Ask about this productRelated genes to: PLCD1 antibody
- 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 antibody
Related articles to: PLCD1 antibody
- Phospholipase c-delta 1 (PLCD1), a key effector in the phospholipid signaling pathway, is indispensable for the growth and development of hair follicles (HF), but its regulatory mechanism in dermal papilla cells (DPCs), the core functional cells of HF, remains unclear. In this study, a PLCD1 knockout rabbit DPC in vitro model (PLCD1) was successfully constructed using CRISPR/Cas9 gene editing. PLCD1 knockout led to notable impairment of DPC physiological functions. Moreover, through transcriptome and metabolomics analyses, we examined differences in gene and metabolite profiles of DPCs between PLCD1 and wild-type (WT) groups, and performed an integrated association analysis of all differentially expressed genes (DEGs) and differential metabolites (DMs). The results showed widespread and significant positive and negative correlations between the screened DEGs and DMs, revealing a closely coordinated regulatory network between the transcriptome and metabolome at the global level after PLCD1 knockout. The functional status of the Hypoxia inducible factor-1 (HIF-1) and Mitogen activated protein kinase (MAPK) signaling pathways was further analyzed by Western blotting. The results showed that PLCD1 deficiency significantly affected the expression levels and phosphorylation status of key proteins in these two pathways. In summary, this study confirmed that PLCD1 deficiency impairs DPC function by inhibiting the HIF-1/MAPK signaling pathway, and the mechanism depends on the PLCD1-regulated gene-metabolite interaction network. This study provides an important theoretical basis for analyzing the regulatory mechanisms of HF growth and development and clarifies that PLCD1 and its downstream gene-metabolic network may serve as potential therapeutic targets for hair-related diseases. - Source: PubMed
Cai JiaweiZhao BohaoLi YunpengChen XinCao XinyuWang SenWang LeiChen YangWu Xinsheng - NR5A2 is a key regulator of zygotic genome activation (ZGA), which primarily takes place at the 4-8-cell stage in porcine embryos; however, its associated metabolic programs remain largely uncharacterized. In this study, single-blastomere RNA sequencing was performed using Smart-seq2 in 8-cell-stage porcine embryos derived from in vitro fertilization (IVF) or somatic cell nuclear transfer (SCNT). Based on the bimodal expression pattern of NR5A2, individual blastomeres were categorized into NR5A2-active and NR5A2-inactive groups. Differential expression analysis identified 46 differentially expressed genes (DEGs) in IVF embryos, which were mainly enriched in steroid hormone and lipid metabolism. In SCNT embryos, the top-ranked DEGs were functionally associated with mitochondrial respiration and ribosome biogenesis. A total of 14 NR5A2-associated DEGs were consistently identified in both embryo types and clustered into three core metabolic modules: glycolysis and energy metabolism (represented by HK2), lipid and steroid metabolism (including STAR, LIPG, PLCD1 and DLC1), and inositol metabolism (represented by MIOX). Single-blastomere qRT-PCR in parthenogenetic embryos further validated the bimodal expression of NR5A2, HK2, STAR and MIOX. Collectively, this study reveals an NR5A2-associated metabolic transcriptional signature in blastomeres of both IVF and SCNT embryos. These findings identify candidate metabolic genes that may inform future optimization of in vitro culture media to enhance the developmental competence of porcine embryos and warrant subsequent functional validation. - Source: PubMed
Publication date: 2026/07/23
Li ZihanXie FuhengHe YuqingMa LiLiang ShuangLiu Qiang - Despite excitotoxicity being a pivotal pathological mechanism in various retinal diseases, effective clinical interventions remain limited. Previous study has shown that adipose stem cell-derived extracellular vesicles (ADSC-EVs) can alleviate glutamate-induced retinal ganglion cells (RGCs) death by suppressing protein kinase C alpha (PKCA) pathway and increasing the expression of α-amino-3-hydroxy-5-methyl-4-isoxazoleproprionic acid receptors (AMPARs) subunit 2 (GluA2) on the cell membrane, but the mechanisms remain unexplored. - Source: PubMed
Publication date: 2026/06/30
Tianqi DuanHuizhuo XuShibo TangHaiyang YuAixiang LuoMing LiJufang Huang - 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