MMP-2 hemopexin-like domain
- Known as:
- MMP-2 hemopexin-like domain
- Catalog number:
- GB0084
- Product Quantity:
- 1 mg
- Category:
- -
- Supplier:
- Giotto Biotech
- Gene target:
- MMP-2 hemopexin-like domain
Related genes to: MMP-2 hemopexin-like domain
- Gene:
- IMMP2L NIH gene
- Name:
- inner mitochondrial membrane peptidase subunit 2
- Previous symbol:
- IMMP2L-IT1
- Synonyms:
- IMP2
- Chromosome:
- 7q31.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-07-11
- Date modifiied:
- 2018-01-23
- Gene:
- MMP2 NIH gene
- Name:
- matrix metallopeptidase 2
- Previous symbol:
- CLG4, CLG4A
- Synonyms:
- TBE-1
- Chromosome:
- 16q12.2
- Locus Type:
- gene with protein product
- Date approved:
- 1989-05-25
- Date modifiied:
- 2015-02-23
- Gene:
- MMP15 NIH gene
- Name:
- matrix metallopeptidase 15
- Previous symbol:
- -
- Synonyms:
- MT2-MMP, MTMMP2, SMCP-2
- Chromosome:
- 16q21
- Locus Type:
- gene with protein product
- Date approved:
- 1996-11-13
- Date modifiied:
- 2016-10-05
- Gene:
- MMP23A NIH gene
- Name:
- matrix metallopeptidase 23A (pseudogene)
- Previous symbol:
- MMP21
- Synonyms:
- MIFR
- Chromosome:
- 1p36.33
- Locus Type:
- pseudogene
- Date approved:
- 1999-08-26
- Date modifiied:
- 2016-10-05
- Gene:
- MMP23B NIH gene
- Name:
- matrix metallopeptidase 23B
- Previous symbol:
- MMP22
- Synonyms:
- MIFR, MIFR-1
- Chromosome:
- 1p36.33
- Locus Type:
- gene with protein product
- Date approved:
- 1999-08-26
- Date modifiied:
- 2016-10-05
Related products to: MMP-2 hemopexin-like domain
"Recombinant Human Trem-like transcript 2 protein_TREML2""Recombinant Human Trem-like transcript 2 protein_TREML2""Recombinant Human Trem-like transcript 2 protein_TREML2""Recombinant Human Trem-like transcript 2 protein_TREML2"(2-5')oligo(A) synthase 1B,2-5A synthase 1B,2'-5'-oligoadenylate synthase 1B,2'-5'-oligoadenylate synthase-like protein 1,Mouse,Mus musculus,Oas1b,Oias2(Ala1)-PAR-4 (1-6) (mouse)
(Ala1)-Thrombin Receptor-Like 3 (1-6) (mouse), (Ala1)-Proteinase Activated Receptor 4 (1-6) (mouse), (Ala1)-Coagulation Factor II Receptor-Like 3 (1-6) (mouse), AYPGKF 98%(Ala1)-PAR-4 (1-6) amide (mouse)
AYPGKFamide, (Ala1)-Thrombin Receptor-Like 3 (1-6) amide (mouse), (Ala1)-Coagulation Factor II Receptor-Like 3 (1-6) amide (mouse), (Ala1)-Proteinase Activated Recepto(Ser8)-GLP-1 (7-36) amide (human, bovine, guinea pig, mouse, rat)
(Ser79)-Proglucagon (78-107) amide (human, bovine, guinea pig, mouse, rat), (Ser8)-Glucagon-Like Peptide 1 (7-36) amide (human, bovine*Please allow 3-5 days for delivery time.* In mammals, TIR domain adapters, including Myd88, TIRAP, TICAM-1 (also called TRIF), and TRAM, act in Toll-like receptor (TLR) signaling pathway. The last me*Please allow 3-5 days for delivery time.* RAIDD (RIP-associated ICH-1 homologous protein with a death domain) is an adaptor molecule that mediates the action of cysteine proteases involved in apoptos*Please allow 3-5 days for delivery time.* Toll-like receptors (TLRs) play an essential role in the detection and elimination of invading pathogens. Recognition of microbial components by TLRs trigger-14 gene protein,Alpha-globin regulatory element-containing gene protein,C16orf35,CGTHBA,Homo sapiens,Human,MARE,Nitrogen permease regulator 3-like protein,NPRL3,Protein CGTHBA09C01,Efha1,EF-hand domain-containing family member A1,Rat,Rattus norvegicus,Smhs21,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase,Acireductone dioxygenase (Ni(2+)-requiring),Adi1,Alp1,Androgen-responsive ARD-like protein 1,ARD,Mtcbp1,Ni-ARD,Rat,Rattus norvegicus1-O-acylceramide synthase,ACS,Bos taurus,Bovine,Group XV phospholipase A2,LCAT-like lysophospholipase,LLPL,LPLA2,LYPLA3,Lysophospholipase 3,Lysosomal phospholipase A2,PLA2G15 Related articles to: MMP-2 hemopexin-like domain
- The extracellular matrix (ECM) plays a pivotal role in facilitating tumour development, invasiveness, metastasis, and immunoevasive processes through dynamic ECM remodelling processes. Testican-1 (SPOCK1), an excretory matricellular proteoglycan, is suggested to exert a role in the facilitation of ECM remodelling processes through interacting with matrix metalloproteases (MMPs) and even its less known forms. The structural mechanisms of interactions between testican-1 and MMPs were studied, and their roles in tumour-promotion pathway processes were also examined using a computational approach and immunofluorescence validated by colocalisation technique analysis. A computational analysis using docking, molecular dynamics (MD), and systems biology analysis was employed. HDock and GROMACS were chosen to analyse binding affinity and testican-1 stability with 28 different MMPs. H-bond, free energy, and root mean square fluctuation (RMSF) analyses were performed to confirm the interactions in the testican-1-MMP complexes. The systems biology toolkit implemented in this study consisted of STRING, BioGRID, and Cytoscape, which were employed for testican-1 interaction network and pathway analysis. Kaplan-Meier survival analysis using the GEPIA2 tool was utilised to correlate SPOCK1 gene expression and clinical survival measures for various malignancies. The docking analysis showed robust interactions between testican-1 and MMP23, MMP25, and MMP28. Additionally, testican-1-MMP complexes were confirmed to form stable interfaces based on comprehensive MD analysis, suggesting solid binding interfaces with the MMP-unique domain of testican-1. Our systems biology experiment indicated testican-1 as a central hub for interactions between immunoevasive and ECM remodelling processes. SPOCK expression was also shown to correlate with significant survival measures for different malignancies, revealing clinical implications in cancer. The testican-1-MMP computational analysis suggests testican-1 plays a pivotal role as a therapeutic target for a wide range of malignancies. SPOCK-MMP interactions could be targeted to interrupt tumour-promoting processes by arresting dynamic changes in the ECM, thereby improving patient survival. © 2026 The Author(s). The Journal of Pathology published by John Wiley & Sons Ltd on behalf of The Pathological Society of Great Britain and Ireland. - Source: PubMed
Publication date: 2026/05/15
Youssefi SepidehSaleki KiarashKadam PrernaMazloomi AmirrezaMukherjee AbhikDekker Lodewijk VNateri Abdolrahman S - Colorectal cancer (CRC) remains a major cause of cancer-related mortality worldwide, largely due to therapeutic resistance and the complexity of the tumor microenvironment. The extracellular matrix (ECM) critically regulates tumor progression by balancing matrix metalloproteinases (MMPs) and their inhibitors (TIMPs). Theranekron D6, an extract of with known anti-inflammatory and wound-healing effects, has shown anticancer potential. This study investigated its molecular impact on ECM remodeling and apoptosis in human CRC. Human colorectal adenocarcinoma (Caco-2) and non-tumoral embryonic kidney (HEK293) cells were treated with Theranekron D6 (1-1000 µL/mL). Cell viability was evaluated using the MTT assay, revealing a dose- and time-dependent cytotoxic response with an IC₅₀ of 400 µL/mL at 48 h. Gene expression of 62 target genes spanning ECM remodeling, apoptosis, and key signaling axes (PI3K/AKT, NF-κB, and SMAD/STAT) was analyzed by quantitative polymerase chain reaction (qPCR), and protein levels of TIMP1, MMP2, MMP9, MMP14 and MMP28 were quantified by enzyme-linked immunosorbent assay (ELISA). Pathway interactions were assessed via STRING-based enrichment and clustering analyses. Theranekron markedly upregulated pyruvate dehydrogenase kinase 1 (PDK1) by 23-fold, with concurrent upregulation of PTEN suggesting a negative feedback mechanism that may limit net pro-survival PI3K/AKT output. This regulation restored a TIMP1-dominant ECM profile and reduced MMP2 and MMP28 protein levels. NF-κB pathway components were broadly downregulated at the transcriptional level. Concurrently, Theranekron induced transcriptional changes associated with mitochondrial and SMAD-dependent apoptotic pathways. Theranekron acts as a cell-context-specific modulator, simultaneously regulating PI3K/AKT/PDK1, NF-κB and SMAD pathways to restore ECM integrity and modulate apoptotic signaling pathways in Caco-2 CRC cells, suggesting its potential as a multi-target experimental therapeutic candidate in in vitro CRC models. - Source: PubMed
Publication date: 2026/03/16
Kuccukturk SerkanDuran TugceVanli SerdarKaraselek Mehmet Ali - Vascular ageing is a major contributor to cardiovascular disease and is closely linked to vascular stiffness. Stiffening of the vascular wall disrupts endothelial homeostasis and promotes chronic inflammation, yet the underlying mechanisms remain poorly understood due to technological limitations. Here, we used a previously developed in vitro microfluidic model to investigate how biomechanical forces, specifically substrate stiffness and shear stress, interact to regulate endothelial cell behaviour. Using RNA sequencing and functional assays, we found that endothelial cells exposed to both physiological and high levels of shear stress were more sensitive to increases in substrate stiffness. Under these conditions, the cells exhibited a greater number of differentially expressed genes and enhanced activation of inflammatory signalling pathways, suggesting that mechanical stiffening promotes endothelial inflammation and contributes to vascular ageing. We identified enriched pathways involved in inflammatory signalling and extracellular matrix (ECM) remodelling in response to substrate stiffness. Endothelial cells exposed to high shear stress and increased stiffness showed up-regulation of genes such as ICAM1, VCAM1, LAMB3, and MMP28, which are known to mediate leukocyte adhesion and ECM remodelling. Importantly, benchmarking our engineered in vitro microfluidic model using human aortic tissue confirmed concordant molecular and histological changes between stiff (aged) and soft (healthy) aortas. Ultimately, this validated microfluidic platform provides proof of concept that biomechanical forces characteristic of vascular ageing drive endothelial inflammation and vascular remodelling, offering new mechanistic insight and a powerful experimental framework to advance therapeutic strategies targeting vascular stiffness and age-related vascular disease. - Source: PubMed
Publication date: 2025/12/19
Lai AustinZhou YingChheang ChanlyMirabedini AzadehMirzaalikhan YasminNoonan JonathanWatson AnnaDayawansa Nalin HHuang WenzhiKhanmohammadi ManijehHoushyar ShadiSalim AgusPeter KarlheinzBaratchi Sara - Prolonged exposure to ozone causes lung injury and persistent inflammation, pathologies associated with emphysema and asthma. Herein, we characterized inflammatory cells in the lungs using a murine model of prolonged ozone exposure, with the long-term goal of assessing their role in disease pathogenesis. Mice were exposed to air or ozone (1.5 ppm, 2 h, 2×/wk, 6 wk). Bronchoalveolar lavage fluid (BAL) and cells and lung tissue were collected 24 h after the final exposure. Alveolar/bronchiolar hyperplasia, epithelial degeneration, and mononuclear cell infiltration were observed following ozone exposure; BAL protein, cells, fibrinogen, and SP-A and SP-D were also increased, along with markers of oxidative stress, and impaired pulmonary function. Flow cytometric analysis of infiltrating myeloid cells revealed that after ozone exposure, the majority of these cells were mature infiltrating macrophages. These were comprised mainly of anti-inflammatory/profibrotic macrophages, with a smaller number of proinflammatory macrophages. Proinflammatory genes (Il1β, Ccl3, Ccl17, Ccl22, Tnfα) and NF-κB activity were increased in BAL cells from ozone-exposed mice (>97% macrophages); profibrotic genes (Mmp12, Mmp28, Tgfβ), but not anti-inflammatory genes (Il10, Arg1), were also upregulated. Following ozone exposure, glycolytic activity and oxidative phosphorylation increased in BAL cells, consistent with proinflammatory and profibrotic activation, respectively. These findings are important as they provide a rationale for evaluating the role of inflammatory macrophages in the pathophysiological response to prolonged ozone exposure. Impact statement: These studies are significant as they may lead to the identification of novel therapeutic approaches for reducing inflammatory lung disease caused by long-term exposure to inhaled ozone. - Source: PubMed
Sunil Vasanthi RVayas Kinal NRadbel JaredSmith Ley CodyMeshanni Jaclynn ALee Jordan MWeinstock DanielAbramova ElenaShmarakov Igor OGow Andrew JLaskin Jeffrey DLaskin Debra L - Sjögren's disease (SjD) is a highly heterogeneous autoimmune disease with substantial challenges in early diagnosis and therapeutic intervention. We developed an integrated approach combining machine learning algorithms, SHAP interpretable modelling, molecular docking, and single-cell analysis to facilitate early diagnosis and treatment of SjD. - Source: PubMed
Publication date: 2025/11/14
Wang QiangqiangHe LinglingHan Yajuan