Ask about this productRelated genes to: PLCD1 Blocking Peptide
- Gene:
- PLCD1 NIH gene
- Name:
- phospholipase C delta 1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 3p22.2
- Locus Type:
- gene with protein product
- Date approved:
- 1997-05-09
- Date modifiied:
- 2018-04-18
Related products to: PLCD1 Blocking Peptide
Related articles to: PLCD1 Blocking Peptide
- Non-muscle invasive bladder cancer (NMIBC) is characterized by frequent recurrence, requiring repeated cystoscopic surveillance that is invasive and burdensome for patients. Although liquid biopsy approaches have been explored, clinically applicable non-invasive biomarkers that directly reflect tumor burden remain limited. As a proof-of-concept, we investigated whether somatic mutant proteins derived from bladder cancer cells can be detected and quantified in urinary extracellular vesicles (EVs) using a proteogenomic strategy. - Source: PubMed
Publication date: 2026/04/15
Hakozaki YujiSugimoto KazumaYamada YutaDanno TetsuyaHashimoto KenichiShinchi HirokiKume HarukiUeda Koji - Integrins are primary extracellular matrix receptors that play essential roles in homeostasis and development. Integrin activity is tightly regulated and is associated with conformational states. Although phosphatidylinositol 4,5-bisphosphate (PIP), produced by phosphatidylinositol 4-phosphate 5-kinases, is involved in integrin activation, it is unclear whether PIP-reducing enzymes affect integrin conformation and integrin-mediated cell behavior by altering PIP levels. Herein, we showed that phospholipase C (PLC) δ1, a PIP-hydrolyzing enzyme, affected integrin-mediated cell adhesion and migration. In PLCδ1 null murine fibroblasts and PLCδ1 knockdown-human melanoma cells, integrin-mediated cell behavior and basal PIP levels in the plasma membrane increased compared with those in control cells. PLCδ1 reduction led to increases in the extended conformation of integrin β1 ectodomain and the interaction between integrin and its activator/stabilizer talin in the absence of ligands. Overexpression of full-length-PLCδ1 or its pleckstrin homology domain but not their PIP-binding incompetent mutants inhibited the integrin-mediated cell behavior. To understand how altering plasma membrane PIP levels affects integrin-mediated cell behavior, the catalytic domain of PIP phosphatase was used. It reduced the basal levels of plasma membrane PIP, inhibited integrin-mediated cell migration, increased the closed conformation of the integrin β1 headpiece, and decreased integrin-talin interaction. These data suggested that the effects of PLCδ1 reduction were due to a PIP increase and that the plasma membrane PIP levels affected integrin conformation in the absence of ligands. Our results revealed that PLCδ1 finely tunes integrin-mediated cell adhesion and migration and integrin conformation by altering available PIP levels in the plasma membrane. - Source: PubMed
Publication date: 2025/12/12
Yoneda AtsukoFujinaka RyosukeTsuchiya NatsukiYaita SaoriSuzuki SachiKishi YuuNakamura YoshikazuSatow ReikoFukami Kiyoko - High-grade serous ovarian cancer (HGSOC) is the most common and aggressive subtype of epithelial ovarian cancer, characterized by rapid progression and poor prognosis. Despite advances in treatment, most cases are diagnosed at an advanced stage, and current diagnostic markers such as CA-125 have limited utility for early detection or treatment stratification. This study aimed to investigate the clinical significance and biological Function of phospholipase C delta 1 (PLCD1) in HGSOC. - Source: PubMed
Publication date: 2025/11/10
Kim Jue YoungShin Ha-YeonHaque RazaulKang Eun-SukKim Jae-Hoon - - Source: PubMed
Publication date: 2025/10/23
Lei XiaofengIzumi TeruakiOkuyama NatsukoShirouchi KazufumiKobayashi KaeYamochi ToshikoKim-Kaneyama Joo-RiInomata NaokoShimomura Yutaka - Phosphatidylinositol 4,5-bisphosphate [PI(4,5)P] is a phospholipid enriched on the cytoplasmic leaflet of the plasma membrane, where it plays important roles in membrane trafficking and cytoskeletal dynamics through proteins that directly bind to it. PI(4,5)P can be metabolized to other phosphorylated forms of phosphatidylinositol to regulate numerous processes such as cell growth and development. PI(4,5)P can also be hydrolyzed to generate the second messengers diacylglycerol (DAG) and inositol triphosphate (IP). Altered metabolism or mislocalization of PI(4,5)P can perturb one or more of its functions and contribute to disease states. Here, we present a protocol to visualize and quantify the localization of PI(4,5)P in live cells. The protocol uses a highly specific PI(4,5)P protein binding domain coupled to enhanced green fluorescence protein (PH-PLCD1-GFP), enabling localization and quantification of cytosol-facing PI(4,5)P to be determined. Localization and quantification of the PH-PLCD1-GFP, PI(4,5)P specific probe, is enabled by fluorescence imaging and confocal microscopy. This approach can be used to study the dynamics of PI(4,5)P localization temporally in live cells under both physiological and pathological conditions. Key features • Protocol for the quantification of PI(4,5)P membrane localization in live cells. • Uses the expression of the highly specific PH-PLCD1-GFP, PI(4,5)P probe, in cells, followed by fluorescence image acquisition using confocal microscopy and subsequent image processing. • Adaptable to various cell types and experimental conditions. • Presents detailed instructions for reagent preparation, fluorescence measurement, and quantification. - Source: PubMed
Publication date: 2025/06/05
Alkandari MariamMcMaster Christopher RTavasoli Mahtab