MCP-1 Synthetic Protein
- Known as:
- MCP-1 Synthetic Protein
- Catalog number:
- x1243c
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Exalpha
- Gene target:
- MCP-1 Synthetic Protein
Related genes to: MCP-1 Synthetic Protein
- Gene:
- CCL2 NIH gene
- Name:
- C-C motif chemokine ligand 2
- Previous symbol:
- SCYA2
- Synonyms:
- MCP1, MCP-1, MCAF, SMC-CF, GDCF-2, HC11, MGC9434
- Chromosome:
- 17q12
- Locus Type:
- gene with protein product
- Date approved:
- 1990-07-05
- Date modifiied:
- 2016-10-05
- Gene:
- SLC25A14 NIH gene
- Name:
- solute carrier family 25 member 14
- Previous symbol:
- -
- Synonyms:
- BMCP1, UCP5
- Chromosome:
- Xq26.1
- Locus Type:
- gene with protein product
- Date approved:
- 1999-02-09
- Date modifiied:
- 2016-10-05
Related products to: MCP-1 Synthetic Protein
Related articles to: MCP-1 Synthetic Protein
- Chronic stress is associated with poor prognosis in colorectal cancer (CRC), but the underlying immune mechanisms remain poorly defined. This study investigates how β-adrenergic signaling, a key component of the stress response, modulates the tumor microenvironment. We demonstrate that stressed CRC patients have elevated serum CCL2, and high tumoral expression of CCL2 and its receptor CCR2 predicts poor survival. Single-cell analysis reveals that within the tumor microenvironment of colorectal cancer, macrophages constitute the primary subset of immune cells responsible for CCL2 secretion. Mechanistically, we demonstrate that stimulating macrophages with isoproterenol, a well-established in vitro method to mimic chronic stress signaling, induces their polarization toward an M2-like phenotype and significantly increases CCL2 secretion. Functionally, conditioned media from these "stressed" macrophages enhanced CRC cell proliferation and invasion in a CCR2-dependent manner, an effect abrogated by pharmacological CCR2 blockade. Collectively, our findings pinpoint the CCL2-CCR2 pathway as the central mediator of a 'stress-macrophage-tumor' axis, validating it as a key therapeutic target to intercept CRC progression driven by a chronic stress state elicited by β-adrenergic activation. - Source: PubMed
Publication date: 2026/06/25
Wang MengyunPang JiayuWang WenbinXu QianLu YanjieZuo YanzhenLi YuHong - This study evaluated the diagnostic value of C-C motif chemokine ligand 2 (CCL2) and C-C chemokine receptor type 2 (CCR2) in pleural effusions for distinguishing histological subtypes of lung cancer (LC). - Source: PubMed
Publication date: 2026/06/28
Yu JieHuang YongChen Weirong - Cerebral malaria (CM) is a severe complication of Plasmodium infection, classically attributed to parasite sequestration and neuroinflammation. Here, we uncover a spleen-centered humoral autoimmune circuit that drives CM pathology. Proteomic analyses identify CD36 as a dominant host-derived antigen enriched in infected red blood cells (iRBCs), triggering anti-CD36 autoantibody production in patients with falciparum malaria. Although contributing to iRBCs clearance, these autoantibodies also target other CD36-expressing cells, thereby driving thrombocytopenia, endothelial injury, and macrophage activation, ultimately amplifying systemic inflammation. Mechanistically, Plasmodium infection recruits Ly6cGlut1 macrophages to the spleen through the CCL2-CCR2 axis. These macrophages exhibit elevated proteasome activity and drive B cell activation and anti-CD36 antibody production. Targeting Ly6cGlut1 macrophages, we develop Glutoborin, a GLUT1-directed proteasome inhibitor that preferentially suppresses their function, reduces autoantibody production, and alleviates CM-associated pathology in vivo. Together, these findings establish a spleen-centered anti-CD36 autoimmune circuit as a key driver of CM and nominate Ly6cGlut1 macrophages as therapeutic targets. - Source: PubMed
Publication date: 2026/06/27
Sun XinLi RidongWang WeixuanYang DanliTian WenyuZhang XinHan LinjiangZhao XuyangXing XiaoyanLi RuntaoLi YuhuiHe JingSong RuiYou FupingLu Dan - The MSMP (MicroSeminoProtein, Prostate-associated) protein is overexpressed in several cancers, including prostate, ovarian, and breast cancers. Its overexpression is particularly prevalent in tumors resistant to hormonal therapy, as well as to antiangiogenic treatments (e.g., anti-VEGF therapies). In hypoxic tumor microenvironments, characteristic of solid tumors, MSMP expression increases and facilitates tumor growth. MSMP binds to the transmembrane receptor CCR2 (C-C chemokine receptor type 2), a GPCR present on monocytes and lymphocytes. This interaction stabilizes an active conformation of CCR2, enabling downstream MAP kinase signaling pathways to reactivate androgen synthesis and promote tumor progression. In this study, we employed molecular modeling, molecular dynamics simulations, and machine learning techniques to elucidate the structural basis of the MSMP-CCR2 interaction. High-resolution models of the MSMP-CCR2-G protein complex were generated using AlphaFold2 and refined with MD simulations. Comparative analyses with the CCL2-CCR2-G protein complex and the unbound CCR2-G protein complex revealed key conformational rearrangements that modulate and stabilize the active state of the receptor. Binding free energy calculations revealed similar energetic profiles for MSMP and CCL2, despite distinct binding modes. Residue-level energy decomposition identified critical residues at the MSMP-CCR2 interface, offering insights into the receptor's activation mechanism. Additionally, machine learning models classified molecular dynamics trajectories, highlighting key structural features associated with stable MSMP-CCR2-G protein states. This integrative approach identified residues essential for maintaining a stable conformation of the MSMP-CCR2-G protein complex, providing a basis for targeting MSMP-CCR2 interactions in therapeutic development. - Source: PubMed
Publication date: 2026/06/25
Quitté LéopoldLeclercq MickaëlMoroy GautierDroit Arnaud - Pulmonary arterial hypertension (PAH) is a fatal vascular disorder with poor prognosis. 6:2 chloro-polyfluorooctane ether sulfonate (F-53B), a persistent environmental contaminant detected in humans, is known to be vasculotoxic, yet its association with PAH remains unexplored. This study aims to elucidate the mechanisms linking F-53B exposure to PAH by integrating network toxicology, molecular docking and in vitro experiments. Potential F-53B targets were predicted using ChEMBL, PharmMapper, and TargetNet. PAH-related genes were compiled from GeneCards, Online Mendelian Inheritance in Man (OMIM), Therapeutic Target Database (TTD), and GSE254617. We identified 42 key targets of F-53B-related PAH. Functional enrichment revealed terms such as inflammatory response and extracellular matrix. Protein-protein interaction (PPI) analysis identified five hub genes: CCL2, CXCL8, CCL5, CCR2, and CCL11. Molecular docking confirmed strong binding between F-53B and these core targets, with CCR2 showing the strongest affinity (-10 kcal/mol). Molecular dynamics simulations further verified stable binding to CCR2. In vitro experiments demonstrated that F-53B activated the CCL2/CCR2 axis and induced IL-1β, TNF-α, and IL-6 in HUVECs and RAW264.7 cells. This study reveals that F-53B is linked to PAH through dysregulation of chemokine signaling networks and induction of inflammatory cytokines. These findings suggest F-53B as a potential environmental risk factor for PAH and pinpoint potential targets for intervention. - Source: PubMed
Publication date: 2026/05/29
Xu LinglingMa YujieZheng ZhenmingZou FeiLi Wenjun