TY - JOUR. T1 - Requirement of phospholipase C-γ2 (PLCγ2) for dectin-1-induced antigen presentation and induction of TH1/TH17 polarization. AU - Tassi, Ilaria. AU - Cella, Marina. AU - Castro, Iris. AU - Gilfillan, Susan. AU - Khan, Wasif N.. AU - Colonna, Marco. PY - 2009/5. Y1 - 2009/5. N2 - DC recognize microbial components through an array of receptors known as PRR. PRR initiate intracellular signals, which engender DC with the capacity to stimulate T-cell responses. Dectin-1 is a PRR that recognizes β-glucan, a major constituent of many fungis outer cell wall. Here we show that Dectin-1 activates DC through phospholipase (PLC)γ2 signaling. PLCγ2-deficient DC were unable to expand antigen-specific T cells and induce TH1 and TH17 differentiation in response to β-glucan. Mechanistically, PLCγ2-deficiency impaired the capacity of DC to secrete polarizing cytokines following exposure to β-glucan. Dectin-1 required PLCγ2 to activate MAPK, AP-1 and NF-κB, which induce cytokine gene ...
Phospholipase C-(gamma) (PLC-(gamma)) is activated in many cell types following growth factor stimulation. Our understanding of the role of PLC-(gamma) in cell growth and differentiation has been severely limited by the dearth of mutations in any organism. In this study, we show that the Drosophila gene small wing (sl), identified by Bridges in 1915, encodes a PLC-(gamma). Mutations of sl result in extra R7 photoreceptors in the compound eye, consistent with overactivation of the receptor tyrosine kinase pathways that control R7 development. The data presented here provide the first genetic evidence that PLC-(gamma) is involved in Ras-mediated signaling and indicate that PLC-(gamma) acts as a negative regulator in such pathways in Drosophila.. ...
AB - Phospholipases C play a role in the pathogenesis of several bacteria. Mycobacterium tuberculosis, the causative agent of tuberculosis, possesses four genes encoding putative phospholipases C, plcA, plcB, plcC and plcD. However, the contribution of these genes to virulence is unknown. We constructed four single mutants of M. tuberculosis each inactivated in one of the plc genes, a triple plcABC mutant and a quadruple plcABCD mutant. The mutants all exhibited a lower phospholipase C activity than the wild-type parent strain, demonstrating that the four plc genes encode a functional phospholipase C in M. tuberculosis. Functional complementation of the Delta plcABC triple mutant with the individual plcA, plcB and plcC genes restored in each case about 20% of the total Plc activity detected in the parental strain, suggesting that the three enzymes contribute equally to the overall Plc activity of M. tuberculosis. RT-PCR analysis of the plc genes transcripts showed that the expression of these ...
The data presented in this study demonstrate that activation of PKC-ε on stimulation of the A1R in the rat or mouse heart elicits the translocation of the kinase to a RACK2 protein of the cardiomyocyte. Previously, we reported A1R activation promotes the translocation of PKC-ε, but not PKC-δ, to the t-tubules of the cardiomyocyte (30). The present data indicate that RACK2 was the target protein for this translocation. Our present observations include the measurement of contractile activity of isolated cardiomyocytes and the visualization with imaging (rat) and coimmunoprecipitation of the kinase and RACK2 (rat and mouse). Translocation of PKC-ε to RACK2 occurred whether the PKC-ε was activated nonspecifically by a phorbol ester, or by A1R activation with PIA, or with the selective agonist CCPA. The action induced by CCPA was selective for the A1R, as indicated by the inhibition elicited by the A1R antagonist DPCPX. Furthermore, PKC-ε translocation most likely results from an A1R-induced ...
Similarly, splenic B cells from one to 4 month old premalignant iMycEu mice exhib ited highly elevated NFB and STAT3 DNA binding exercise, at as early as one month of age, relative to splenic B cells from age matched, typical BL6 mice. These data show that constitutive activation of the two NFB and STAT3 happens months before tumors are current, and at an early age, in iMycEu mice. We also evaluated the degree of Myc protein in splenic B cells of premalignant and malignant iMycEu mice, likewise as in iMycEu one cells. Its broadly accepted the cellular level of Myc must continue to be exquisitely titrated to induce neoplastic growth but steer clear of apoptosis. Consistent with this particular, only a marginal elevation of Myc protein was repeat edly observed in premalignant iMycEu B splenocytes. Myc protein was, however, drastically elevated in malignant B cells and in iMycEu one cells. Despite the fact that NFB and STAT3 are acknowledged to drive Myc expression, constitutive exercise of NFB and ...
Phospholipase C (PLC) cleaves phosphatidylinositol 4,5-bisphosphate to form the second messengers inositol 1,4,5-trisphosphate and diacylglycerol. Recently, PLC-L2, a PLC-like protein that lacks lipase activity, has been identified in skeletal muscle, as well as in B and T lymphocytes. Takenaka et al. generated PLC-2-deficient mice to investigate the possible role of PLC-2 signaling in B lymphocytes. PLC-L2-deficient mature B cells showed an enhanced proliferative response and increased expression of the activation marker CD69 after B cell receptor (BCR) stimulation in vitro, and mice displayed increased production of immunoglobulin M (IgM), IgG1, and IgG3 in response to antigen treatment in vivo. The authors used fura-2 imaging to show that Ca2+ influx after BCR stimulation was enhanced in PLC-2-deficient cells; moreover, translocation of nuclear factor of activated T cells (which is regulated by calcineurin, which is itself calcium-dependent) was enhanced. Finally, PLC-2-deficient cells showed ...
This study reports the successful purification of the P2Y12-R to near homogeneity. The purified receptor, when stimulated by 2MeSADP, functionally activates reconstituted purified G proteins, promoting GTPase activity that is greatly augmented by RGS4. This reconstitution system provides the most unambiguous means available to date to assess the pharmacological selectivity of the P2Y12-R and to directly determine its Gα-subunit selectivity.. The P2Y12-R was one of the first receptors illustrated to inhibit adenylyl cyclase and the first P2Y receptor studied biochemically (Cooper and Rodbell, 1979). Subsequent investigations revealed the P2Y12-R to be a unique member of the P2Y receptor family in that it coupled to Gαi rather than Gαq (Hollopeter et al., 2001). The eventual cloning of the P2Y12-R revealed a sequence with very low homology to the five previously cloned Gq/phospholipase C-coupled P2Y receptors (Foster et al., 2001; Hollopeter et al., 2001; Takasaki et al., 2001; Zhang et al., ...
PLC activity is required for directional protrusion in response to an EGF source. (A) The response of a control (U73343) cell (top) and of a PLC-inhibited (U731
Together, the results from this study provide evidence for B1 receptor homo-oligomerization and the importance of this mechanism in the expression of the receptor on the cell surface of HEK293 cells. This mechanism directly translates into the presentation of a constitutive mechanism for cellular signaling through Gq/11-mediated phospholipase Cβ activity. Such homo-oligomers may be a regulatory point in B1 receptor maturation, and their disruption could provide a unique way for silencing signaling through this and other B1 receptor-stimulated pathways during inflammation.. Multiple methods were used to investigate whether B1 receptors form homo-oligomers in HEK293 cells. Although neither of these methods alone is sufficient to prove oligomerization, together they are consistent with such a mechanism. Higher order oligomeric receptor forms were readily apparent on immunoblots of SDS-PAGE gels. Such complexes were also indicated by coimmunoprecipitation of differentially tagged receptors. ...
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PLC-γ1 contains two SH2 domains and one SH3 domain. On the basis of our data showing a constitutive association between RIAM and PLC-γ1 that was enhanced after stimulation of the TCR (Fig. 5A), we hypothesized that RIAM might interact with the SH3 domain of PLC-γ1 through its proline-rich regions (PRRs) before stimulation of T cells; after undergoing tyrosine phosphorylation, RIAM might also interact with the SH2 domains of PLC-γ1. To test these possibilities, we first investigated whether the interaction between RIAM and PLC-γ1 was direct. We examined a potential interaction between PLC-γ1 and RIAM in an in vitro protein association assay. Glutathione S-transferase (GST) and GST fusion proteins of full-length PLC-γ1, the N-terminal and C-terminal SH2 domains of PLC-γ1 (PLC-γ1-N+C-SH2), and the SH3 domain of PLC-γ1 (fig. S4A) were coupled to glutathione-Sepharose and incubated with [35S]methionine-labeled RIAM or luciferase, as a negative control. Full-length PLC-γ1 and the SH3 domain ...
0004]The present invention comprises the method of treating host organisms (i.e. human or animal) in need of a drug having anti-neoplastic activity comprising the administration of a therapeutically effective amount of venom anti-serum either alone or preferably in combination with a Phospholipase C inhibitor of non-toxic nature or monoclonal or polyclonal anti-serum to Phospholipase C enzyme or a vaccine containing in whole or in part venom and/or other components of animal, insect or plant origin showing Phospholipase A2 and/or Phospholipase C activity. This patent presents pharmaceutical formulations containing snake and/or insect venoms, or extracts from such venoms which may contain, total or partial, Phospholipase A2 enzyme activity alone or in combination with animal or plant Phospholipase A2 with or without Phospholipase C inhibiting compounds or Phospholipase C mono or polyclonal anti-serum to Phospholipase C enzyme as therapeutic vaccine candidate for all neoplastic diseases. This ...
TY - JOUR. T1 - Distinct CCK-2 Receptor Conformations Associated with β-Arrestin-2 Recruitment or Phospholipase-C Activation Revealed by a Biased Antagonist. AU - Magnan, Rémi. AU - Escrieut, Chantal. AU - Gigoux, Véronique. AU - De, Kavita. AU - Clerc, Pascal. AU - Niu, Fan. AU - Azema, Joelle. AU - Masri, Bernard. AU - Cordomi, Arnau. AU - Baltas, Michel. AU - Tikhonova, Irina G. AU - Fourmy, Daniel. PY - 2013/2/20. Y1 - 2013/2/20. N2 - Seven-transmembrane receptors (7TMRs), also termed G protein-coupled receptors (GPCRs), form the largest class of cell surface membrane receptors, involving several hundred members in the human genome. Near 30% of marketed pharmacological agents target 7TMRs. 7TMRs adopt multiple conformations upon agonist binding. Biased agonists, in contrast to non-biased agonists, are believed to stabilize conformations preferentially activating either G-protein- or ß-arrestin-dependent signalling pathways. However, proof that cognate conformations of receptors display ...
Phylogenetic analysis of PLC-γ proteins: The PLC-γ homolog encoded by sl is the only one present in the now almost-complete D. melanogaster genome sequence, and only a single gene has been identified in the other invertebrate genomes sequenced to date. By contrast, a gene duplication event produced separate γ1 and γ2 subtypes at some point in the vertebrate lineage; each subtype has identical domain structure and similar sequence, but distinct functions. To reveal the relationships between PLC-γ homologs, we produced a translation of the putative ORFs from both D. pseudoobscura and D. virilis and compared them to all other complete PLC-γ homologs in the GenBank database, including D. melanogaster, the mosquito Anopheles gambiae, the sponge E. fluviatilis, the nematode Caenorhabditis elegans, the cow Bos taurus (γ1), the rat Rattus rattus (γ1 and γ2), and Homo sapiens (γ1 and γ2). The best tree from this comparison is shown in Figure 1A. The tree divides the taxa unambiguously into a ...
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Phospholipase C (PLC) regulates various cellular processes by catalyzing the formation of inositol-1,4,5-trisphosphate (IP3) and diacylglycerol from phosphatidylinositol-4,5-bisphosphate (PIP2). Here, we have investigated the influence of Ca2+ on receptor-triggered PLC activity in individual insulin-secreting β-cells. Evanescent wave microscopy was used to record PLC activity using green fluorescent protein (GFP)-tagged PIP2/IP3-binding pleckstrin homology domain from PLCδ1, and the cytoplasmic Ca2+ concentration ([Ca2+]i) was simultaneously measured using the indicator Fura Red. Stimulation of MIN6 β-cells with the muscarinic-receptor agonist carbachol induced rapid and sustained PLC activation. By contrast, only transient activation was observed after stimulation in the absence of extracellular Ca2+ or in the presence of the non-selective Ca2+ channel inhibitor La3+. The Ca2+-dependent sustained phase of PLC activity did not require voltage-gated Ca2+ influx, as hyperpolarization with ...
최근 외부자극에 대한 생체 신호전달체계에서 중요한 효소로 알려진 phospholipase C(PLC) 동위효소(isozyme)들의 발현은 조직의 종류와 발달과정에 따라 특이한 양상을 보이며 PLC동위효소 중 PLC-γ1은 세포의 성장, 분화 및 증식에 중추적 요소로 알려져 있다. 또한 ras 암유전자단백도 세포의 성장을 유도하는 것으로 알려져 있어 방사선 조사 후 PLC 동위효소와 ras암유전단백이 관여하는지를 규명하고, 이러한 재생과정에 방사선감작약물로 널리 알려져 있는 5-fluorouracil(5-FU)투여방법이 미치는 영향을 보고자 본 연구를 계획하였다. 흰쥐를 실험동물로 하여 정상대조군(I), 방사선조사 단독군(II), 방사선과 5-FU 12시간 지속성 정주병행군(III), 방사선조사 단독군 (II), 방사선과 5-FU12시간 지속성 정주단독군 (V), 5FU 일시정주단독군 (VI)로 나누어 관찰하였다. 방사선은 흰쥐 ...
Gemphire Therapeutics (NASDAQ: GEMP) and GW Pharmaceuticals PLC- (NASDAQ:GWPH) are both medical companies, but which is the superior business? We will compare the two companies based on the strength of their risk, valuation, earnings, dividends, institutional ownership, profitability and analyst recommendations. Analyst Ratings This is a summary of current ratings and price targets for Gemphire […]
Plasmid pGEX PLCg1(NC)-SH2 from Dr. Bruce Mayers lab contains the insert PLCg1(NC) and is published in Mol Cell. 2007 Jun 22;26(6):899-915. This plasmid is available through Addgene.
We are interested in learning how small molecules in the blood stream can cause cells to react in specific ways, such as growing, dividing or migrating. While there are many agents that can stimulate or inhibit cell behavior, we are most interested in the ability of certain hormones and neurotransmitters to activate a family of proteins called "G Proteins". G proteins can simulate an enzyme called phospholipase Cbeta (PLCbeta). Activation of PLCbeta raises the level of calcium in the cell, which changes the activity of many other proteins. Additionally, PLCbeta can also affect the ability of a cell to control the transcription of specific genes into proteins by changing the stability of their messenger RNA. ...
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Overexpression on plasma membrane of human epidermal growth factor receptor 2 (HER2) is reported in 25% to 30% of breast cancers. Heterodimer formation with cognate members of the epidermal growth factor receptor (EGFR) family, such as HER3 and EGFR, activates abnormal cell-signalling cascades responsible for tumorigenesis and further transcriptional HER2 gene upregulation. Targeting the molecular mechanisms controlling HER2 overexpression and recycling may effectively deactivate this feedback-amplification loop. We recently showed that inactivation of phosphatidylcholine-specific phospholipase C (PC-PLC) may exert a pivotal role in selectively modulating the expression on the membrane of specific receptors or proteins relevant to cell function. In the present study, we investigated the capability of PC-PLC inhibition to target the molecular mechanisms controlling HER2 overexpression on the membrane of breast cancer cells by altering the rates of its endocytosis and lysosomal degradation. Localization
This study was undertaken to define pathways by which LPS might activate the ERK kinases in alveolar macrophages. We hypothesized that LPS activates a PC-PLC, leading to production of DAG, an activator of sphingomyelinase activity. This, in turn, results in increased amounts of ceramide, an important effector molecule, which activates PKC ζ. PKC ζ activates MEK, which subsequently leads to ERK kinase activation. To test this hypothesis, we showed that LPS activates the ERK 2 kinase in alveolar macrophages and that this activation is inhibited by D609, a relatively specific inhibitor of PC-PLC. We next showed that LPS increases amounts of DAG and ceramide and that both of these effects of LPS are inhibited by D609. Our present studies indicate that LPS induction of DAG in alveolar macrophages is derived, at least in part, from a PC-containing phospholipid. Thus, we conclude from these experiments that the LPS-induced DAG is derived from hydrolysis of PC via activation of PC-PLC. In separate ...
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Required for secondary responses to abscisic acid signals.
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.
... , Authors: Matilde Y. Follo, Vincenza Rita Lo Vasco, Giovanni Martinelli, Giandomenico Palka, Lucio Cocco. Published in: Atlas Genet Cytogenet Oncol Haematol.
TY - JOUR. T1 - Phospholipase β4-knockout mouse exhibits retinal phenotype. AU - Jiang, Huiping. AU - Lyubarsky, A.. AU - Vardi, N.. AU - Pugh Jr, Edward N. AU - Chen, J.. AU - Xu, J.. AU - Simon, M. I.. AU - Wu, Dianqing. PY - 1996/2/15. Y1 - 1996/2/15. N2 - Purpose: Determine if PLC-β4 has a retinal function by making/assessing a mouse knockout. Rationale: PLC-β4 is one of the four PLC-β isoforms that have been cloned and can be activated by the Gα subunits of G-proteins of the Gq class, but not by the Gβγ subunits. PLC-β4 shares a closer homology to the NorpA protein (which mediates phototransduction in Drosopnila) than to the isoforms PLC-β1-β3. Previous immunohistochemical studies have shown that PLC-β4 is expressed in cone photoreceptors, and in bipolar and ganglion cells1. Method: A mouse line was generated in which the PLC-β4 genes are disrupted. Retinal rod function was assessed with single-flash a- and b-wave electroretinography. Anatomical analysis of rod density, rod ...
1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1 is an enzyme that in humans is encoded by the PLCD1 gene. PLCd1 is essential to maintain homeostasis of the skin. Phospholipase C GRCh38: Ensembl release 89: ENSG00000187091 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000010660 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Ishikawa S, Takahashi T, Ogawa M, Nakamura Y (Nov 1997). "Genomic structure of the human PLCD1 (phospholipase C delta 1) locus on 3p22→p21.3". Cytogenet Cell Genet. 78 (1): 58-60. doi:10.1159/000134629. PMID 9345909. "Entrez Gene: PLCD1 phospholipase C, delta 1". Yagisawa H (2006). "Nucleocytoplasmic shuttling of phospholipase C-delta1: a link to Ca2+". J. Cell. Biochem. 97 (2): 233-43. doi:10.1002/jcb.20677. PMID 16240320. Cefai D, Debre P, Kaczorek M, et al. (1991). "Human immunodeficiency virus-1 glycoproteins gp120 and gp160 specifically inhibit the CD3/T cell-antigen receptor phosphoinositide transduction pathway". ...
The activity of the early signaling enzyme, phospholipase Cβ1b (PLCβ1b), is elevated in diseased myocardium and activity increases with disease progression. PLCβ1b and the alternative splice variant, PLCβ1a, were expressed in mouse hearts using adeno-associated viral constructs (rAAV6-FLAG-PLCβ1b, rAAV6-FLAG- PLCβ1a) delivered intravenously. Functional responses were assessed in vivo and confirmatory mechanistic studies were conducted in neonatal rat ventricular myocytes (NRVM). FLAG-PLCβ1b was expressed in all of the chambers of the mouse heart, but was highest in left ventricle, where expression was observed in ,90% of the cells and was localized to the sarcolemma and T-tubules. Heightened PLCβ1b expression caused a rapid loss of contractility and down-regulation of Phospholamban expression. The loss of contractility induced by PLCβ1b was reversed by inhibition of protein kinase Cα (PKCα). PLCβ1a did not affect contractile function or phospholamban expression. Mechanistic analysis ...
Wright, Michelle H., Farquhar, Michelle J., Aletrari, Mina-Olga , Ladds, Graham and Hodgkin, Matthew N.. (2008) Identification of caspase 3 motifs and critical aspartate residues in human Phospholipase D1b and Phopsholipase D2a. Biochemical and Biophysical Research Communications, Vol.369 (No.2). pp. 478-484. ISSN 0006-291x ...
... δ-1 Phosphatidylinositol-specific phospholipase C Identifiers Symbol PI-PLC-X Pfam PF00388 InterPro IPR000909 SMART PLCXc SCOP
Calcineurin has functions in T cell activation, activation-induced cell death (AICD), T cell tolerance, ion channel regulation, cardiac myocyte hypertrophy, sperm motility, synaptic endocytosis, and Alzheimers disease (17-20). In lymphocytes, antigen engagement of lymphocyte receptors promotes the activation of phospholipase C-γ (PLC-γ) (Figure 10). Activated PLC-γ hydrolyzes phosphatidylinositol-4,5-bisphosphate into inositol-1,4,5-trisphosphate (IP3) and diacylglycerol. IP3 then binds to receptors on the endoplasmic reticulum and drives Ca2+ release from the endoplasmic reticulum into the cytoplasm, which triggers opening of Ca2+ release-activated Ca2+ channels. Calcineurin is activated by binding of CaM in response to sustained increased levels of intracellular calcium (11;21). Upon calcineurin activation, it dephosphorylates members of the nuclear factor of activated T cells (NFAT) family, promoting their translocation from the cytosol to the nucleus and subsequent induction of the ...
Complete information for PLCXD3 gene (Protein Coding), Phosphatidylinositol Specific Phospholipase C X Domain Containing 3, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
PubMed lists over 1,500 papers with U73122 in the abstract. The large majority use the inhibitor simply as a tool to check that some signaling pathway requires PLC. However, numerous papers report additional unexpected effects, raising question whether this agent can be used as a pharmacological tool without serious side effects. We select results from just four early papers. The initial brief announcement of U73122 from Upjohn reports that it inhibits partially purified PLC in vitro when the molar ratio of Ca2+:PI in the assay was ,2, but "increased PLC activity" when the molar ratio was 4-12 (Bleasdale et al., 1989). There are no data or experimental details in that book chapter. A careful study in NG108-15 neuroblastoma-glioma cells and in dorsal root ganglion cells shows that U73122 blocks bradykinin-induced Ca2+ transients irreversibly with a steep dose-response curve and a half-effective dose IC50 of 200 nM for 20-min preincubations and that U73343 is without effect (Jin et al., 1994). ...
Certainly, 6 ME did not have an impact on VEGF induced phosphorylation of AKT, one of the key cascades that confer endothelial cell survival, Likewise, six ME did not have an impact on VEGF induced phosphorylation of p38 MAPK, a signaling cascade that mediates the induction selleck chemicalWZ4003 of endothelial cell migration by VEGF, These success, along with the truth that six ME isnt going to inhibit PLC activation, as VEGF induced calcium release in not impacted, exclude the kinase exercise of VEGFR2 KDR of becoming the target of six ME. In confirmation, six ME plainly inhibited, at 10uM concentration, the phosphorylation of MEK1 two and its downstream target ERK1 two, parts from the mitotic MAPK pathway that VEGF triggers by means of PLC activation. Numerous growth factors acti vate the ERK1 two MAPK pathway in a Ras dependent manner, Without a doubt, 6 ME inhibited also FGF2 induced phosphorylation of ERK1 2 absolutely compatible together with the undeniable fact that 6 ME inhibited also ...
1P5X: Using X-ray crystallography of the Asp55Asn mutant of the phosphatidylcholine-preferring phospholipase C from Bacillus cereus to support the mechanistic role of Asp55 as the general base.
Plasmid TrkB Acceptor from Dr. Ryohei Yasudas lab contains the insert Phospholipase C gamma 1 and is published in Nature. 2016 Sep 28;538(7623):99-103. doi: 10.1038/nature19766. This plasmid is available through Addgene.
Yue, Caiping and Ku, Chun-Ying and Liu, Mingyao et al. (2000) Molecular Mechanism of the Inhibition of Phospholipase C β3 by Protein Kinase C. Journal of Biological Chemistry, 275 (39). pp. 30220-30225. ISSN 0021-9258. https://resolver.caltech.edu/CaltechAUTHORS:YUEjbc00 ...
a receptor for 5-hydroxytryptamine (serotonin); activates phospholipase C signaling pathway; involved in promoting cellular transformation
Orome1 writes Many prisons and jails use SCADA systems with PLCs to open and close doors. Using original and publicly available exploits along with evaluating vulnerabilities in electronic and physical security designs, researchers discovered significant vulnerabilities in PLCs used in correctional...
Screening of inhibitors of porcine dipeptidyl peptidase IV activity in aqueous extracts from marine organisms, Pascual, Isel, Lopéz Alí, Gómez Hansel, Chappé Mae, Saroyán Angélika, Gonzalez Yamile, Cisneros Miguel, Charli Jean Louis, and Chávez María de los Ang , Enzyme Microb. Technol., Volume 40, Number {3, SI}, {360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA}, p.414-419, (2007) ...
The IUPHAR/BPS Guide to Pharmacology. PLD1 - Phosphatidylcholine-specific phospholipase D. Detailed annotation on the structure, function, physiology, pharmacology and clinical relevance of drug targets.
Nuclear envelope assembly is promoted by phosphoinositide- specific phospholipase C with selective recruitment of phosphatidylinositol-enriched membranes Nuclear envelope (NE) formation in a cell-free egg extract proceeds by precursor membrane vesicle binding to chromatin in an ATP-dependent manner, followed by a GTP-induced NE assembly step. The requirement for GTP in the latter step of this process can be mimicked by addition of bacterial PI-PLC [phosphoinositide (PtdIns)-specific phospholipase C]. The NE assembly process is here dissected in relation to the requirement for endogenous phosphoinositide metabolism, employing recombinant eukaryotic PI-PLC, inhibitors and direct phospholipid analysis using ESI-MS (electrospray ionization mass spectrometry). PtdIns (phosphatidylinositol) species analysis by ESI-MS indicates that the chromatin-bound NE precursor vesicles are enriched for specific PtdIns species. Moreover, during GTP-induced precursor vesicle fusion. the membrane vesicles become ...
In rat parotid acinar cells prelabelled with [3H]inositol, substance P (100 nM) induced the formation of [3H]inositol 1,4,5-trisphosphate [Ins(1,4,5)P3]. Ins(1,4,5)P3 reached a maximum 7 s after substance P stimulation, and thereafter decreased and reached a stable value at 60 s. When the cells were exposed to substance P for 10, 30, 60, or 300 s, washed, and re-exposed to this peptide, the formation of [3H]inositol trisphosphate (InsP3) was attenuated in a time-dependent manner. In the cells pretreated as described above, the number of [3H]substance-P-binding sites (Bmax) was also decreased. Possible role(s) of Ca2+ and protein kinase (protein kinase C) control mechanisms in regulating substance P responses were investigated. Desensitization of substance P-induced InsP3 was not affected by the Ca2+ ionophore ionomycin, nor was it dependent on Ca2+ mobilization. On the other hand, in the presence of 4 beta-phorbol 12,13-dibutyrate (PDBu) and 12-O-tetradecanoyl-4 beta-phorbol 13-acetate, known ...
Phospholipase C gamma: A phosphoinositide phospholipase C subtype that is primarily regulated by PROTEIN-TYROSINE KINASES. It is structurally related to PHOSPHOLIPASE C DELTA with the addition of SRC HOMOLOGY DOMAINS and pleckstrin homology domains located between two halves of the CATALYTIC DOMAIN.
Phospholipase D (PLD) hydrolyzes the phosphodiester bond of the predominant membrane phospholipid, phosphatidylcholine producing phosphatidic acid and free choline. This activity can participate in signal transduction pathways and impact on vesicle trafficking for secretion and endocytosis, as well as receptor signalling. Phospholipids can regulate PLD activity directly, through specific intermolecular interactions, or indirectly, through their effect on the localization or activity of PLDs protein effectors. This short review highlights these various phospholipid inputs into the regulation of PLD activity and also reviews potential roles for PLD-generated phosphatidic acid, particularly a mechanism by which the phospholipid may participate in the process of vesicular trafficking.