PUMP, DILUTER, VP9101
- Known as:
- PUMP, DILUTER, VP9101
- Catalog number:
- rvdia07620037000
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Diasource
- Gene target:
- PUMP DILUTER VP9101
Related genes to: PUMP, DILUTER, VP9101
- Gene:
- MMP7 NIH gene
- Name:
- matrix metallopeptidase 7
- Previous symbol:
- MPSL1
- Synonyms:
- PUMP-1
- Chromosome:
- 11q22.2
- Locus Type:
- gene with protein product
- Date approved:
- 1991-07-15
- Date modifiied:
- 2015-08-25
Related products to: PUMP, DILUTER, VP9101
0.5 mm 2-pump Connecting Tube0.9 mm 2-pump Connecting Tube1-pump Control Cable, AC-21101-pump Control Cable, AC-21202-pump Control Cable, AC-21102-pump Control Cable, AC-212023 kDa subunit of V-ATPase,Atp6f,Atp6v0b,Mouse,Mus musculus,Vacuolar proton pump 21 kDa proteolipid subunit,V-ATPase 21 kDa proteolipid subunit,V-type proton ATPase 21 kDa proteolipid subunit32 kDa accessory protein,ATP6D,ATP6V0D1,Bos taurus,Bovine,P39,Vacuolar proton pump subunit d 1,V-ATPase 40 kDa accessory protein,V-ATPase AC39 subunit,V-ATPase subunit d 1,VPATPD,V-type proton ATPase32 kDa accessory protein,ATP6D,ATP6V0D1,Homo sapiens,Human,p39,Vacuolar proton pump subunit d 1,V-ATPase 40 kDa accessory protein,V-ATPase AC39 subunit,V-ATPase subunit d 1,VPATPD,V-type proton ATPaseAC-2110 Perista Pump 1-ch, 110VAC-2110 Perista Pump 1-ch, 230VAC-2110 Perista Pump 2-ch, 110VAC-2110 Perista Pump 2-ch, 230VAC-2120 Perista Pump, 110VAC-2120 Perista Pump, 230V Related articles to: PUMP, DILUTER, VP9101
- The ruminal epithelium maintains livestock health by absorbing nutrients while maintaining a tight barrier between the lumen and the plasma space. This study demonstrates that rumen organoid-derived 2D cultures approximate native tissue architecture and reach greater epithelial purity than primary cultures, particularly at later passages. For the initial transcriptomic and structural comparison, cells isolated from stratum basale by fractional trypsinization, were used to generate model epithelia on cell culture inserts either from early-passage primary cultures ( passage 3) or after organoid expansion ( passage 10). Transcriptomic analysis was used to compare the primary culture inserts, the organoid-derived inserts and the native tissues from which they had been derived. While both cell culture models yielded epithelial-like growth with barrier formation (TER >400 Ω×cm), transcriptomic analysis revealed higher expression of fibroblast-/mesenchymal stromal ECM markers () in the inserts from the primary cultures. Additionally, extracellular matrix (ECM)-remodeling genes () were upregulated in primary culture inserts, suggesting increased tissue remodeling activity in conjunction with the expression of inflammatory mediators (). Organoid-derived inserts showed less affected mitochondrial pathways (Cytochrome c oxidase (), synthase genes) and ribosomal machinery (), while maintaining epithelial purity with no detectable fibroblast or immune cell contamination. The expression of mRNA for numerous short-chain fatty acid (SCFA) transporters is confirmed, including MCT1, MCT4, DRA, PAT, SMCT1, AE2, and . This study establishes organoids as a physiologically relevant model for studying rumen epithelial physiology. - Source: PubMed
Publication date: 2026/06/02
Khomeijani Farahani SaeedLiebe FranziskaManna SubhakankhaWeiß FranziskaStumpff FriederikeGünzel Dorothee - Benign prostatic hyperplasia (BPH), prevalently in aging men, is characterized by aberrant cell death of prostate cells. Anoikis, a specific subtype of apoptosis, is triggered when cells detach from the extracellular matrix (ECM), in contrast, cells with anoikis resistance contribute to pathological processes such as unregulated cell proliferation and impaired cell death. However, the role of anoikis resistance in BPH pathogenesis remains poorly understood. In this study, an elevated anoikis resistance level was observed in BPH tissues compared to normal prostates. Furthermore, matrix metalloproteinase 7 (MMP7) was identified as a key regulator of anoikis resistance in hyperplastic prostatic epithelium. Under anoikis-inducing conditions, MMP7 promoted mitophagy via the PINK1-Parkin pathway, alleviated mitochondrial stress damage, and enhanced anoikis resistance in BPH-1 cells. Mechanistically, MMP7 interacted with VDAC1 and bound specifically to lysine residues K109 and K110, thereby inhibiting VDAC1 oligomerization and increasing the accumulation of VDAC1 monomers, which served as additional binding sites to Parkin-mediated polyubiquitination. Moreover, clinical data revealed that MMP7 expression levels correlated significantly with the International Prostate Symptom Score (IPSS) and nocturia frequency. Additionally, in vivo experiments demonstrated that inhibition of MMP7 suppressed mitophagy and markedly attenuated prostatic epithelial hyperplasia in a rat model BPH. Collectively, our findings clarify the functional role of the MMP7-VDAC1 axis in BPH pathogenesis and highlight its potential as a therapeutic target for BPH management. - Source: PubMed
Publication date: 2026/06/01
Zhou YongyingLi YanLiu HuanZhang JunchaoQiu JizhangDu LuLai HuanChen PingGuo YumingLuo YongwenDiSanto Michael EZhang Xinhua - The extracellular matrix (ECM) provides both architectural integrity and signaling cues to tissues, largely through its fibrous components-collagen and elastin. Collagen fibrils consist of a core of various collagen types associated with several non-collagenous binding partners and confer tensile strength to tissues, while elastic fibers, composed of cross-linked elastin on a fibrillin-rich scaffold, ensure elasticity and resilience. Far from being mere degradative enzymes, proteases are key regulators of both the assembly and turnover of these networks. Metalloproteinases of the BMP1/tolloid-like, meprin and ADAMTS families orchestrate procollagen maturation, while lysyl oxidases and related enzymes drive covalent cross-linking of collagen and elastin fibers, also under proteolytic control. Matrix metalloproteinases (MMPs) and cysteine cathepsins further modulate collagen structure and degradation, generating bioactive fragments used as clinical biomarkers. In parallel, ADAMTS and ADAMTS-like proteases orchestrate fibrillin microfibril organization, fibulin interactions, and the topography of elastogenesis. Elastolytic proteases-including cathepsins K, S, and V, as well as MMP2, MMP7, MMP9, and MMP12-mediate physiological remodeling but also fuel pathological states when dysregulated, releasing elastin-derived peptides that act as potent signaling matrikines. Genetic or acquired defects in these proteolytic pathways underlie diverse connective tissue diseases such as osteogenesis imperfecta, Ehlers-Danlos, and acromelic dysplasias, as well as fibrosis, emphysema, and vascular aging. This review integrates recent structural, biochemical, and pathological insights into how proteases coordinate collagen and elastin dynamics, highlighting novel therapeutic strategies-including substrate- and exosite-selective inhibitors-to restore ECM homeostasis while minimizing off-target effects. - Source: PubMed
Publication date: 2026/05/29
Haddou SabrinaDavid AlexisLipinski OskarPuertas Rosa DoñateMaroteaux AgatheLe Goff CarineMoali CatherineLecaille FabienDuca Laurent - Matrix metalloproteinase-2 (MMP-2) is a key enzyme involved in extracellular matrix remodeling and is implicated in several pathological conditions, including cancer and neurodegenerative diseases. Peptide-based inhibitors such as APP-IP represent a promising strategy for selectively targeting MMP-2 while limiting off-target effects. In this study, we used molecular docking, molecular dynamics simulations, and MM/PBSA calculations to evaluate how targeted mutations in APP-IP affect binding affinity and selectivity. Mutations were introduced at three positions (Y, G, and N) of the peptide. Screening against MMP-2 identified two variants, Gly to Leu (G4L) and Asn to Thr (N5T), with predicted improved binding affinity relative to the native peptide, while mutations at position Y did not significantly alter affinity but were retained due to the known importance of this position for selectivity in accommodating S1´ pocket. To assess off-target effects, selected variants were further tested against MMP-9, a close homolog of MMP-2, and MMP-7, a more structurally distinct family member. The N5T variant showed reduced binding to MMP-9 while maintaining enhanced affinity for MMP-2, indicating improved selectivity trends. In contrast, G4L did not significantly alter binding to either off-target proteases. Mutations at position Y (Y3F) preserved affinity for MMP-2 while consistently reducing binding to both MMP-9 and MMP-7, highlighting the role of the S1' pocket in modulating selectivity. Simulations with MMP-7 confirmed intrinsically weaker binding of APP-IP and its variants, consistent with experimental observations, and showed no enhancement of off-target affinity. Overall, this structure-based approach enabled the identification of promising candidate variants with favorable predicted selectivity profiles, with N5T, G4L, and Y3F emerging as candidates for further experimental validation. Importantly, among all variant, N5T is particularly notable, as in our comparative prediction report, it not only improved affinity in MMP-2 but also enhanced selectivity trends by reducing binding to MMP-9 while maintaining a favorable profile in MMP-7. Also at position Y, although the overall binding affinity was largely retained, the observed reduction in off-target binding against both MMP-9 and MMP-7 underscores the importance of the S1' pocket, suggesting that subtle modifications here can modulate specificity. This research offers insights into the rational design of peptide-based inhibitors for MMP-2 and emphasizes the value of extending computational selectivity testing across both close and divergent MMPs. Future studies could further investigate these findings through combined mutation analyses, residue-level structural assessments, and the application of more rigorous free energy methods such as QM/MM-PBSA. However, these findings represent computationally predicted comparative trends and require experimental validation to confirm their biological relevance. - Source: PubMed
Publication date: 2026/05/26
Mirkhalaf SamiraTaghdir MajidArab Seyed Shahriar - Pulmonary fibrosis is a severe, chronic, and often lethal interstitial lung disease characterized by a destructive cycle of alveolar injury and inflammation, culminating in irreversible lung scarring. Its complex and multifactorial pathogenesis contributes to a poor prognosis and susceptibility to recurrent lung damage. This study employed an integrated network pharmacology and molecular docking approach to investigate the therapeutic repurposing of cilostazol for pulmonary fibrosis. Cilostazol was selected as a highly promising candidate owing to its broad pharmacological profile, encompassing anti-inflammatory, antioxidant, antiapoptotic, and antifibrotic properties. Network pharmacology analysis identified 10 potential targets of cilostazol, of which eight emerged as key network regulators: phosphodiesterase 3 (PDE3), PIK3CA, PTK2, RPS6KB1, VEGFR, F2-thrombin, ULK3 kinase, and PI3K delta. Molecular docking demonstrated that cilostazol binds to these profibrotic and fibrotic target proteins with binding affinities comparable to those of established experimental inhibitors. Experimental validation was performed using a bleomycin (BLM)-induced rat model of pulmonary fibrosis, incorporating histopathological and biochemical analyses of lung tissue and bronchoalveolar lavage fluid. Cilostazol exhibited significant antioxidant activity by reducing lipid peroxidation and restoring antioxidant enzyme levels. It exerted anti-inflammatory effects by downregulating proinflammatory cytokines (TNF-α, NO, and IL-6) and inflammatory markers (CRP, LDH, and MPO). Furthermore, cilostazol attenuated key indicators of fibrosis progression, including KL-6 and endothelin-1, alongside fibrotic markers such as TGF-β, α-SMA, and collagen I and III. At the molecular level, it significantly reduced the mRNA expression of fibrosis-associated genes, including TGF-β, fibronectin, α-SMA, collagen I, and MMP-7. Collectively, these findings demonstrate that cilostazol confers significant protection against bleomycin-induced pulmonary fibrosis through the targeted inhibition of the TGF-β/Smad, PI3K/AKT, and Wnt/β-catenin signaling cascades, highlighting its potential as a viable repurposed therapeutic strategy for inflammation-driven pulmonary fibrosis. - Source: PubMed
Publication date: 2026/05/28
Misar Pranaya LOtari Kishor VPande Vishal VIge Pradyumna P