Ask about this productRelated genes to: CACNA2D1 Blocking Peptide
- Gene:
- CACNA2D1 NIH gene
- Name:
- calcium voltage-gated channel auxiliary subunit alpha2delta 1
- Previous symbol:
- CACNL2A, CACNA2, MHS3, LINC01112
- Synonyms:
- lncRNA-N3
- Chromosome:
- 7q21.11
- Locus Type:
- gene with protein product
- Date approved:
- 1992-03-27
- Date modifiied:
- 2019-04-23
Related products to: CACNA2D1 Blocking Peptide
Related articles to: CACNA2D1 Blocking Peptide
- In the previous single-cell transcriptome analysis of goat ovulation, we identified that CACNA2D1 may play a critical role in immune cell infiltration during the ovulation process. Therefore, this study aimed to investigate the function of CACNA2D1 in ovulation. - Source: PubMed
Publication date: 2026/06/13
Guo ConghuiLiu JieChen KaihaoLiu GuangbinLiu DewuLi Yaokun - Chaihu Shugan San (CSS) is a classical traditional Chinese medicine formula widely used in improving depression. The purpose of this study was to investigate the molecular mechanisms underlying the antidepressant effects of CSS. - Source: PubMed
Wei XinHou LingchenBan ZiyunZang ShuxianZhang YuxuanWang MingyanAn FeiyuLiu YuqiLi De-PeiWang YuanyuanGao Yonggang - HIV-1 infection often results in sensory neuropathy, with more than 60% of affected individuals developing chronic pain. Although viral proteins such as glycoprotein 120 (gp120) contribute to neuronal injury and pain hypersensitivity, their specific effects on nociceptive signaling remain unclear. Hyperactivity of N-methyl-D-aspartate receptor (NMDAR) in the spinal dorsal horn is a hallmark of neuropathic pain. Here, we determined how gp120 affects synaptic NMDAR activity in spinal excitatory and inhibitory neurons in male and female mice. Intrathecal gp120 enhanced expression of α2δ-1 and GluN1 in the dorsal root ganglion and spinal cord. Gp120 also increased α2δ-1-GluN1 interaction and their synaptic trafficking in the spinal cord. Functionally, gp120 induced hyperactivity of presynaptic NMDARs on primary afferent terminals and postsynaptic NMDARs in vesicular glutamate transporter 2 (VGluT2)-expressing excitatory, but not vesicular GABA/glycine transporter (VGAT)-expressing inhibitory, dorsal horn neurons. Importantly, gp120-induced hyperactivity of both presynaptic and postsynaptic NMDARs was eliminated by the α2δ-1 inhibitory ligand gabapentin or by an α2δ-1 C-terminal peptide that disrupts α2δ-1-NMDAR interactions. Correspondingly, treatment with the NMDAR antagonist, gabapentin, or α2δ-1 C-terminal peptide consistently reversed gp120-induced persistent nociceptive hypersensitivity. Furthermore, genetic deletion of or selective ablation of GluN1 in dorsal root ganglion neurons significantly attenuated gp120-induced nociceptive hypersensitivity. Together, these findings indicate that gp120 drives nociceptive hypersensitivity by augmenting presynaptic and postsynaptic activity of α2δ-1-bound NMDARs, thereby amplifying nociceptive transmission from primary afferents to spinal excitatory neurons. Targeting α2δ-1-associated NMDARs may therefore represent a promising therapeutic approach for HIV-associated chronic neuropathic pain. HIV-associated chronic pain affects a large proportion of people living with HIV and remains challenging to treat. This study reveals how the HIV viral protein gp120 augments transmission from peripheral nerves to spinal cord neurons to produce persistent pain. We show that gp120 strengthens the interaction between the α2δ-1 protein and NMDA receptors in the spinal cord. Remarkably, gp120 selectively potentiates synaptic NMDA receptor activity in spinal excitatory, but not inhibitory, neurons, leading to heightened nociceptive sensitivity. Importantly, blocking α2δ-1 or disrupting its coupling with NMDA receptors reverses these effects and alleviates pain-like behaviors in animal models. These findings uncover a molecular mechanism underlying gp120-induced central sensitization and identify a potential therapeutic target for chronic pain in people with HIV. - Source: PubMed
Publication date: 2026/06/01
Gautam VipashaHuang 黄玉莹 YuyingChen 陈红 HongChen 陈少瑞 Shao-RuiPan 潘惠麟 Hui-Lin - The prevalence of coronary heart disease (CHD) continues to rise, and there is a lack of methods for early detection. To identify biomarkers for CHD, we analyzed the CACNA2D1 protein concentration in patients with different degrees of coronary artery stenosis to explore the correlation between plasma CACNA2D1 protein concentration and the severity of coronary artery stenosis. - Source: PubMed
Publication date: 2026/05/15
An LeRen YanhuiYang JinPei Zuowei - Tibetan chickens exhibit adaptive traits for the hypoxic Tibetan Plateau, yet how distinct ancestral inputs, their timing, and their functional consequences jointly shape this adaptation remains poorly understood. To address this, we integrated admixture modeling with ancestry tract-length dating across 1054 whole genomes, resolving three distinct ancestral sources-Northwest China (NWC), the Sichuan-Yunnan adjacent region (SYA), and the Southern Himalayan Foothills (SHF)-whose contributions are temporally stratified: NWC forms the deepest founding layer (>928 generations), SHF records an ancient but low-intensity signal (∼928 generations; 95% CI: 875-1024), and SYA reflects a major recent expansion (∼514 generations; 95% CI: 493-541) with stepwise diffusion across the plateau. Selection scans calibrated against a demographic null model indicated that these sources are enriched for distinct functional categories: NWC for vascular homeostasis and coagulation (e.g., VWF, TSPAN9), SYA for calcium signaling and metabolic regulation (e.g., CACNA2D1, AMY2A), and SHF for pulmonary vascular remodeling (e.g., AGTR1). These findings indicate that high-altitude adaptation in Tibetan chickens involves temporally layered contributions from multiple ancestral sources, each associated with distinct candidate functional pathways-a pattern consistent with human-mediated dispersal shaping the genetic architecture of highland populations. - Source: PubMed
Publication date: 2026/05/12
Zhao ZongyiNie RuixueFan HailuNgodroup TenzinZhu LiPan HongbinZhang BoZhang Hao