PPAP2A Blocking Peptide
- Known as:
- PPAP2A Blocking Peptide
- Catalog number:
- 33r-2098
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- PPAP2A Blocking Peptide
Related genes to: PPAP2A Blocking Peptide
- Gene:
- PLPP1 NIH gene
- Name:
- phospholipid phosphatase 1
- Previous symbol:
- PPAP2A
- Synonyms:
- PAP-2a, LPP1
- Chromosome:
- 5q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-12-02
- Date modifiied:
- 2016-10-05
Related products to: PPAP2A Blocking Peptide
Related articles to: PPAP2A Blocking Peptide
- Lipid phosphate phosphatases (LPPs) dephosphorylate lipid phosphates to regulate signaling and metabolism. Among the three mammalian isoforms, LPP1, LPP2, and LPP3, LPP2 has been strongly associated with cancer, making it a potential therapeutic target. However, the molecular mechanisms underlying its structural organization, substrate recognition, and catalysis remain elusive. Here, we report the cryo-EM structure of human LPP2 (hLPP2). hLPP2 assembles as a homo-tetramer, with phosphatidylcholine bound in the substrate pocket. The tetrameric arrangement provides a structural basis for LPP oligomerization. The wide, open-ended substrate pocket explains the enzyme's broad substrate specificity. Structural comparison with PAP2 family members, including hG6PC1 and ecPgpB, suggests a conserved catalytic mechanism and highlights the regulatory role of residue E159 in stabilizing the catalytic center and phosphate release. Collectively, these findings advance our understanding of the structural basis and enzymatic mechanism of LPPs and may provide insights for the development of novel cancer therapies. - Source: PubMed
Publication date: 2026/05/01
Wang WanyiXu YueGuo PeilinHan HanHan Lei - Lipid metabolism disorder is known to promote fat accumulation and increase the risk of metabolic syndrome. Hexaconazole (Hex) has been reported to disrupt lipid homeostasis while its mechanism of action and enantioselective behavior remain unclear. Therefore, this study investigated the effects of Hex enantiomers on lipid metabolism in 3T3-L1 preadipocytes. The results showed Hex induced lipid droplet accumulation, total cholesterol (TC) content enhancement, along with the up-regulation of lipogenic genes and down-regulation of lipolytic genes in an enantioselective manner as (−)-Hex > Rac-Hex> (+)-Hex. Lipidomic analysis revealed the significant alterations in lipids of phosphatidylethanolamine (PE), phosphatidylglycerol (PG), and ceramide (Cer) by Hex exposure leading to the interference of glycerophospholipid and sphingolipid metabolism. Machine learning suggested that (−)-Hex achieved the highest binding affinity with phosphatidic acid phosphatase (PLPP1) resulting in the activation of PLPP1-PA/DAG signaling pathway. This study elucidated the potential mechanism of lipid disruption by Hex, providing a theoretical basis for assessing the enantiomer-specific health risks of triazole pesticides. - Source: PubMed
Publication date: 2026/04/28
Zhang JinxuYang TianmingLi ZiweiYang QianqianHuang ZhoubingSun Dali - Lung cancer is the leading cause of cancer-related deaths worldwide, yet there has been little attention given to the correlation between the cancer transcriptome and the incidence and mortality of lung cancer across different geographic regions. - Source: PubMed
Zhang LingFan CongShang HuanxiaWang XiaojingZhang XinQiao QingzheNi JiajiaWu Shucai - Lipid phosphate phosphatases (LPPs) catalyze the dephosphorylation of a broad range of bioactive lipid phosphates, including lysophosphatidic acid and sphingosine-1-phosphate, playing essential roles in embryonic vasculogenesis, cell differentiation and inflammation. Here we present the cryo-electron microscopic structure of human LPP1 as a tetramer with C4 symmetry. We capture the phosphohistidine intermediate state by using vanadate as a phosphate analog, where vanadate is coordinated by positively charged residues from three conserved motifs (C1, C2 and C3). Structural investigations of LPP1 variants with mutations in two catalytic histidine residues confirm that the histidine in the C2 motif facilitates phosphate bond cleavage. Enzymatic assays validate our structural observations. Additionally, a phosphatidylinositol 4,5-bisphosphate (PIP) molecule was discovered in the LPP1 structure, underscoring a potential regulatory role for PIP in the catalytic activity of LPP1. - Source: PubMed
Publication date: 2026/01/09
Yang MengSun ChunpingHe YonglinQian Hongwu - Feline panleukopenia, caused by the highly lethal feline parvovirus (FPV), lacks effective prevention and treatment strategies. This study aimed to elucidate the key metabolic regulatory mechanisms during FPV infection. - Source: PubMed
Publication date: 2025/08/22
Sun ZhenZhu HongweiLiu YangZhang JianlongJiang LinlinYu XinYu JiayuZhang Xingxiao