Ask about this productRelated genes to: HINT1 Blocking Peptide
- Gene:
- HINT1 NIH gene
- Name:
- histidine triad nucleotide binding protein 1
- Previous symbol:
- PRKCNH1, HINT
- Synonyms:
- PKCI-1
- Chromosome:
- 5q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1996-05-15
- Date modifiied:
- 2016-10-05
Related products to: HINT1 Blocking Peptide
Related articles to: HINT1 Blocking Peptide
- Atherosclerosis (AS) is the primary cause of most cardiovascular diseases, such as coronary artery disease (CAD), myocardial infarctions and strokes. S-nitrosylation (SNO), a prototypic redox-based posttranslational modification, is involved in cardiovascular diseases. Histidine triad nucleotide-binding protein 1 (HINT1) was identified S-nitrosylated at cysteine 84 (Cys84) in oxidized low-density lipoprotein (ox-LDL)-stimulated macrophages. S-nitrosylation of HINT1 (SNO-HINT1) in macrophages exacerbates lipid uptake and foam cell formation through upregulating SR-A1 and CD36. Furthermore, SNO-HINT1 was determined to inhibit degradation of SR-A1 mediated by lysosome pathway and promote CD36 transcription mediated by USF2. Mechanistically, comparing to unmodified HINT1, S-nitrosylation of HINT1 drives its CRM1 dependent nuclear export, which resulted in its more interaction with SR-A1 in cytoplasm and less interaction with USF2 in nucleus. Furthermore, inducible nitric oxide synthase (iNOS) was demonstrated as the enzyme that mediates the S-nitrosylation of HINT1. SNO-HINT1 was demonstrated to drive the development of atherosclerosis in LDLR mice fed with high fat diet. Overall, SNO-HINT1 drives foam cell formation and atherosclerosis through reducing degradation of SR-A1 mediated by lysosome pathway and promoting CD36 transcription mediated by USF2. Our findings suggest that SNO-HINT1 can be a potential therapeutic target for atherosclerosis. - Source: PubMed
Publication date: 2026/01/28
Tang KeZheng TianshuZhu HaoXu FanMa CongcongQi ZhenhuaCao SiyiDa QiangYan KeWu WenchengHan YiXie LipingZhang YanJi Yong - Depression leads to complex changes in protein regulation in the brain and other tissues. Reproducibility and data integration remain challenges in this field. We systematically integrated proteomic data from our previous established database Pro-MENDA, encompassing brain, cerebrospinal fluid (CSF), blood, and urine samples from patients with depression. Using a vote-counting statistics to assess consistency of protein expression changes across studies, we identified 2094 different expression proteins from 1804 samples. Functional characterization included Gene Ontology, KEGG pathway enrichment, protein-protein interaction analysis, and post-translational modification. In brain, we observed changes in proteins related to synaptic function and energy metabolism, such as Glial fibrillary acidic protein (GFAP) and Histidine triad nucleotide-binding protein 1 (HINT1). These changes suggest issues with oxidative phosphorylation and synaptic activity. The CSF and blood revealed immune-inflammatory markers like Afamin (AFM) and Serpin Family F Member 1 (SERPINF1), while urine analysis showed signs of neutrophil activation. We also identified 13 shared proteins across brain, CSF, and blood, including Clusterin (CLU), that link complement and coagulation, and reactive oxygen pathways. In this protein-protein interaction network of brain, proteins related to cell adhesion, respiration, neuron and synapse are significantly enriched. Post-translational modifications, particularly phosphorylation, were common. Our findings highlight systemic protein dysregulation in depression. This connects brain and peripheral mechanisms, offering insights for identifying multi-tissue biomarkers and developing targeted therapies. - Source: PubMed
Publication date: 2026/01/30
Xiang YajieDu XiaoyanYang HongmeiWang PengYin BangminWang ZhengyangWang HaiyangLiu LanxiangZhang HanpingRen YikunChen XiangyuRen YiLi WeiXie Peng - Protein ubiquitination is a key post-translational modification that governs protein stability and cellular homeostasis. KLHDC3 is a substrate recognition receptor in the recently identified C-terminal degron-mediated DesCEND ubiquitination pathway. It selectively binds proteins with C-terminal RxxxG motifs, targeting them for degradation. While N-terminal degron pathways are well-characterized, the physiological roles of C-terminal degrons remain poorly understood. To explore KLHDC3’s function in a physiological context, we generated mice deficient in the gene. - Source: PubMed
Publication date: 2026/01/28
Buco Paula Armina VHoque AshfaqulCastillo-Tandazo WilsonChalk Alistair MSmeets Monique FWalkley Carl R - Differentiating hereditary axonal polyneuropathies caused by distinct gene variants remains a clinical challenge. This comparative case study of DNAJB2- and HINT1-related neuropathies aimed to broaden the phenotypic spectrum associated with these genes and to explore non-motor symptoms and quality of life (QoL) in affected individuals. - Source: PubMed
Bjelica BogdanHendrich Corinnavon Hardenberg SandraVukojevic MilicaKörner SonjaGschwendtberger ThomasHaghikia AidenPeric StojanPetri Susanne - Venous thromboembolism (VTE) is a common vascular disease and a major cause of mortality. Development of early diagnostic biomarkers that accurately predict the occurrence of VTE is key for its initial management. The present study was designed to identify potential early diagnostic biomarkers based on the crosstalk between pyroptosis and VTE. The GSE19151 and GSE48000 datasets were utilized as the training and validation cohorts, respectively. Pyroptosis-related genes (PRGs) were sourced from the existing literature. Multiple bioinformatic analyses were conducted to pinpoint key PRGs in VTE. The possible functions of these genes were elucidated through gene set enrichment analysis (GSEA). Molecular regulatory networks were synthesized to probe into the underlying molecular mechanism of VTE. Moreover, a total of 5 pairs of frozen blood samples were analyzed quantifiably by reverse transcription-quantitative polymerase chain reaction (RT-qPCR) to evaluate the expression levels of these biomarkers. a total of Five critical biomarkers (RPL31, RPL34, RPL9, RPS27L and HINT1) were eventually screened, with significantly elevated expression levels observed in VTE samples in both the training and validation cohorts compared with control. The RT-qPCR results further confirmed that expression trends of these genes were consistent with those in the GSE19151 and GSE48000 datasets. GSEA indicated a correlation between the five biomarkers and ribosomal proteins as well as oxidative phosphorylation signaling pathways, suggesting their potential role in triggering VTE by regulating pyroptosis-inflammation-coagulation axis. A total of five critical pyroptosis-related biomarkers have been initially characterized, showing potential for early diagnosis of VTE. While these findings are promising, further investigation into the precise mechanisms and clinical thresholds is warranted. - Source: PubMed
Publication date: 2025/11/18
Han ShengbinXu JingzheYu ChenchenGuan HongxiDing Shun