| 2005 |
MMP-10 activates pro-MMP-1, and both MMP-10 and MMP-1 are required for capillary tube regression in 3D collagen matrices; serine proteases (plasma kallikrein, trypsin, neutrophil elastase, cathepsin G, tryptase, chymase) activate pro-MMP-10, which in turn activates MMP-1 to drive collagen proteolysis, tube collapse, and endothelial cell apoptosis. siRNA silencing of MMP-10 markedly delayed regression, while adenoviral overexpression of MMP-10 accelerated it. |
siRNA knockdown, adenoviral overexpression, in vitro capillary tube regression assay in 3D collagen matrices, zymography, biochemical MMP activation assays |
Journal of cell science |
High |
15870107
|
| 2004 |
Active stromelysin-2 (MMP-10) degrades laminin-5 in vitro, and constitutively active MMP-10 expressed in keratinocytes in vivo disrupts laminin-5 deposition, mislocalizes β1-integrins and phosphorylated focal adhesion kinase at the wound edge, and increases keratinocyte apoptosis, indicating MMP-10 controls keratinocyte migration through regulated matrix degradation. |
Transgenic mouse model (constitutively active MMP-10 in keratinocytes), in vitro laminin-5 degradation assay, immunohistochemistry, skin wound-healing model |
Molecular biology of the cell |
High |
15371548
|
| 2012 |
Crystal structure of TIMP-1 bound to the MMP-10 catalytic domain solved at 1.9 Å; TIMP-1 inhibits MMP-10cd with Ki = 1.1 × 10⁻⁹ M and TIMP-2 with Ki = 5.8 × 10⁻⁹ M, both ~10-fold weaker than their inhibition of the closely related MMP-3. Structural comparison with MMP-3·TIMP-1 revealed interface differences explaining the differential binding. |
X-ray crystallography (1.9 Å resolution, molecular replacement), kinetic inhibition assays (multiple approaches), comparative structural analysis |
The Journal of biological chemistry |
High |
22427646
|
| 2013 |
MMP10 is required for macrophage migration and invasion; RNAi silencing of MMP10 in primary macrophages markedly reduced migration (reversed by exogenous active MMP10 protein), and Mmp10⁻/⁻ bone marrow-derived macrophages showed significantly reduced migration over fibronectin and impaired invasion into Matrigel supplemented with fibronectin. |
Time-lapse microscopy, RNAi silencing, Mmp10⁻/⁻ knockout macrophages, exogenous recombinant MMP10 rescue, 2D migration and Matrigel invasion assays |
PloS one |
High |
23691065
|
| 2016 |
MMP10 moderates macrophage inflammatory activation: Mmp10⁻/⁻ mice showed ~3-fold more macrophages in infected lungs, elevated M1 markers and reduced M2 markers; global gene expression showed infection-induced transcriptional changes persisted in Mmp10⁻/⁻ macrophages. Adoptive transfer of wild-type BMDMs normalized morbidity in Mmp10⁻/⁻ recipients, demonstrating the protective effect is macrophage-derived MMP10. |
Mmp10⁻/⁻ knockout mice, Pseudomonas aeruginosa infection model, adoptive transfer of BMDMs, genome-wide gene expression analysis, flow cytometry for macrophage markers |
Journal of immunology |
High |
27316687
|
| 2015 |
MMP-10 from alternatively activated (M2) resident macrophages regulates collagenolytic activity in wounds by controlling expression of metallocollagenases MMP-8 and MMP-13 (particularly MMP-13); Mmp10⁻/⁻ wounds showed increased collagen deposition, skin stiffness, and reduced collagenolytic activity. Ablation and adoptive transfer experiments confirmed the effect is macrophage-derived. |
Mmp10⁻/⁻ knockout mice, wound healing model, macrophage ablation and adoptive transfer, collagen assays, biomechanical testing, cell-based models |
The Journal of investigative dermatology |
High |
25927164
|
| 2012 |
Loss of MMP10 exacerbates DSS-induced colitis and impairs resolution of inflammation; MMP10 is produced predominantly by infiltrating myeloid cells in murine and human colitis, and bone marrow transplant experiments confirmed that bone marrow-derived MMP10 contributes to disease severity. Mmp10⁻/⁻ mice had higher propensity for dysplasia after repeated DSS exposure. |
Mmp10⁻/⁻ knockout mice, DSS colitis model, bone marrow transplantation, immunohistochemistry, histological scoring |
Laboratory investigation |
High |
23044923
|
| 2009 |
TGF-β transcriptionally induces MMP-10 in mammary epithelial cells through MEF2A: TGF-β promotes proteasome-dependent degradation of class IIa HDACs, leading to increased acetylation of MEF2A and core histones around the MEF2 site of the MMP-10 promoter, driving transactivation. Knockdown of MEF2A reduced MMP-10 induction; knockdown of class IIa HDACs increased it. |
Reporter gene (luciferase) assays, siRNA knockdown, overexpression experiments, chromatin immunoprecipitation (ChIP), real-time PCR, proteasome inhibitor experiments |
Oncogene |
High |
19935709
|
| 2005 |
Zinc finger protein ZNF267 is a negative transcriptional repressor of MMP-10: ZNF267 is constitutively nuclear, its KRAB-A domain mediates repressor activity, it binds the MMP-10 promoter region (demonstrated by ChIP), and its overexpression reduces MMP-10 reporter activity in hepatic stellate cells. |
Microarray, RNase protection assay, reporter gene assay, chromatin immunoprecipitation (ChIP), GAL4 fusion constructs, fluorescent protein localization |
Biochemical and biophysical research communications |
Medium |
16054593
|
| 2010 |
MMP-10 transcription in endothelial cells is induced by VEGF in a time- and dose-dependent manner; MMP-10 expression is mediated by the Ets-1 transcription factor but not ERP/NET/ELK3, and via PI3K and MAPK signaling pathways. MMP-10 siRNA inhibited VEGF-induced endothelial cell migration and tube formation in vitro, and vessel formation in matrigel plugs in vivo. |
Quantitative RT-PCR, siRNA knockdown, migration and tube formation assays, in vivo matrigel plug assay, pharmacological inhibitors of PI3K and MAPK, luciferase reporter for Ets-1 |
Journal of cellular physiology |
Medium |
20432469
|
| 2011 |
C-reactive protein (CRP) promotes MMP-10 expression and activity in cardiomyocytes via c-Raf/MEK/ERK and JAK1/ERK signaling pathways, with DNA binding sites for AP-1 and STAT3 in the nucleus mediating the effect; blocking ERK1/2 (U0126) or JAK1 (piceatannol) significantly decreased CRP-induced MMP-10 expression. |
Real-time PCR, Western blot, casein zymography, pharmacological pathway inhibitors, phospho-specific antibodies, cell culture |
Cellular signalling |
Medium |
22142512
|
| 2011 |
β1 integrin signaling via the ERK/MAPK pathway upregulates MMP-10 mRNA and protein expression in human lymphatic endothelial cells, and MMP-10 is required for collagen I-induced lymphatic tubulogenesis; knockdown of MMP-10 impaired tubulogenesis. |
Protein-based screening, siRNA knockdown, ERK/MAPK pathway analysis, lymphatic endothelial cell tubulogenesis assay |
Matrix biology |
Medium |
21406228
|
| 2014 |
MMP-10 deficiency impairs skeletal muscle regeneration after injury: Mmp10⁻/⁻ muscles displayed reduced endothelial cell recruitment, diminished extracellular matrix proteins, decreased collagen deposition, decreased fiber size, and delayed regeneration. MMP-10 mRNA silencing in vivo reduced muscle regeneration, while recombinant MMP-10 accelerated repair. MMP-10-mediated muscle repair was associated with VEGF/Akt signaling. |
Mmp10⁻/⁻ knockout mice, notexin injury model, mdx muscular dystrophy model, siRNA in vivo silencing, recombinant MMP-10 treatment, immunohistochemistry, Western blot |
Stem cells |
High |
24123596
|
| 2014 |
CXCR4/SDF1-regulated muscle repair is dependent on MMP-10 activity: siRNA silencing of SDF1 or CXCR4 in injured muscles impaired regeneration, and MMP-10 was identified as the downstream effector of this axis. SDF1 ligand addition accelerated repair, and CXCR4 antagonism (AMD3100) delayed it, linking the CXCR4/SDF1 pathway to MMP-10-dependent matrix remodeling in muscle repair. |
In vivo siRNA silencing of SDF1, CXCR4, pharmacological CXCR4 antagonism (AMD3100), notexin injury model, functional and histological analysis |
Stem cells and development |
Medium |
24548137
|
| 2014 |
MMP-10 functions are required for efficient tissue repair after hind limb ischemia; Mmp10⁻/⁻ mice showed delayed reperfusion, increased necrosis, and excessive neutrophil/macrophage infiltration. MMP-10 deficiency led to higher Cxcl1 mRNA and protein levels, revealing a transcriptional inhibitory role for MMP-10 on Cxcl1. Injection of MMP-10 into Mmp10⁻/⁻ mice rescued the phenotype. |
Mmp10⁻/⁻ knockout mice, femoral artery excision ischemia model, small animal PET, immunohistochemistry, siRNA knockdown of MMP-10 in vivo, recombinant MMP-10 rescue |
FASEB journal |
High |
25414484
|
| 2021 |
During secondary fracture healing, MMP-10 is expressed by hematopoietic cells and is required for cartilage resorption; Mmp10⁻/⁻ mice showed delayed cartilage resorption and TRAP-positive cell accumulation at 14 days post-fracture. The phenotype was rescued by wild-type bone marrow transplant. MMP-10 functions in macrophages to promote proMMP-9 processing and gelatinase activity required for endochondral ossification. |
Mmp10⁻/⁻ knockout mice, fracture healing model, bone marrow transplantation rescue, proMMP-9 processing assay, TRAP staining, immunohistochemistry |
Journal of bone and mineral research |
High |
34173256
|
| 2018 |
MMP10 functions as a thrombolytic and neuroprotective agent in ischemic stroke; recombinant MMP10 reduced infarct size in a thrombin-induced middle cerebral artery occlusion model, and in vitro MMP10 reduced tPA-promoted endothelial ionic permeability, preserved claudin-5, decreased ERK1/2 activation, prevented tPA-mediated neuronal excitotoxicity and calcium influx. These effects were blocked by an anti-MMP10 monoclonal antibody. |
In vivo murine ischemic stroke model, brain endothelial cell and neuron cultures, Western blot for claudin-5, ERK1/2 phosphorylation, calcium imaging, anti-MMP10 antibody neutralization |
Cardiovascular research |
Medium |
28379489
|
| 2018 |
MMP10 moderates TLR7-induced immune tolerance in skin macrophages: Mmp10⁻/⁻ mice failed to develop hypo-responsiveness to repeated TLR7 (imiquimod) stimulation, with failure to upregulate negative TLR regulators (TNFAIP3, IRAK3) and immunosuppressive cytokines (IL-10, TGFβ1). In vitro, prior IMQ exposure made wild-type BMDMs refractory to re-stimulation but not Mmp10⁻/⁻ macrophages. |
Mmp10⁻/⁻ knockout mice, in vivo TLR7 tolerance model, BMDM cultures, cytokine/gene expression analysis |
Frontiers in immunology |
Medium |
30564235
|
| 2020 |
Recombinant MMP-10 induces osteogenic, fibrotic, and inflammatory markers in aortic valve interstitial cells (interleukin-1β, α-SMA, vimentin, collagen, BMP-4, Sox9, osteopontin, BMP-9, and Smad 1/5/8) and promotes cell mineralization via Akt phosphorylation; these effects were prevented by TIMP-1 or an anti-MMP-10 antibody. MMP-10 co-localizes with calcification markers (Runx2, SOX9) in stenotic aortic valves. |
In vitro treatment of primary human aortic valve interstitial cells with recombinant MMP-10, TIMP-1 inhibition, anti-MMP-10 antibody neutralization, Akt phosphorylation assay, calcification (mineralization) assay, immunohistochemistry |
Arteriosclerosis, thrombosis, and vascular biology |
Medium |
32188274
|
| 2017 |
MMP10 facilitates clearance of long multiwalled carbon nanotubes (MWCNTs) from lung and moderates macrophage inflammatory activation and survival; Mmp10⁻/⁻ mice showed impaired pulmonary clearance of MWCNTs and reduced macrophage survival, with enhanced caspase-3-dependent cell death and elevated IL-6 and IL-1β in Mmp10⁻/⁻ macrophages. |
Mmp10⁻/⁻ knockout mice, oropharyngeal aspiration of MWCNTs, alveolar macrophage and BMDM cultures, caspase-3 assay, cytokine analysis, gene expression |
International journal of nanomedicine |
Medium |
28223796
|
| 2022 |
Directed evolution of yeast-displayed TIMP-1 yielded variants highly selective for MMP-3 over MMP-10. Protein crystal structures and models of MMP-3-selective TIMP-1 variants bound to MMP-3 and counter-target MMP-10 showed that structural alterations in N- and C-terminal TIMP-1 domains create favorable interactions with MMP-3 and disrupt unique interactions with MMP-10, defining the binding interface determinants of stromelysin selectivity. |
Directed evolution (yeast display, counter-selective screening), X-ray crystallography of protein complexes, structural modeling |
The Journal of biological chemistry |
High |
35101440
|
| 2011 |
CHF1/Hey2 is a direct transcriptional repressor of MMP10: loss or knockdown of CHF1/Hey2 in vascular smooth muscle cells increases MMP10 expression and activity. A 2.5 kb MMP10 promoter region contains 12 E-boxes mediating constitutive activity and CHF1/Hey2 repression; mutation of these E-boxes abolished repression and unmasked an activator function for CHF1/Hey2. |
Luciferase reporter assays, siRNA knockdown of CHF1/Hey2, E-box mutagenesis, gene expression analysis in smooth muscle cells |
Biochemical and biophysical research communications |
Medium |
22079635
|
| 2016 |
AJUBA promotes migration and invasion of esophageal squamous cell carcinoma cells by upregulating MMP10 and MMP13 expression through activation of the ERK1/2 signaling pathway; AJUBA knockdown reduced migration/invasion and decreased MMP10/MMP13 levels, while AJUBA overexpression had the opposite effect, both in vitro and in vivo. |
RNA sequencing, siRNA knockdown and overexpression of AJUBA, Western blot, migration and invasion assays, in vivo xenograft models, ERK1/2 pathway analysis |
Oncotarget |
Medium |
27172796
|
| 2014 |
YY1 suppresses PDAC invasion and metastasis by downregulating MMP10 in a MUC4/ErbB2/p38/MEF2C-dependent mechanism: YY1 expression negatively correlated with MMP10 levels; YY1 overexpression suppressed invasion/metastasis and reduced MMP10, while YY1 knockdown enhanced them. Luciferase assays and pathway blockage experiments placed MMP10 downstream of YY1/MUC4/ErbB2/p38/MEF2C. |
Digital gene expression sequencing, siRNA knockdown, overexpression, luciferase reporter assays, signaling pathway inhibitors, in vivo xenograft and tail vein metastasis models |
Molecular cancer |
Medium |
24884523
|
| 2009 |
IL-6 regulates MMP-10 expression via the JAK2/STAT3 pathway in lung adenocarcinoma cells: IL-6 moderately reduced MMP-10 mRNA but significantly enhanced MMP-10 protein. The JAK2 inhibitor AG490 blocked both IL-6-induced STAT3 upregulation and the bidirectional IL-6 effects on MMP-10 mRNA and protein levels. |
Real-time RT-PCR, Western blot, pharmacological JAK2 inhibition (AG490), A549 cell culture |
Anticancer research |
Low |
20032397
|
| 1997 |
Recombinant murine stromelysin-2 (MMP-10) produced in COS cells is secreted as a proenzyme that undergoes autocatalytic processing upon addition of the organomercurial salt APMA, establishing that MMP-10 is an autocatalytically activatable metalloproteinase. |
COS cell expression of recombinant protein, organomercurial (APMA)-induced autocatalytic processing assay |
Gene |
Medium |
9427548
|
| 2022 |
MMP10 is required for proMMP-9 processing in macrophages during bone fracture healing; Mmp10⁻/⁻ macrophages showed reduced gelatinase activity and lack of proMMP-9 processing, contributing to impaired cartilage resorption and delayed vascular invasion during endochondral ossification. |
Mmp10⁻/⁻ knockout mice, wild-type bone marrow transplant rescue, proMMP-9 processing assay, gelatinase activity assay, fracture healing histology |
Journal of bone and mineral research |
High |
34173256
|
| 2023 |
MMP10 alleviates non-alcoholic steatohepatitis by promoting M2 macrophage polarization via STAT3 signaling: PPARγ binds the MMP10 promoter and upregulates MMP10 expression upon IL-4 stimulation. MMP10 overexpression activated downstream STAT3 signaling to induce M2 polarization, reducing pro-inflammatory IL-1β and TNF-α and increasing IL-10. MMP10-KO mice showed worse NASH phenotype on HFD. |
MMP10-OE and MMP10-KO mice on HFD, PPARγ-OE, ChIP (PPARγ binding to MMP10 promoter), Kupffer cell transfection, IL-4 stimulation, STAT3 pathway analysis, HFD NASH model |
International immunopharmacology |
High |
37844469
|
| 2022 |
MMP-10 knockdown in hypertrophic chondrocytes decreases expression of Col II, Col X, Runx2, and MMP-13, and significantly increases chondrocyte apoptosis, indicating MMP-10 is required for terminal chondrocyte differentiation and survival during endochondral osteogenesis. |
MMP-10 shRNA knockdown in ATDC5 hypertrophic chondrocytes, flow cytometry (apoptosis), RT-PCR, Western blot, in vivo rat/human KBD cartilage analysis |
Cartilage |
Medium |
35818290
|
| 2025 |
MMP10 induces Ca²⁺ mobilization in dorsal root ganglion (DRG) neurons through a PAR1-independent mechanism (in contrast to MMP3, MMP8, and MMP9 which act via PAR1), establishing a distinct neuronal signaling pathway for MMP10. |
Intracellular Ca²⁺ imaging in DRG neurons, PAR1 pharmacological blockade, comparison with other MMPs |
bioRxivpreprint |
Low |
|
| 2025 |
Endothelial TRIM35 inhibits MMP10 expression and secretion by promoting K63-linked ubiquitination of RelB, maintaining its nuclear localization to inhibit MMP10 transcription through the non-canonical NF-κB signaling pathway; conditional endothelial TRIM35 knockout leads to increased MMP10 secretion, which drives smooth muscle cell calcification in vascular grafts. |
Conditional endothelial TRIM35 KO mice, arterial isograft model, single-cell analysis, co-culture experiments, ubiquitination assays (K63-linked), RelB localization studies, in situ MMP10 targeting |
Advanced science |
Medium |
39865905
|
| 2024 |
NOX5-generated ROS upregulates MMP-10 expression in endothelial cells via the redox-sensitive JNK/AP-1 signaling pathway, promoting endothelial cell migration; NOX5 and MMP-10 silencing prevented this pro-migratory effect, and effects were enhanced by angiotensin II. |
NOX5 overexpression and siRNA silencing in human endothelial cells, MMP-10 siRNA, wound healing assay, JNK/AP-1 pathway inhibition, MMP-10 promoter activity assay, in vivo NOX5-expressing mouse hearts |
Antioxidants |
Medium |
39456453
|
| 2025 |
Active MMP-10 cleaves nephrin in vitro, contributing to podocyte injury; in vivo, MMP-10 knockout mice showed less albuminuria and reduced pro-inflammatory/pro-fibrotic gene expression in anti-GBM nephritis, and MMP-10 overexpression in podocytes upregulated inflammatory responses to TNF-α while MMP-10 knockdown mitigated inflammation. |
Mmp10⁻/⁻ knockout mice, anti-GBM nephritis model, GC-A/MMP-10 double KO mice, in vitro nephrin cleavage assay, podocyte MMP-10 OE and KD, co-culture of podocytes with endothelial cells, Western blot |
Nephrology, dialysis, transplantation |
Medium |
40328459
|
| 2025 |
SOX9 directly transcriptionally activates MMP10 expression (identified by ChIP-seq), and MMP10 promotes ECM degradation downstream of SOX9 in tracheal fibroblasts via the Wnt/β-catenin signaling pathway; SOX9 overexpression increased and SOX9 siRNA decreased MMP10 expression, fibroblast activation, and ECM deposition. |
RNA-seq, ChIP-seq, adenoviral SOX9 overexpression, siRNA knockdown, Wnt/β-catenin pathway analysis, in vivo tracheal fibrosis model, MMP10 expression quantification |
Genes & diseases |
Medium |
38993791
|
| 2024 |
A missense variant p.L245P in MMP10 (identified in families with premature myocardial infarction) alters the MMP10-TIMP1 binding interface, reduces total free binding energy, and minimizes the substrate-binding cleft volume (molecular dynamics simulations). In macrophages transfected with the variant, cells were more adherent, less migratory, and secreted higher levels of pro-inflammatory CXCL1 and CXCL8 compared to wild-type MMP10. |
Whole-exome sequencing (variant identification), molecular dynamics simulations, macrophage transfection with WT and p.L245P cDNA, adhesion assay, migration assay, ELISA for chemokines |
Scientific reports |
Medium |
38806571
|
| 1998 |
SL-2 (MMP-10) in developing human bone is produced in an active form (confirmed by in situ zymography) at sites of resorption in endochondral ossification, the chondro-osseous junction (chondrocytes), and in osteoclasts and mononuclear marrow cells, with associated matrix degradation activity. This differs from SL-1 (MMP-3), which is present predominantly as a latent matrix-bound proenzyme. |
Immunohistochemistry, in situ zymography on human osteophytic and neonatal rib bone sections |
Bone |
Medium |
9662124
|
| 2020 |
Ski associates with the pericentromeric region and promoters of Mmp10 (along with Mmp3 and Mmp13) on chromosome 9 during mitosis, promotes H3K9 tri-methylation at these loci, and is required for transcriptional repression of these genes during M/G1 transition; Ski⁻/⁻ MEFs show increased Mmp activity and derepressed Mmp10 expression. |
Chromatin immunoprecipitation (ChIP) of Ski at Mmp10 promoter, H3K9 methylation/acetylation assays, Ski⁻/⁻ MEFs, differential gene expression assays, MMP activity assay |
Journal of molecular biology |
Medium |
32198114
|
| 2022 |
miR-148/152 family members negatively regulate MMP10; deficiency of any member increases MMP10 (and MMP13) expression, disrupts intestinal barrier, and activates NF-κB signaling in part through MMP10-mediated cleavage of pro-TNF-α into bioactive fragments. Blocking NF-κB exerted a restorative effect only in knockout mice. |
Individual and full-family miR-148/152 KO mice, colitis/CAC models (DSS/AOM), MMP10 expression analysis, intestinal barrier assays, NF-κB pathway analysis, NF-κB blockade experiments |
Cancer letters |
Medium |
34979166
|