Ask about this productRelated genes to: Pcnp antibody
- Gene:
- PCNP NIH gene
- Name:
- PEST proteolytic signal containing nuclear protein
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 3q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 2006-03-06
- Date modifiied:
- 2014-11-19
Related products to: Pcnp antibody
Related articles to: Pcnp antibody
- Peripheral type cranial neuropathies (PCNP) other than idiopathic peripheral facial paralysis are quite rare. In this study, we analysed patients with PCNP who were treated in our inpatient clinic. - Source: PubMed
Publication date: 2026/01/31
Karabudak SaniyeMatur ZelihaÖzçelik PınarErdal YükselKula Aslı YamanGüzel VildanNalbantoğlu MecbureUslu FerdaAkman Gülşen - Homocysteine (Hcy) is an independent risk factor for atherosclerosis (AS). Hcy induces the transformation of vascular smooth muscle cells (VSMCs) into foam cells, which play a crucial role in this process. However, the detailed mechanism is still unclear. To identify the key regulatory proteins during this process and clarify the possible mechanism of Hcy-induced foam cell formation in VSMCs, thereby providing theoretical support for the intervention of AS. VSMCs were allocated into two groups: a control cohort and a group exposed to Hcy to simulate an AS-like state. Quantitative proteomic profiling was performed using the label-free quantitative DIA (LFQ-DIA) approach to detect differentially expressed proteins between these groups. To explore functional implications, enrichment analyses involving Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) pathways were conducted. Protein-protein interaction networks were constructed using the STRING database to identify central interactors. Target proteins were subsequently validated through parallel reaction monitoring (PRM). Furthermore, histological analyses (hematoxylin and eosin (HE) staining, Oil Red O staining), biochemical assays of lipid content (total cholesterol (TC) and triglycerides (TG)), and Western blot analysis were utilized to confirm the role and mechanism of identified proteins in the context of Hcy-driven foam cell conversion. The results showed that proteomic analysis identified 4804 proteins in total, of which 4799 passed missing-value filtering and were retained for downstream quantitative analysis. A total of 54 proteins were identified as differentially expressed using thresholds of adjusted p-value < 0.05 and fold change > 1.5. Among them, 13 proteins were upregulated, while 41 were downregulated in response to Hcy treatment. For PRM validation, 20 candidate proteins were selected according to proteomic evidence, biological relevance, and technical feasibility. Among them, 16 proteins (COX7C, STX5, UBQLN2, DDX50, TBCB, GSR, PCNP, CDV3, PEBP1, PPIA, S100A6, EIF4E2, UBQLN1, ARMC1, NUDCD2, and H1-2) showed the same direction of fold-change values as in the LFQ-DIA dataset, thereby underscoring the reliability of the proteomic analysis. Data are available via ProteomeXchange with identifier PXD064315. Histological staining demonstrated enhanced lipid accumulation, and the protein expression of the contraction phenotype marker a-SMA decreased, while the protein expression of the synthesis phenotype marker OPN increased. This indicates that Hcy induces VSMCs to transform from a contraction phenotype to a synthesis phenotype, resulting in the formation of foam cells. The protein levels of COX7C and sterol regulatory element-binding proteins (SREBP1C and SREBP2) were elevated upon Hcy exposure. Overexpression of COX7C further augmented the expression of SREBP1C and SREBP2, exacerbated lipid accumulation, and promoted foam cell transformation in Hcy-treated VSMCs. On the other hand, knockdown of COX7C had the opposite effect. Overall, the results of the present study suggest that COX7C plays a crucial regulatory role in Hcy-induced transformation of VSMCs into foam cells. Its pathogenic role is likely mediated through the upregulation of SREBP1C and SREBP2, thereby promoting lipid accumulation. These findings provide new insights into AS pathogenesis and identify COX7C maybe a potential therapeutic target. - Source: PubMed
Publication date: 2026/02/05
Wang XiuyuMa XinpengZhang XiangMa XingZhang Minghao - Patient dignity is fundamental to nursing ethics and care quality, yet nurses often face challenges in upholding it. This study examines how nurses' Job-Esteem influences their behaviors for maintaining patient dignity in China. - Source: PubMed
Publication date: 2026/01/07
Guo CongZhang ChunlinZhou CuizhuZhu MengqiChen LinglingLiu YouranZhang YequnWang JieLiang Tengfei - Retinal neovascularization (RNV) is a pathological hallmark of vision-threatening diseases such as diabetic retinopathy. Current therapies targeting vascular endothelial growth factors (VEGF) have limitations, highlighting the need for novel therapeutic targets. PEST-containing nuclear protein (PCNP) has been implicated in cell cycle regulation and tumorigenesis, but its function in endothelial cells and angiogenesis is unknown. This study aimed to explore the function and underlying mechanisms of PCNP in angiogenesis using an in vitro model. Human umbilical vein endothelial cells (HUVECs) were transfected to achieve PCNP overexpression or knockdown. The effects on key angiogenic processes were evaluated using cell proliferation (CCK-8), migration (wound healing), and tube formation assays. VEGF levels in culture supernatants and cell lysates were quantified by ELISA, Cytometric Bead Array (CBA), and Western blot. To identify potential molecular mechanisms, transcriptome sequencing was performed on PCNP-overexpressing HUVECs. PCNP overexpression significantly inhibited HUVEC proliferation, migration, and tube formation. Conversely, PCNP knockdown promoted these pro-angiogenic processes. Investigation into the role of VEGF yielded complex results; unexpectedly, supernatant VEGF levels were significantly reduced following both PCNP overexpression and knockdown, while intracellular VEGF levels remained unchanged. Transcriptome analysis of PCNP-overexpressing cells revealed a significant enrichment of genes associated with inflammatory signaling pathways, including the Interleukin-17 (IL-17), Tumor Necrosis Factor (TNF), and Nuclear Factor-kappa B (NF-κB) pathways. PCNP is a novel negative regulator of endothelial cell proliferation, migration, and tube formation in vitro. Its mechanism of action does not appear to involve direct modulation of VEGF expression and may instead be mediated through the regulation of key inflammatory signaling pathways. These findings identify PCNP as a potential new factor in the control of angiogenesis, warranting further investigation as a therapeutic target in neovascular diseases. - Source: PubMed
Publication date: 2025/12/11
Du YuxiXu ChaoyuanDang Yalong - The PEST-containing nuclear protein (PCNP) has been reported to play paradoxical roles in tumorigenesis. While PCNP functions as a tumor suppressor in neuroblastoma and lung adenocarcinoma, it has been identified as a tumor promoter in ovarian cancer. However, the underlying mechanisms driving these contrasting effects remain unclear. Gene Expression Profiling Interactive Analysis (GEPIA) was employed to analyze relevance of PCNP expression with prognosis in HCC. To evaluate the role of PCNP in hepatocellular carcinoma (HCC), we analyzed the expression of PCNP in 87 HCC tissues and 80 adjacent normal tissues. Correlation between PCNP and ubiquitin-like with PHD and ring finger domains 2 (UHRF2) was transcriptionally detected, and then their effects on malignant behaviors, including proliferation, invasion, tumor formation in vitro and in vivo were evaluated. According to tissues array results, it is found that PCNP was significantly upregulated in HCC tissues, which was further confirmed in HCC cell lines by western blotting. Importantly, both the cytoplasmic and nuclear PCNP fractions were correlated with pathological grade, T staging, clinical staging and recurrence, and patients with a high level of PCNP had lower overall survival and disease-free survival and a higher recurrence rate than those with a low PCNP level, indicating that PCNP might be an independent prognostic factor for HCC patients. Functional investigations revealed that PCNP knockdown inhibited malignant behaviors, including proliferation, invasion, colony formation and tumor formation, in vitro and in vivo. Pearson correlation analysis indicated a positive association between PCNP and UHRF2, with evidence that PCNP transcriptionally upregulates UHRF2. Furthermore, ectopic overexpression of PCNP activated the ErbB3/Ras/Raf1 signaling pathway through upregulation of UHRF2. Our findings suggest that PCNP promotes HCC progression by activating the ErbB3/Ras/Raf signaling pathway through upregulation of UHRF2. Consequently, PCNP holds potential as both a diagnostic biomarker and a therapeutic target for hepatocellular carcinoma. - Source: PubMed
Publication date: 2025/11/21
Luo JinlongZhou ZhiyiZhao XiangyuYang Yuting