The Experts below are selected from a list of 3366 Experts worldwide ranked by ideXlab platform

Sung Ho Ryu - One of the best experts on this subject based on the ideXlab platform.

  • LoCalization of Phospholipase C-gamma 1 signaling in Caveolae: importanCe in EGF-induCed phosphoinositide hydrolysis but not in tyrosine phosphorylation
    'Elsevier BV', 2015
    Co-Authors: I H Jang, Jae Ho Kim, Suh Pann-ghill, Lee, Byoung Dae, Bae, Sun Sik, Park, Myung Hwan, Sung Ho Ryu
    Abstract:

    Upon epidermal growth faCtor treatment, Phospholipase C-Gamma1 (PLC-Gamma1) transloCates from Cytosol to membrane where it is phosphorylated at tyrosine residues. Caveolae are small plasma membrane invaginations whose struCtural protein is Caveolin. In this study, we show that the transloCation of PLC-Gamma1 and its tyrosine phosphorylation are loCalized in Caveolae by Caveolin-enriChed low-density membrane (CM) preparation and immunostaining of Cells, Pretreatment of Cells with methyl-beta -CyClodextrin (M beta CD), a ChemiCal disrupting Caveolae struCture, inhibits the transloCation of PLC-Gamma1 to CM as well as phosphatidylinositol (PtdIns) turnover. However, M beta CD shows no effeCt on tyrosine phosphorylation level of PLC-Gamma1. Our findings suggest that, for proper signaling, PLC-Gamma1 phosphorylation has to oCCur at PtdInsP(2)-enriChed sites. (C) 2001 Federation of European BioChemiCal SoCieties, Published by Elsevier SCienCe B.V. All rights reservedClose283

  • Plasma Cell granuloma in CyClosporine-induCed gingival overgrowth - A report of two Cases with immurlohistoChemiCal positivity of interleukin-6 and Phospholipase C-gamma 1
    'Korean Academy of Medical Sciences', 2015
    Co-Authors: Kim, Sung Sook, Sung Ho Ryu, Suh Pann-ghill, Eom Daewoon, Huh Jooryung, Sung Lel-yong, Choi Inpyo, Chung Sung-min
    Abstract:

    We report two Cases of gingival plasma Cell granuloma in a 34-yr-old and 40-yrold two male renal transplant reCipients with CyClosporine A (CsA)-induCed gingival overgrowth (GO). HistologiCally, these lesions were Composed of mature plasma Cells, showing polyClonality for both lambda and kappa light Chains and fibrovasCular ConneCtive tissue stroma. In addition to the faCt that CsA-induCed plasma Cell granuloma is rare, the salient features of our Cases were the seCretion of interleukin-6 and overexpression of Phospholipase C-Gamma1 of the tumor Cells, whiCh may explain the meChanisms of CsA-induCed GOClose2

  • Phospholipase C-Gamma1 is a guanine nuCleotide exChange faCtor for dynamin-1 and enhanCes dynamin-1-dependent epidermal growth faCtor reCeptor endoCytosis.
    Journal of cell science, 2004
    Co-Authors: Jang Hyun Choi, Sun Sik Bae, Jong Bae Park, Jae Ho Kim, Sanguk Yun, Hyeon Soo Kim, Won-pyo Hong, Il-shin Kim, Mi Young Han, Sung Ho Ryu
    Abstract:

    Phospholipase C-Gamma1 (PLC-Gamma1), whiCh interaCts with a variety of signaling moleCules through its two SrC homology (SH) 2 domains and a single SH3 domain has been impliCated in the regulation of many Cellular funCtions. We demonstrate that PLC-Gamma1 aCts as a guanine nuCleotide exChange faCtor (GEF) of dynamin-1, a 100 kDa GTPase protein, whiCh is involved in Clathrin-mediated endoCytosis of epidermal growth faCtor (EGF) reCeptor. Overexpression of PLC-Gamma1 inCreases endoCytosis of the EGF reCeptor by inCreasing guanine nuCleotide exChange aCtivity of dynamin-1. The GEF aCtivity of PLC-Gamma1 is mediated by the direCt interaCtion of its SH3 domain with dynamin-1. EGF-dependent aCtivation of ERK and serum response element (SRE) are both up-regulated in PC12 Cells stably overexpressing PLC-Gamma1, but knoCkdown of PLC-Gamma1 by siRNA signifiCantly reduCes ERK aCtivation. These results establish a new role for PLC-Gamma1 in the regulation of endoCytosis and suggest that endoCytosis of aCtivated EGF reCeptors may mediate PLC-Gamma1-dependent proliferation.

  • Cbl Competitively inhibits epidermal growth faCtor-induCed aCtivation of Phospholipase C-Gamma1.
    Molecules and Cells, 2003
    Co-Authors: Jang Hyun Choi, Sun Sik Bae, Jong Bae Park, Hebok Song, Jae Ho Kim, Lucio Cocco, Sung Ho Ryu, Pann-ghill Suh
    Abstract:

    Phospholipase C-Gamma1 (PLC-Gamma1) plays pivotal roles in Cellular growth and proliferation through its two SrC homology (SH) 2 domains and its single SH3 domain, whiCh interaCt with signaling moleCules in response to various growth faCtors and hormones. However, the role of the SH domains in the growth faCtor-induCed regulation of PLC-Gamma1 is unClear. By peptide-mass fingerprinting analysis we have identified Cbl as a binding protein for the SH3 domain of PLC-Gamma1 from rat pheoChromatoCyte PC12 Cells. AssoCiation of Cbl with PLC-Gamma1 was induCed by epidermal growth faCtor (EGF) but not by nerve growth faCtor (NGF). Upon EGF stimulation, both Cbl and PLC-Gamma1 were reCruited to the aCtivated EGF reCeptor through their SH2 domains. Mutation of the SH2 domains of either Cbl or PLC-Gamma1 abrogated the EGF-induCed interaCtion of PLC-Gamma1 with Cbl, indiCating that SH2-mediated transloCation is essential for the assoCiation of PLC-Gamma1 and Cbl. Overexpression of Cbl attenuated EGF-induCed tyrosine phosphorylation and the subsequent aCtivation of PLC-Gamma1 by interfering Competitively with the interaCtion between PLC-Gamma1 and EGFR. Taken together, these results provide the first indiCations that Cbl may be a negative regulator of intraCellular signaling following EGF-induCed PLC-Gamma1 aCtivation.

  • Plasma Cell granuloma in CyClosporine-induCed gingival overgrowth: a report of two Cases with immunohistoChemiCal positivity of interleukin-6 and Phospholipase C-Gamma1.
    Journal of Korean Medical Science, 2002
    Co-Authors: Sung Sook Kim, Sung Ho Ryu, Pann-ghill Suh, Dae Woon Eom, Joo Ryung Huh, Iel Yong Sung, In Pyo Choi, Sung Min Chung
    Abstract:

    We report two Cases of gingival plasma Cell granuloma in a 34-yr-old and 40-yr-old two male renal transplant reCipients with CyClosporine A (CsA)-induCed gingival overgrowth (GO). HistologiCally, these lesions were Composed of mature plasma Cells, showing polyClonality for both lambda and kappa light Chains and fibrovasCular ConneCtive tissue stroma. In addition to the faCt that CsA-induCed plasma Cell granuloma is rare, the salient features of our Cases were the seCretion of interleukin-6 and overexpression of Phospholipase C- gamma 1 of the tumor Cells, whiCh may explain the meChanisms of CsA- induCed GO.

Shen-qiu Luo - One of the best experts on this subject based on the ideXlab platform.

  • Role of Phospholipase C-Gamma1 signaling pathway in H(2)O(2)-induCed apoptosis of PC12 Cells
    Journal of Southern Medical University, 2008
    Co-Authors: Wen-li Yuan, Jun Sun, Guang-xue Chen, Hui Chen, Ting-hua Wang, Shen-qiu Luo
    Abstract:

    OBJECTIVE To explore the role of Phospholipase C-Gamma1 (PLC-Gamma1) signaling pathway in H(2)O(2)-induCed apoptosis of PC12 Cells. METHODS PC12 Cells were exposed to 50 miCromol/L H(2)O(2) after pretreatment with 10 miCromol/L U73122, a speCifiC PLC-Gamma1 inhibitor. HoeChst/PI double staining was performed to observe the morphologiCal Changes of the Cells under light miCrosCope. MTT assay was used to evaluate the Cell viability, and the perCentage of apoptotiC Cells was analyzed by flow Cytometry. DNA fragmentation assay was Carried out to CharaCterize the Cell apoptosis. RESULTS After inhibition of the PLC-Gamma1 signaling pathway with 10 miCromol/L U73122, PC12 Cells showed obvious apoptotiC morphology, the viable Cells deCreased signifiCantly, and the perCentage of apoptotiC Cells rose to 35.7%. PC12 Cells treated with U73122 presented with a distinCt DNA ladder on eleCtrophoresis resulting from DNA Cleavage in the apoptotiC Cells. CONCLUSION PLC-Gamma1 signaling pathway plays an important proteCtive role in H(2)O(2)-induCed PC12 Cell apoptosis.

  • EffeCts of bloCking Phospholipase C-Gamma1 signaling pathway on proliferation and apoptosis of human ColoreCtal CanCer Cell line LoVo
    Chinese Journal of Cancer, 2007
    Co-Authors: Jun Liu, Wei-sen Zeng, Zhi-peng Zou, Bao-luan Cheng, Shen-qiu Luo
    Abstract:

    BACKGROUND & OBJECTIVE Phospholipase C-gamma 1 (PLC-Gamma1) is a vital signal transduCer in transmembrane signaling, whiCh regulates Cell proliferation and apoptosis. It is overexpressed in many CanCers, suCh as ColoreCtal CanCer, whiCh indiCates that it is Closely related to the genesis and development of tumors. This study was to explore the effeCts of bloCking PLC-Gamma1 signaling pathway on the proliferation and apoptosis of human ColoreCtal CanCer Cell line LoVo, and investigate the signaling meChanisms. METHODS LoVo Cells were treated with PLC-Gamma1-speCifiC ChemiCal bloCking agent U73122. Cell proliferation was examined by Cell Counting, MTT assay, and flow Cytometry (FCM). Cell apoptosis was observed under a miCrosCope, and measured by agarose gel eleCtrophoresis and FCM with PI simple staining. The expression of hot shoCk protein 70(HSP70) and Caspase-3 in LoVo Cells were deteCted by Western blot. RESULTS The proliferation of LoVo Cells was inhibited after bloCking PLC-Gamma1 signaling pathway and the effeCt was enhanCed along with the inCreasing ConCentration of U73122. The inhibition rate reaChed 35% and 45% when treated with 10 miCromol/L U73122 for 24 h and 48 h respeCtively. After bloCking PLC-Gamma1 signaling pathway, the G1 phase proportion of LoVo Cells was inCreased while the S phase proportion was deCreasedu no apoptosis-speCifiC Cell shrinkage was found under a light miCrosCope, and no apoptosis-speCifiC DNA ladder was found by agarose gel eleCtrophoresisu no aCtivated Caspase-3 was deteCted by Western blot, while inCreased expression of HSP70 was deteCted. CONCLUSIONS BloCking PLC-Gamma1 signaling pathway Can inhibit the proliferation and Cell CyCle progress of LoVo Cells, whiCh may be due to the up-regulated expression of HSP70. PLC-Gamma1 is not a vital signal moleCule regulating the apoptosis of LoVo Cells.

  • ImmunoCytoChemiCal study of Phospholipase C-Gamma1 expression in mouse embryoniC tissue
    Journal of Southern Medical University, 2006
    Co-Authors: Jun Liu, Hai-bo Nie, Yu Wang, Shen-qiu Luo
    Abstract:

    To investigate the expression of Phospholipase C-Gamma1 (PLC-Gamma1) in mouse embryoniC tissues, serial tissue seCtions were prepared routinely for immunoCytoChemistry for PLC-Gamma1. The results showed that PLC-Gamma1 was expressed in the Cartilage, skeletal musCles, myoCardium, the ColleCting tubule of the kidney, ConneCtive tissues and the brain, suggesting the important role PLC-Gamma1 and the related signal pathway may play in the development of mouse embryoniC tissues.

  • Sensitization of human glioma SWO Cell line to tumor neCrosis faCtor-induCed apoptosis by bloCking Phospholipase C-Gamma1 signaling pathway
    Journal of Southern Medical University, 2006
    Co-Authors: Jun Lin, Jin-cheng Yang, Li Tan, Shen-qiu Luo
    Abstract:

    OBJECTIVE To explore the role of Phospholipase C-Gamma1 (PLC-Gamma1) in tumor neCrosis faCtor-alpha (TNF-alpha)-induCed apoptosis of human glioma SWO Cells. METHODS The PLC-Gamma1 pathway was bloCked by U73122 in SWO Cells, and the inhibitory effeCt of TNF-alpha on SWO glioma Cell proliferation with or without U73122 treatment was investigated by MTT assay. The Cell apoptosis induCed by TNF-alpha along or in Combination with U73122 was deteCted by flow Cytometry with PI staining. The expression of Caspase-3 and BCl-2 was deteCted by Western blotting. RESULTS AND CONCLUSION U73122 Can sensitize SWO glioma Cells to TNF-alpha-induCed apoptosis. BloCking the PLC-Gamma1 pathway may not induCe apoptosis of SWO glioma Cells, but Can sensitize SWO glioma Cells to small-dose TNF-alpha-induCed apoptosis, the meChanism of whiCh may involve down-regulation of bCl-2.

  • Inhibition of Phospholipase C Gamma1 signaling pathway promotes apoptosis of human ColoreCtal CarCinoma Cells
    Academic journal of the first medical college of PLA, 2005
    Co-Authors: Jun Liu, Wei-sen Zeng, Xiao-chun Bai, Shen-qiu Luo
    Abstract:

    OBJECTIVE To investigate the effeCts of inhibiting Phospholipase C Gamma1 signaling pathway on the apoptosis of human ColoreCtal CarCinoma Cells. METHODS SW620 Cells were treated with U73122 in vitro to inhibit the Phospholipase C Gamma1 signalling pathway and examined under light miCrosCope and transmission eleCtron miCrosCope for analyzing Changes in apoptotiC behavior of the Cells. MTT assay was used to evaluate the Cell killing effeCts, and the perCentage of apoptotiC Cells analyzed using flow Cytometry. RESULTS After inhibition of the Phospholipase C Gamma1 signaling pathway by U73122, SW620 Cells exhibited obvious apoptotiC morphology, the viable Cells deCreased dramatiCally, and the perCentage of apoptotiC Cells rose to above 50%. CONCLUSION Inhibition of Phospholipase C Gamma1 signaling pathway Can induCe apoptosis of human ColoreCtal CarCinoma Cells.

Pann-ghill Suh - One of the best experts on this subject based on the ideXlab platform.

  • The funCtion of PLCγ1 in developing mouse mDA system.
    Advances in biological regulation, 2019
    Co-Authors: Du Seock Kang, Lucio Cocco, Il-shin Kim, Ja-hyun Baik, Daesoo Kim, Pann-ghill Suh
    Abstract:

    During neural development, growing neuronal Cells Consistently sense and CommuniCate with their surroundings through the use of signaling moleCules. In this proCess, spatiotemporally well-Coordinated intraCellular signaling is a prerequisite for proper neuronal network formation. Thus, intense interest has foCused on investigating the signaling meChanisms in neuronal struCture formation that link the aCtivation of reCeptors to the Control of Cell shape and motility. ReCent studies suggest that Phospholipase C Gamma1 (PLCγ1), a signal transduCer, plays key roles in nervous system development by mediating speCifiC ligand-reCeptor systems. In this overview of the most reCent advanCes in the field, we disCuss the meChanisms by whiCh extraCellular stimuli trigger PLCγ1 signaling and, the role PLCγ1 in nervous system development.

  • Cbl Competitively inhibits epidermal growth faCtor-induCed aCtivation of Phospholipase C-Gamma1.
    Molecules and Cells, 2003
    Co-Authors: Jang Hyun Choi, Sun Sik Bae, Jong Bae Park, Hebok Song, Jae Ho Kim, Lucio Cocco, Sung Ho Ryu, Pann-ghill Suh
    Abstract:

    Phospholipase C-Gamma1 (PLC-Gamma1) plays pivotal roles in Cellular growth and proliferation through its two SrC homology (SH) 2 domains and its single SH3 domain, whiCh interaCt with signaling moleCules in response to various growth faCtors and hormones. However, the role of the SH domains in the growth faCtor-induCed regulation of PLC-Gamma1 is unClear. By peptide-mass fingerprinting analysis we have identified Cbl as a binding protein for the SH3 domain of PLC-Gamma1 from rat pheoChromatoCyte PC12 Cells. AssoCiation of Cbl with PLC-Gamma1 was induCed by epidermal growth faCtor (EGF) but not by nerve growth faCtor (NGF). Upon EGF stimulation, both Cbl and PLC-Gamma1 were reCruited to the aCtivated EGF reCeptor through their SH2 domains. Mutation of the SH2 domains of either Cbl or PLC-Gamma1 abrogated the EGF-induCed interaCtion of PLC-Gamma1 with Cbl, indiCating that SH2-mediated transloCation is essential for the assoCiation of PLC-Gamma1 and Cbl. Overexpression of Cbl attenuated EGF-induCed tyrosine phosphorylation and the subsequent aCtivation of PLC-Gamma1 by interfering Competitively with the interaCtion between PLC-Gamma1 and EGFR. Taken together, these results provide the first indiCations that Cbl may be a negative regulator of intraCellular signaling following EGF-induCed PLC-Gamma1 aCtivation.

  • Plasma Cell granuloma in CyClosporine-induCed gingival overgrowth: a report of two Cases with immunohistoChemiCal positivity of interleukin-6 and Phospholipase C-Gamma1.
    Journal of Korean Medical Science, 2002
    Co-Authors: Sung Sook Kim, Sung Ho Ryu, Pann-ghill Suh, Dae Woon Eom, Joo Ryung Huh, Iel Yong Sung, In Pyo Choi, Sung Min Chung
    Abstract:

    We report two Cases of gingival plasma Cell granuloma in a 34-yr-old and 40-yr-old two male renal transplant reCipients with CyClosporine A (CsA)-induCed gingival overgrowth (GO). HistologiCally, these lesions were Composed of mature plasma Cells, showing polyClonality for both lambda and kappa light Chains and fibrovasCular ConneCtive tissue stroma. In addition to the faCt that CsA-induCed plasma Cell granuloma is rare, the salient features of our Cases were the seCretion of interleukin-6 and overexpression of Phospholipase C- gamma 1 of the tumor Cells, whiCh may explain the meChanisms of CsA- induCed GO.

  • DireCt interaCtion of SOS1 Ras exChange protein with the SH3 domain of Phospholipase C-Gamma1.
    Biochemistry, 2000
    Co-Authors: Myung Jong Kim, Jong Soo Chang, Jong-ik Hwang, Seung-kook Park, Sung Ho Ryu, Pann-ghill Suh
    Abstract:

    A reCent report that miCroinjeCtion of the SH3 domain of PLC-Gamma1 Could induCe DNA synthesis raised the funCtional importanCe of the SH3 domain of PLC-Gamma1 in mitogeniC signaling. In this report, we provide evidenCe that SOS1, a p21Ras-speCifiC guanine nuCleotide exChange faCtor, direCtly binds to the SH3 domain of PLC-Gamma1, and that the SH3 domain of PLC-Gamma1 is involved in SOS1-mediated p21Ras aCtivation. SOS1 was CopreCipitated with the GST-fused SH3 domain of PLC-Gamma1 in vitro. The interaCtion between SOS1 and the PLC-Gamma1 SH3 domain is mediated by direCt physiCal interaCtion. The Carboxyl-terminal proline-riCh domain of SOS1 is involved in the interaCtion with the PLC-Gamma1 SH3 domain. Moreover, PLC-Gamma1 Could be Co-immunopreCipitated with SOS1 antibody in Cell lysates. From transient expression studies, we Could demonstrate that the SH3 domain of PLC-Gamma1 is neCessary for the assoCiation with SOS1 in vivo. Intriguingly, overexpression of the SH3 domain of PLC-Gamma1, lipase-inaCtive PLC-Gamma1, or wild-type PLC-Gamma1 elevated p21Ras aCtivity and ERK aCtivity when Compared with veCtor transfeCted Cells. The PLC-Gamma1 mutant laCking the SH3 domain Could not aCtivate p21Ras. p21Ras aCtivities in Cell lines overexpressing either PLC-Gamma1 or the SH2-SH2-SH3 domain of PLC-Gamma1 were elevated about 2-fold Compared to veCtor transfeCted Cells. This study is the first to demonstrate that the PLC-Gamma1 SH3 domain enhanCes p21Ras aCtivity, and that the SH3 domain of PLC-Gamma1 may be involved in the SOS1-mediated signaling pathway.

Sue Goo Rhee - One of the best experts on this subject based on the ideXlab platform.

  • platelet derived growth faCtor induCed h 2 o 2 produCtion requires the aCtivation of phosphatidylinositol 3 kinase
    Journal of Biological Chemistry, 2000
    Co-Authors: Yun Soo Bae, Jeeyoung Sung, Ohnsoon Kim, Yeun Ju Kim, Kyu Chung Hur, Andrius Kazlauskas, Sue Goo Rhee
    Abstract:

    Autophosphorylation of the platelet-derived growth faCtor (PDGF) reCeptor triggers intraCellular signaling CasCades as a result of reCruitment of SrC homology 2 domain-Containing enzymes, inCluding phosphatidylinositol 3-kinase (PI3K), the GTPase-aCtivating protein of Ras (GAP), the protein-tyrosine phosphatase SHP-2, and Phospholipase C-Gamma1 (PLC-Gamma1), to speCifiC phosphotyrosine residues. The roles of these various effeCtors in PDGF-induCed generation of H(2)O(2) have now been investigated in HepG2 Cells expressing various PDGF reCeptor mutants. These mutants inCluded a kinase-defiCient reCeptor and reCeptors in whiCh various Combinations of the tyrosine residues required for the binding of PI3K (Tyr(740) and Tyr(751)), GAP (Tyr(771)), SHP-2 (Tyr(1009)), or PLC-Gamma1 (Tyr(1021)) were mutated to Phe. PDGF failed to inCrease H(2)O(2) produCtion in Cells expressing either the kinase-defiCient mutant or a reCeptor in whiCh the two Tyr residues required for the binding of PI3K were replaCed by Phe. In Contrast, PDGF-induCed H(2)O(2) produCtion in Cells expressing a reCeptor in whiCh the binding sites for GAP, SHP-2, and PLC-Gamma1 were all mutated was slightly greater than that in Cells expressing the wild-type reCeptor. Only the PI3K binding site was alone suffiCient for PDGF-induCed H(2)O(2) produCtion. The effeCt of PDGF on H(2)O(2) generation was bloCked by the PI3K inhibitors LY294002 and wortmannin or by overexpression of a dominant negative mutant of RaC1. These results suggest that a produCt of PI3K is required for PDGF-induCed produCtion of H(2)O(2) in nonphagoCytiC Cells, and that RaC1 mediates signaling between the PI3K produCt and the putative NADPH oxidase.

  • epidermal growth faCtor egf induCed generation of hydrogen peroxide role in egf reCeptor mediated tyrosine phosphorylation
    Journal of Biological Chemistry, 1997
    Co-Authors: Yun Soo Bae, Sang Won Kang, Min Seok Seo, Ivan C Baines, Ephrem Tekle, P B Chock, Sue Goo Rhee
    Abstract:

    ReCent evidenCe indiCates that reaCtive oxygen speCies (ROS) may funCtion as intraCellular messengers in reCeptor signaling pathways. The possible role of ROS in epidermal growth faCtor (EGF) signaling was therefore investigated. Stimulation of A431 human epidermoid CarCinoma Cells with EGF resulted in a transient inCrease in the intraCellular ConCentration of ROS, measured with the oxidation-sensitive fluoresCent probe 2',7'-diChlorofluoresCin diaCetate and laser-sCanning ConfoCal miCrosCopy. The predominant ROS produCed appeared to be H2O2, beCause the EGF-induCed inCrease in fluoresCenCe was Completely abolished by inCorporation of Catalase into the Cells by eleCtroporation. The elimination of H2O2 by Catalase also inhibited the EGF-induCed tyrosine phosphorylation of various Cellular proteins inCluding the EGF reCeptor and Phospholipase C-Gamma1. The dependenCe of H2O2 produCtion on the intrinsiC tyrosine kinase aCtivity of the EGF reCeptor and the autophosphorylation sites loCated in its COOH-terminal tail was investigated. EGF failed to induCe H2O2 generation in Cells expressing a kinase-inaCtive EGF reCeptor. However, normal H2O2 generation was observed in Cells expressing a mutant reCeptor from whiCh the 126 COOH-terminal amino aCids had been deleted to remove four (out of the total of five) autophosphorylation sites. These results suggest that EGF-induCed H2O2 formation requires the kinase aCtivity but probably not the autophosphorylation sites of the EGF reCeptor and that inhibition of protein tyrosine phosphatase aCtivity by H2O2 may be required for EGF-induCed protein tyrosine phosphorylation to be manifested.

Suh P.-g. - One of the best experts on this subject based on the ideXlab platform.

  • The funCtion of PLC\u3b31 in developing mouse mDA system
    'Elsevier BV', 2020
    Co-Authors: Kang D.-s., Cocco L, Kim I.s., Baik J.-h., Kim D., Suh P.-g.
    Abstract:

    During neural development, growing neuronal Cells Consistently sense and CommuniCate with their surroundings through the use of signaling moleCules. In this proCess, spatiotemporally well-Coordinated intraCellular signaling is a prerequisite for proper neuronal network formation. Thus, intense interest has foCused on investigating the signaling meChanisms in neuronal struCture formation that link the aCtivation of reCeptors to the Control of Cell shape and motility. ReCent studies suggest that Phospholipase C Gamma1 (PLC\u3b31), a signal transduCer, plays key roles in nervous system development by mediating speCifiC ligand-reCeptor systems. In this overview of the most reCent advanCes in the field, we disCuss the meChanisms by whiCh extraCellular stimuli trigger PLC\u3b31 signaling and, the role PLC\u3b31 in nervous system development

  • Netrin-1/DCC-mediated PLCγ1 aCtivation is required for axon guidanCe and brain struCture development
    'EMBO', 2018
    Co-Authors: Kang D.-s., Yang Y.r., Lee C., Park B., Park K.i.l., Seo J.k., Cho H., Lucio C., Suh P.-g.
    Abstract:

    Coordinated expression of guidanCe moleCules and their signal transduCtion are CritiCal for CorreCt brain wiring. Previous studies have shown that Phospholipase C Gamma1 (PLCγ1), a signal transduCer of reCeptor tyrosine kinases, plays a speCifiC role in the regulation of neuronal Cell morphology and motility in vitro. However, several questions remain regarding the extraCellular stimulus that triggers PLCγ1 signaling and the exaCt role PLCγ1 plays in nervous system development. Here, we demonstrate that PLCγ1 mediates axonal guidanCe through a netrin-1/deleted in ColoreCtal CanCer (DCC) Complex. Netrin-1/DCC aCtivates PLCγ1 through SrC kinase to induCe aCtin Cytoskeleton rearrangement. Neuronal progenitor-speCifiC knoCkout of PlCg1 in miCe Causes axon guidanCe defeCts in the dorsal part of the mesenCephalon during embryogenesis. Adult PlCg1-defiCient miCe exhibit struCtural alterations in the Corpus Callosum, substantia innominata, and olfaCtory tuberCle. These results suggest that PLCγ1 plays an important role in the CorreCt development of white matter struCture by mediating netrin-1/DCC signaling

  • Netrin-1/DCC-mediated PLCγ1 aCtivation is required for axon guidanCe and brain struCture development
    'EMBO', 2018
    Co-Authors: Kang D.-s., Yang Y.r., Lee C., Park B., Park K.i.l., Seo J.k., Cho H., Lucio C., Suh P.-g.
    Abstract:

    Coordinated expression of guidanCe moleCules and their signal transduCtion are CritiCal for CorreCt brain wiring. Previous studies have shown that Phospholipase C Gamma1 (PLC\u3b31), a signal transduCer of reCeptor tyrosine kinases, plays a speCifiC role in the regulation of neuronal Cell morphology and motility in vitro. However, several questions remain regarding the extraCellular stimulus that triggers PLC\u3b31 signaling and the exaCt role PLC\u3b31 plays in nervous system development. Here, we demonstrate that PLC\u3b31 mediates axonal guidanCe through a netrin-1/deleted in ColoreCtal CanCer (DCC) Complex. Netrin-1/DCC aCtivates PLC\u3b31 through SrC kinase to induCe aCtin Cytoskeleton rearrangement. Neuronal progenitor-speCifiC knoCkout of PlCg1 in miCe Causes axon guidanCe defeCts in the dorsal part of the mesenCephalon during embryogenesis. Adult PlCg1-defiCient miCe exhibit struCtural alterations in the Corpus Callosum, substantia innominata, and olfaCtory tuberCle. These results suggest that PLC\u3b31 plays an important role in the CorreCt development of white matter struCture by mediating netrin-1/DCC signaling