PC_FB_W w. cap1
- Known as:
- PC_FB_W w. cap1
- Catalog number:
- 253580
- Product Quantity:
- 1
- Category:
- -
- Supplier:
- Herolab
- Gene target:
- PC_FB_W . cap1
Related genes to: PC_FB_W w. cap1
- Gene:
- CAP1 NIH gene
- Name:
- cyclase associated actin cytoskeleton regulatory protein 1
- Previous symbol:
- -
- Synonyms:
- CAP
- Chromosome:
- 1p34.2
- Locus Type:
- gene with protein product
- Date approved:
- 2003-07-17
- Date modifiied:
- 2017-05-17
Related products to: PC_FB_W w. cap1
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- Proprotein convertase subtilisin/kexin type 9 (PCSK9) acts as a pleiotropic modulator of inflammation. This study aimed to investigate the role and underlying mechanism of PCSK9 in Kawasaki disease (KD)-associated vasculitis. A Candida albicans water-soluble fraction (CAWS)-induced murine vasculitis model (n = 5-8 mice per group) and CAWS-stimulated RAW 264.7 macrophages (n = 3-8 independent experiments) were used. PCSK9 was pharmacologically inhibited in vivo with SBC-115076 and in vitro with PF-06446846. Vascular pathology, inflammatory markers, macrophage polarization, and signaling pathways were evaluated using hematoxylin-eosin (H&E) staining, immunofluorescence (IF), Western blot, quantitative real-time polymerase chain reaction (qRT-PCR), and RNA sequencing (RNA-seq). CAP1 overexpression was performed via lentiviral infection in RAW 264.7 cells to further validate its functional role. PCSK9 expression was significantly upregulated (two-fold) in the coronary arteries of CAWS-treated mice, and PCSK9 was predominantly co-localized with macrophages. Pharmacological inhibition of PCSK9 attenuated coronary arteritis, reduced the inflammatory infiltrate fraction by 54%, attenuated systemic inflammation, and decreased cardiac macrophage infiltration by 89%. In vitro, PCSK9 blockade suppressed CAWS-induced M1 macrophage polarization, as shown by reduced expression of the markers CD86 (by 96%) and iNOS (by 60%), and decreased secretion of the pro-inflammatory cytokines TNF-α (by 80%), IL-1β (by 86%), and IL-6 (by 89%). Transcriptomic analysis identified the NF-κB pathway as a key downstream signaling pathway. Mechanistically, PCSK9 inhibition downregulated CAP1 (adenylyl cyclase-associated protein 1) expression by 64% and suppressed NF-κB p65 nuclear translocation by 91% in macrophages. Importantly, CAP1 overexpression reversed the inhibitory effects of PCSK9 blockade on p65 nuclear translocation, M1 polarization, and inflammatory cytokine production. PCSK9 promotes KD-like vasculitis by activating the CAP1-mediated NF-κB pathway in macrophages, thereby driving pro-inflammatory responses. Pharmacological inhibition of PCSK9 attenuates vascular immunopathology, highlighting PCSK9 as a potential therapeutic target for KD. - Source: PubMed
Zhang HaoShuai DujuanRuan MiaohuaWu MaoWang LinlinChu MaopingRong Xing - Cyclase-associated protein 1 (CAP1) is widely expressed in mammalian tissues; however, its physiological role in the lung remains largely unclear. This study aimed to explore the function of CAP1 in alveolar type 2 (AT2) cells and its potential association with pulmonary fibrosis. - Source: PubMed
Publication date: 2026/06/09
Wang BingbingGu YunluZhang JushanTuerhong AmanguliZhu YujieShah Binay KumarWang ChanghuiXie Shuanshuan - Pulmonary capillary endothelial cells (ECs) form a highly specialized vascular interface that sustains gas exchange and organismal survival across species. Recent advances in single-cell transcriptomics and lineage tracing have revealed substantial heterogeneity within the pulmonary endothelium, redefining traditional views of capillary structure and function. In the adult lung, two major capillary populations: general capillary ECs (CAP1) and aerocyte capillary ECs (CAP2), have been identified, with CAP1 cells increasingly recognized as a heterogeneous and functionally diverse compartment that includes EC progenitors and reparative subpopulations. Emerging datasets further demonstrate arterial-venous polarization within the capillary bed and reveal gradients of gene expression that extend from macrovascular arteries and veins into the alveolar microvasculature. Within this polarized CAP1 landscape, several transcriptionally distinct EC subsets exhibit enhanced angiogenic potential and may contribute to EC regeneration during injury. This review synthesizes current knowledge of pulmonary capillary EC heterogeneity, emphasizing arterial-venous polarization of the capillary network, and the identification of reparative EC progenitors within the CAP1 population. We highlight emerging technologies including EC enrichment strategies, and transcriptomics, and epigenomic profiling that are beginning to resolve rare EC states and functional niches within the alveolar microvasculature. A deeper understanding of capillary EC diversity and lineage dynamics will be essential for identifying therapeutic targets aimed at restoring vascular stability, promoting regenerative angiogenesis, and preserving gas exchange in aging lungs and chronic lung diseases. - Source: PubMed
Publication date: 2026/06/02
Majka Susan MNiethamer Terren KCaporarello NunziaThorndyke Hannah FClair GeremyWest James DKarmouty-Quintana HarryAlvira Cristina M - Aberrant mitochondrial dynamics in podocytes are closely associated with the progression of diabetic nephropathy (DN); however, the underlying mechanisms remain incompletely understood. Recent research has demonstrated that cyclase-associated protein 1 (CAP1), an actin-binding protein, mediates mitochondrial fission. Therefore, we aimed to explore the regulatory role and mechanisms of CAP1 in high glucose (HG)-induced mitochondrial dysfunction in podocytes. CAP1 knockout reduced the severity of glomerular injuries and curtailed mitochondrial fission in podocytes in streptozotocin (STZ)-induced DN models. Subsequently, we observed that HG levels induced the mitochondrial translocation of CAP1 in podocytes, and CAP1 inhibition mitigated excessive mitochondrial fission. Mechanistically, our findings demonstrate that CAP1 facilitates HG-induced mitochondrial fission in podocytes by modulating actin reorganization. Furthermore, we present evidence that CAP1 interacts with Cofilin1, and this interaction plays a role in enhancing HG-induced mitochondrial fission in podocytes. This study elucidates the critical role of CAP1 in facilitating HG-induced mitochondrial fission in podocytes by regulating actin dynamics. These findings offer novel insights for the prevention and treatment of DN. - Source: PubMed
Publication date: 2026/06/01
Ma HuiminYao ShuangWang ZihanYu XinyingLi ZongdaZhang RuiLiang HaihaiJiao Jundong - Platelets are key mediators of hemostasis and thrombosis. Acid-sensing ion channel 3 (ASIC3), a proton-gated cation channel, can be directly activated at pH 7.4 by the synthetic compound 2-guanidine-4-methylquinazoline (GMQ). However, the role of GMQ in platelet activation and its potential dependence on ASIC3 remain unclear. This study investigated whether GMQ modulates platelet function at physiological pH (7.4), whether this regulation is mediated by ASIC3, and what the underlying molecular mechanisms are. We found that GMQ significantly suppressed platelet activation in both human and murine platelets at pH 7.4 and attenuated thrombus formation and hemostatic function in mice. ASIC3 was confirmed to be functionally expressed in human and murine platelets. Although ASIC3 deficiency did not affect basal platelet characteristics or platelet activation at pH 7.4, it markedly diminished GMQ-mediated suppression of platelet activation, thrombosis, and hemostasis. Mechanistically, GMQ enhanced cyclic adenosine monophosphate (cAMP) production and promoted protein kinase A (PKA) Thr197 phosphorylation through interaction with ASIC3-cyclase-associated protein 1 (CAP1), thereby suppressing platelet function. Overall, this study demonstrates, for the first time, that GMQ inhibits platelet activation and thrombosis under physiological pH by targeting ASIC3 and activating the CAP1/cAMP/PKA signaling pathway. These findings suggest that targeting the non-proton domain of ASIC3 at physiological pH may represent a novel and promising antiplatelet therapeutic strategy. - Source: PubMed
Publication date: 2026/05/30
Zhang PengLiu PengYu HanwenLiu DongshengWei MengZhang KandiHuang JianpengLi YingSu YuanyuanZhang TiantianZhang Junfeng