Anti_Mouse, mab ICAM_1 Source Rat
- Known as:
- Anti_Mouse, mab ICAM_1 Source Rat
- Catalog number:
- 103-M97
- Product Quantity:
- 200 µg
- Category:
- -
- Supplier:
- Reliatech
- Gene target:
- Anti_Mouse mab ICAM_1 Source Rat
Related genes to: Anti_Mouse, mab ICAM_1 Source Rat
- Gene:
- ICAM1 NIH gene
- Name:
- intercellular adhesion molecule 1
- Previous symbol:
- -
- Synonyms:
- BB2, CD54
- Chromosome:
- 19p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1989-04-24
- Date modifiied:
- 2016-01-15
Related products to: Anti_Mouse, mab ICAM_1 Source Rat
Related articles to: Anti_Mouse, mab ICAM_1 Source Rat
- Endometriosis (EMs) is an estrogen-dependent inflammatory disease characterized by the presence of endometrial-like tissue outside the uterine cavity, yet its precise pathogenesis remains incompletely elucidated. TICAM1, a key adaptor protein in the Toll-like receptor (TLR) signaling pathway, is known to be involved in inflammatory responses; however, its specific role in EMs has not been defined. This study integrated evidence from clinical tissue samples of patients with ovarian endometriomas, in vitro studies, and in vivo models to explore the role of TICAM1 in EMs. TICAM1 expression was significantly upregulated in both eutopic and ectopic endometrium, with the highest levels observed in ectopic lesions, where it was primarily localized to stromal and glandular epithelial cells. Functional experiments showed that TICAM1 overexpression promoted the proliferation, migration, and invasion of human endometrial stromal cells (hESCs), while TICAM1 knockdown suppressed these activities. Concurrently, TLR3 and TLR4 were also upregulated in EMs tissues, and their activation increased TICAM1 expression. Knockdown of TICAM1 attenuated the enhanced cellular activities induced by TLR3/TLR4 activation. Mechanistically, IRF3 and IFN-β levels were elevated in both EMs tissues and TICAM1-overexpressing hESCs, while TICAM1 knockdown inhibited TLR3/TLR4-induced IRF3 phosphorylation and subsequent IFN-β production. These findings were further corroborated in a mouse model of EMs. Together, our findings suggest that TICAM1 may enhance the proliferation, migration, and invasion of hESCs by mediating TLR3/TLR4 signaling and promoting IRF3 phosphorylation and subsequent IFN-β production, thereby potentially contributing to EMs progression. Therefore, targeting TICAM1 may represent a potential therapeutic direction for ovarian endometrioma-associated EMs, while its relevance to superficial peritoneal and deep infiltrating EMs requires further investigation. - Source: PubMed
Publication date: 2026/06/04
MuDanLiFu HaLiSaiHuang SumingLi YameiLiang YanZhao XiaoyaZhu QianJi SifanZhou JieHe ChuqingGe ShunnaZhang Jian - To establish effective infection, viral pathogens employ diverse strategies through encoded proteins to interfere with host antiviral responses. While previous studies have predominantly focused on elucidating the mechanisms by which individual viral proteins regulate type I interferon (IFN) responses, this study presents the first demonstration that Japanese encephalitis virus (JEV)-encoded NS1 and NS4B proteins cooperatively target the TLR3 receptor signaling pathway to suppress IFN production. Here, we first discovered JEV-encoded multifunctional glycoprotein NS1, which inhibits TLR3-mediated IFN-β production by targeting TLR3 and TRIF. Mechanistically, NS1 interacts with these host factors and may induce their degradation via the autophagy pathway. Building on these findings, we further demonstrated that NS1 and NS4B act synergistically to suppress type I IFN production by enhancing TLR3 and TRIF degradation, thereby facilitating JEV replication. Structural simulation of the NS1-NS4B-TLR3 complex unveiled a dynamic mechanism that NS4B binding induces conformational changes in dimerized NS1, which leads to a tighter binding posture between NS1 and TLR3. Notably, NS4B binding expands the interface between NS1 and TLR3 by 1.5-fold that results in enhanced TLR3 degradation and downstream IFN-β suppression. Functional analysis confirmed that the C291/K293/R314 triple mutation in NS1 synergistically impairs TLR3 degradation. Collectively, using JEV as a model, this study reveals a novel mechanism by which two viral components can act synergistically to evade the host antiviral response. Given the common coexistence and functional interplay of viral-encoded proteins in naturally infected cells, this study establishes a framework for investigating cooperative interactions among multiple viral proteins. - Source: PubMed
Publication date: 2026/05/01
Zeng QuanHe MaozhouLi MengyaoYang DongWang LeiHao ChenlinWang ZhaoqingZhou MinminZhu TianrenzhengNiu XueshiChen ZhihuiZhang BingqianZu ShaopoDing XueyanWei ZhanyongChu HinZhang Honglei - Rotavirus (RV) infection has become a significant public health risk worldwide, but the specific molecular mechanisms of the mucosal immune response have not been elucidated. Dendritic cells (DCs), professional antigen-presenting cells, have a pivotal role in linking innate and adaptive immunity. In the present study, we found that TIR domain-containing adapter-inducing interferon-β (TRIF) is critical for the activation of DCs to antagonize RV infection. TRIF deficiency limited DCs maturation in the spleen and DCs differentiation in MLNs during porcine rotavirus (PRV) infection. Further studies confirmed that blocking TRIF expression in DCs resulted in an impaired ability to promote T lymphocyte proliferation and differentiation. Mechanistically, TRIF promoted the release of IL-6, IL-10, IL-12, and IFN-γ through the TRAF3-activated NF-κB signaling pathway while helping to activate DCs in MLNs to express MHC-Ⅱ and thus accelerate antigen presentation. Our results establish the concept that a TRIF-dependent positive-feedback loop is critical for sustained DC activation, indicating a novel role for TRIF in PRV-induced mucosal immunity. - Source: PubMed
Publication date: 2026/04/22
Sun YuNiu TianmingZhang RanLi DanniCheng MingyangJiang ChenxiShao YiranWang HongyuanGuo ZiqunYang WentaoCao XinWang ChunfengYe LipingShi Chunwei - The blood-brain barrier (BBB) protects the brain but becomes compromised during systemic inflammatory conditions such as sepsis. The mechanisms driving BBB disruption remain incompletely understood. Here, we identified a significant enrichment of the macroautophagy/autophagy-lysosome-related pathway in the upregulated proteome using quantitative proteomics on brain microvessels from mice after cecal ligation and puncture (CLP) that induces polymicrobial sepsis. CLP progressively induced autophagic flux in brain endothelial cells, peaking at 24 h post-procedure before subsiding. Similarly, an mRFP-GFP-LC3 reporter assay and immunoblotting showed that lipopolysaccharide (LPS) treatment increased autophagic flux in bEnd.3 cells in a time- and dose-dependent manner. Mice intraperitoneally (IP) injected with the autophagy inhibitors chloroquine (CQ) or 3-methyladenine (3-MA) were resistant to BBB disruption caused by CLP or IP injection of LPS, whereas those injected with the autophagy inducer rapamycin (Rapa) were more susceptible. CQ and 3-MA reduced, while Rapa increased, CLP-induced lethality in mice. These effects were confirmed using a dextran infiltration assay on bEnd.3 cell transwell cultures. CQ alleviated both the acute disruption of the tight junction proteins TJP1/ZO-1 and CLDN5 in brain microvessels and the long-term memory and anxiety deficits in LPS-challenged mice. siRNA-mediated knockdown of the SNARE protein STX17, which inhibits autophagosome-lysosome fusion, attenuated LPS-induced tight junction protein degradation in bEnd.3 cells. Importantly, inhibition of TLR4 or its downstream kinase TBK1 reduced LPS-induced autophagy and preserved tight junction proteins, implicating TLR4-TBK1 signaling in endothelial autophagy activation. These results suggest that excessive autophagy in endothelial cells drives BBB damage and cognitive dysfunction in sepsis.: 3-MA: 3-methyladenine; ATG5: autophagy related 5; BBB: blood-brain barrier; bEnd.3 cells: brain-derived endothelial cells.3; CLP: cecal ligation and puncture; CQ: chloroquine; EPM, elevated plus maze; GO: Gene Ontology; IP: intraperitoneal; LPS: lipopolysaccharide; MAP1LC3/LC3-II: microtubule associated protein 1 light chain 3-II; MWM: Morris Water Maze; NOR: novel object recognition test; OFT: open field test; Rapa: rapamycin; SAE: sepsis-associated encephalopathy; SNARE: soluble N-ethylmaleimide-sensitive factor attachment protein receptor; TBK1: TANK binding kinase 1; TICAM1/TRIF: TIR domain containing adaptor molecule 1; TLR4: toll like receptor 4; TMT: tandem mass tag. - Source: PubMed
Publication date: 2026/04/25
Peng MilinChen WeiGao QingtaoZhu XuejingYu LaidongZhang LinZou XinyingHu ZhonghuaZhang Lina - Hepatitis C virus (HCV) infection induces hyperinsulinemia and is associated with various extrahepatic manifestations, including effects on pancreatic β cells. However, the specific impact of HCV infection on β-cell function remains unclear. This study elucidates the mechanisms of hyperinsulinemia in HCV-infected individuals and its clinical significance in the era of direct-acting antiviral (DAA) therapy. Analysis of 118 non-diabetic HCV-positive patients demonstrated significantly elevated basal insulin levels and C-peptide concentrations compared with 30 healthy controls, with serum/hepatic HCV RNA load positively correlating with insulin secretion. In vitro investigations revealed regulatory effect of HCV on insulin secretion: stimulation under low-glucose conditions via nitric oxide (NO)-dependent pathways, and inhibition under high-glucose conditions. Mechanistically, HCV infection activated the TLR3/TRIF/NF-κB signaling axis to upregulate inducible nitric oxide synthase (iNOS), leading to enhanced NO production that promoted basal insulin release. Pharmacological inhibition of NO or iNOS abrogated HCV-induced insulin hypersecretion without compromising viral replication. Clinically, these findings establish hyperinsulinemia as a pre-diabetic marker in HCV infection and identify the NF-kB/iNOS/NO pathway as a therapeutic target for metabolic comorbidity prevention. Despite HCV curability with DAAs, this work highlights persistent virus-induced β-cell dysfunction and informs integrated strategies for antiviral and metabolic intervention to optimize long-term patient outcomes. - Source: PubMed
Publication date: 2026/04/18
Wang ShitongWu MengliRong RongWang JinxinTursun KebinurKsimu SulaimanZhou YuanWang NingWang QianChen Jizheng