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Validated All-in-One™ qPCR Primer for PLCG1(NM_002660.2) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
The protein encoded by this gene catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of receptor-mediated tyrosine kinase activators. For example, when activated by SRC, the encoded protein causes the Ras guanine nucleotide exchange factor RasGRP1 to translocate to the Golgi, where it activates Ras. Also, this protein has been shown to be a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase. Two transcript variants encoding different isoforms have been found for this gene.
Gene References into function
- Pharmacological and molecular inhibition of phospholipase C-gamma1 inhibits growth factor receptor-mediated invasion of breast and prostate tumor cells through Matrigel in vitro.
- Interaction of elongation factor-1alpha and pleckstrin homology domain of phospholipase C-gamma 1 with activating its activity
- Translocation of PKC[theta] in T cells is mediated by a nonconventional, PI3-K- and Vav-dependent pathway, but does not absolutely require phospholipase C
- Leukotriene D4 induces association of active RhoA with phospholipase C-gamma1 in intestinal epithelial cells.
- Phospholipase C gamma 1 is essential for NF-kappa B activation and lipid raft translocation of protein kinase C theta and the I kappa B kinase complex.
- activation of Src kinase by depletion of glucosylceramide-based glycosphingolipids in cultured ECV304 cells is a critical up-stream event in the activation of phospholipase C-gamma1.
- Stabilizes F-actin, preventing oxidative stress disruption of intestinal barrier. Essential for cellular prevention of oxidative stress of iNOS. Ability to suppress iNOS-driven reactions and cytoskeletal oxidation and disassembly.
- in response to Src-dependent activation of phospholipase Cgamma1, the Ras guanine nucleotide exchange factor RasGRP1 translocated to the Golgi where it activated Ras
- PLC gamma-dependent component of Fc epsilon RI-mediated calcium flux leading to degranulation of mast cells is independent of PI 3-kinase
- PLCgamma function and activation are mediated by GIT1 through c-Src, which integrates signal transduction by GPCRs and TKRs
- tr-kit promotes the formation of a multimolecular complex composed of Fyn, PLCgamma1 and Sam68, which allows phosphorylation of PLCgamma1 by Fyn, and may modulate RNA metabolism.
- T-cell receptor activation of Rap1 depends on phospholipase C-gamma1
- Treatment of cells of a carcinoma cell line with cysteine proteinase inhibitors results in increasing PLC1 intracellular level. Iyt is concluded that PLC1 is ubiquitinated and degraded by proteasomes.
- Data suggest that hyaluronan-CD44 interaction with Rac1-protein kinase N gamma plays a pivotal role in phospholipase C gamma1-regulated calcium signaling and cortactin-cytoskeleton function required for keratinocyte cell-cell adhesion and differentiation
- LAB resembled a LAT molecule unable to bind phospholipase C-gamma1.
- Tyr-783 phosphorylation of of phospholipase C-gamma 1 is not sufficient for enzyme activation
- SHP-2 has a role in regulating IL-1-induced Ca2+ flux and ERK activation via phosphorylation of PLCgamma1
- SLP-76 need not interact with SH3(PLC) to activate PLC-gamma1, and the P-I region of SLP-76 serves a structural role that is sequence-independent and is not directly related to protein-protein interactions
- activation of store operated channels in keratinocytes depends, at least partly, on the interaction of TRPC with PLCgamma1 and IP3R
- calcium activates PLC-gamma1 via increased PIP3 formation mediated by c-src- and fyn-activated PI3K
- PLCgamma1 in cell motility, functioning as a mediator of both growth factor and integrin-initiated signals
- PLC-gamma1 and PLC-gamma2 both regulate the functions of ITAM-containing receptors, whereas only PLC-gamma2 regulates the function of DAP10-coupled receptors.
- PLCgamma1 plays a pivotal role in the migration of human colorectal cancer cells, and the upregulation of NF-kappaB binding activity and downregulation of Hsp70 expression in LoVo cells.
- Data show that membrane transport of p42(IP4) induced by epidermal growth factor is inhibited by stimulation of phospholipase C-coupled thrombin receptor.
- phospholipase C-gamma1 interaction with villin regulates epithelial cell migration
- observations suggest a model in which TFII-I suppresses agonist-induced calcium entry by competing with TRPC3 for binding to phospholipase C-gamma
- High phosphatidylcholine-specific phospholipase C expression on the cell membrane surface is apparently involved in the ability of natural killer (NK) cytolytic cells to lyse sensitive target cells.
- We show that Fas-mediated apoptosis requires endoplasmic reticulum-mediated calcium release in a mechanism dependent on phospholipase C-gamma1 (PLC-gamma1) activation and Ca2+ release from inositol 1,4,5-trisphosphate receptor (IP3R) channels.
- Phospholipase C-gamma1 (PLC-gamma1) activation depends on a heterotrimeric complex of adaptor proteins such as SLP76.
- the recruitment of PI3K to the E-cadherin/beta-catenin/p120-catenin complex via beta-catenin at the plasma membrane is required for calcium-induced phospholipase C-gamma1 activation and, ultimately, keratinocyte differentiation
- Review discusses how the interaction between PLC-gamma1 and effector proteins plays a key role in on- or off-regulating PLC-gamma1-mediated cellular proliferation independent of its enzymatic activity.
- corecruitment of c-Cbl and PLCgamma1 to VEGFR-2 serves as a mechanism to fine-tune the angiogenic signal relay of VEGFR-2
- Results demonstrate that the gamma 1 isoform of phospholipase C associates with nuclear promyelocytic leukemia protein.
- Cellular knockdown of protein kinase Cepsilon (PKCepsilon) leads to decreased activation of PLCgamma1 by epidermal growth factor (EGF). EGF induces tyrosine phosphorylation of PKCepsilon as well as its association with EGF receptor and PLCgamma1.
- Results suggest that a PLCgamma-STAT1 pathway mediates apoptotic signaling by FGFR3 in genetic dwarfism and chondrogenic cell lines.
- The association of PLCgamma1 with complexes containing GIT1 and beta-Pix is essential for its role in integrin-mediated cell spreading and motility. As a component of this complex, PLCgamma1 is also involved in the activation of Cdc42 and Rac1.
- PLCgamma-mediated activation of PKCepsilon and PKCbetaI and intracellular calcium is involved in EGF-mediated protection of tight junctions from acetaldehyde-induced insult
- Controls tumor cell adhesion by controlling the RAP guanine nucleotide exchange factor (RAPGEF) molecular switch.
- HDAC8-selective inhibitors have a unique mechanism of action involving PLCgamma1 activation and calcium-induced apoptosis
- tau interactions with Src homology 3 domains of phosphatidylinositol 3-kinase, phospholipase Cgamma1, Grb2, and Src family kinases are regulated by phosphorylation
- PLSCR1 is a novel amplifier of FcepsilonRI signaling that acts selectively on the Lyn-initiated LAT/phospholipase Cgamma1/calcium axis, resulting in potentiation of a selected set of mast cell responses
- PLCgamma-1 and c-Src activation contribute to HNSCC invasion downstream of EGF receptor
- while Vav-1 and LAT preferentially bound to Syk, phospholipase C-gamma1 bound to both Syk and ZAP-70
- Data show a critical role of PLCgamma1 in the metastatic potential of cancer cells.
