Ask about this productRelated genes to: PFKP antibody
- Gene:
- PFKP NIH gene
- Name:
- phosphofructokinase, platelet
- Previous symbol:
- -
- Synonyms:
- PFK-C, PFKF
- Chromosome:
- 10p15.2
- Locus Type:
- gene with protein product
- Date approved:
- 1986-01-01
- Date modifiied:
- 2016-10-05
Related products to: PFKP antibody
Related articles to: PFKP antibody
- Reactive oxygen species (ROS) are critical regulators of tumor development and progression, yet their clinical significance and cellular mechanisms remain poorly defined in hepatocellular carcinoma (HCC). - Source: PubMed
Publication date: 2026/05/14
Xia XuesongXu HaoxuanLin GangChen LipingWei ShaomingLu Qinghui - Vitexin, a natural flavonoid compound, has shown anti-tumor effects, but its mechanism in Renal cell carcinoma (RCC) remains unclear. Galectin-1, a β-galactoside-binding lectin, promotes tumor progression through metabolic reprogramming. - Source: PubMed
Publication date: 2026/05/11
Wang XinjunBu YueLi ZhangqunZong QianWang XuqiangZhou BinLuo Guangcheng - Pestivirus bovine viral diarrhea virus (BVDV) is a major causative agent of bovine viral diarrhea-mucosal disease, responsible for substantial economic losses in the global cattle industry. BVDV employs sophisticated strategies to evade host antiviral innate immune responses; however, the precise mechanisms remain incompletely understood. In this study, we demonstrate that BVDV infection induces HIF-1α-mediated glycolytic reprogramming, which, in turn, antagonizes the RIG-I/MAVS pathway and suppresses type I interferon (IFN-I) production, thereby facilitating viral replication. We show that BVDV infection activates endoplasmic reticulum stress, leading to a marked increase in reactive oxygen species (ROS) that promote both the expression and stabilization of HIF-1α. As a key regulator of glycolysis, nuclear translocation of HIF-1α upregulates glycolysis-related proteins, including GLUT1, PFKP, HK2, and LDHA, thereby enhancing glycolytic flux. Furthermore, BVDV-induced glycolysis stimulates the formation of an HK2/MAVS/VDAC1 complex, which disrupts RIG-I-MAVS interaction and impairs pathway activation, inhibiting IFN-I production. Additionally, we found that lactate, a glycolytic byproduct, competitively binds to MAVS, impedes its mitochondrial localization, and consequently disrupts the engagement between RIG-I and MAVS. Collectively, our findings reveal a novel mechanism by which BVDV exploits the ROS-HIF-1α-glycolysis axis to attenuate MAVS-mediated antiviral signaling and promote viral replication. - Source: PubMed
Publication date: 2026/05/07
Li YuanZhou JiangfeiWang JingYan KaiGuan YuemingWang MengmengXiang JiayiLiu YimeiYu HanJia ShuoYang WentaoXu Yigang - Breast cancer is the leading cause of cancer-related deaths in women, primarily due to distant metastasis. Metabolic reprogramming plays a critical role in tumor growth and spread, but the metabolic mechanisms underlying metastasis in breast cancer remain unclear. The primary objective of this study is to identify molecular targets mediating breast cancer progression and to evaluate whether targeting the metabolic reprogramming represents a potential therapeutic strategy. - Source: PubMed
Publication date: 2026/04/22
Liu CongZhang ZhenyuFeng RonghuaZeng MengsiLi HuiZhu MeiZhuang LanLi ZongjuanWu Tao - Hepatocellular carcinoma (HCC) is associated with poor clinical outcomes, underscoring the need to identify novel biomarkers and therapeutic targets. PFKP, a key rate-limiting enzyme in glycolysis, is involved in tumor metabolic reprogramming, but its role in HCC prognosis, immune regulation, and therapeutic responsiveness remains incompletely understood. - Source: PubMed
Publication date: 2026/04/27
Cen LilanTian ZheHua HaomingLi ShengyiChen WanlingLu Junhua