (promoter) | Promoter variant | ~20% | Affects transcription; linked to cancer susceptibility |
| rs2010877 (intronic) | Intronic | ~15% | Potential regulatory effect; disease association unclear |
| Somatic mutations in cancer | Various | Low (<5%) | May affect catalytic activity or stability; found in some tumors |
Mutation functional classification
Loss of Function (LOF)
Loss-of-function mutations reduce collagenolytic activity, potentially impairing tissue remodeling and immune response. In cancer, loss may reduce tumor invasion but can also alter immune surveillance.
Gain of Function (GOF)
Gain-of-function mutations increase enzyme activity, enhancing ECM degradation and promoting tumor invasion or inflammatory tissue destruction.
Dominant Negative (DN)
Dominant-negative effects are rare; mutant MMP8 may interfere with dimerization or substrate binding, reducing overall activity.
View complete mutation data：
Gene Ontology (GO)
| • metalloendopeptidase activity | • collagen binding |
| • zinc ion binding | • calcium ion binding |
| • extracellular matrix disassembly | • proteolysis |
| • collagen catabolic process | • inflammatory response |
| • neutrophil degranulation |
Pathways
• Matrix metalloproteinase pathway
• Collagen degradation pathway
• Neutrophil degranulation pathway
• TNF signaling pathway
• IL-17 signaling pathway
Protein Summary
MMP8 is a 467-amino acid protein with a signal peptide, prodomain, catalytic domain containing zinc-binding motif, and hemopexin-like domain. It is synthesized as a zymogen and activated by proteolytic cleavage. The enzyme degrades fibrillar collagens and is inhibited by tissue inhibitors of metalloproteinases (TIMPs). MMP8 is stored in neutrophil granules and released upon inflammatory stimuli. It also regulates chemokine activity and immune cell migration.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| MMP8 Knockout HEK293 Cell Line | EDJ-KQ5221 | Human | 4317 | Details Get a Quote |
| MMP8 Knockout HeLa Cell Line | EDJ-KQ53884 | Human | 4317 | Details Get a Quote |
| MMP8 Knockout A-549 Cell Line | EDJ-KQ62375 | Human | 4317 | Details Get a Quote |
| MMP8 Knockout HCT 116 Cell Line | EDJ-KQ70845 | Human | 4317 | Details Get a Quote |
