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Regulation of mitochondrial fusion and apoptosis by the mitochondrial protein CTMP
Piao, Longzhen,Yang, Keum-Jin,Shin, Sanghee,Shin, Eulsoon,Li, Yuwen,Park, Kyung-Ah,Byun, Hee-Sun,Won, Min-Ho,Kim, Young-Rae,Lee, Hyunji,Hur, Gang-Min,Seok, Jeong-Ho,A. Hermmings, Brian,Park, Jongsun 충남대학교 형질전환복제돼지연구센터 2007 논문집 Vol. No.10
Piao, Longzhen,Shin, Sang-Hee,Yang, Keum-Jin,Park, Ji-Soo,Shin, Eul-Soon,Li, Yu-Wen,Park, Kyung-Ah,Byun, Hee-Sun,Won, Min-Ho,Lee, Choong-Jae,Hur, Gang-Min,Seok, Jeong-Ho,Kim, Ju-Duck Korean Society of ToxicologyKorea Environmental Mu 2006 Toxicological Research Vol.22 No.3
The survival and growth of epithelial cells depends on adhesion to the extracellular matrix. An adhesion signal may regulate the initiation of differentiation, since epidermal keratinocytes differentiate as they leave the basement membrane. A metabolically dead cornified cell envelope is the end point of epidermal differentiation so that this process may be viewed as a specialized form of programmed cell death. In order to investigate the precise cellular signaling events loading to terminal differentiation of keratinocytes, we have utilized HaCaT cells to monitor the biological consequences of $Ca^{2+}$ stimulation and numerous downstream signaling pathways, including activation of the extracellular signal-regulated protein kinase(ERK) pathway and activation of phosphatidylinositol 3-kinase(PI3K). The results presented in this study show that $Ca^{2+}$ function as potent agents for the differentiation of HaCaT keratinocytes, and this differentiation depends or the activation of ERK, Protein kinase B(PKB) and p70 ribosomal protein S6 kinase(p70S6K). Finally, the results show that the expression of Activator protein 1(AP-1; c-Jun and c-Fos) increased following $Ca^{2+}$-mediated differentiation of HaCaT cells, suggesting that ERK-mediated AP-1 expression is critical for initiating the terminal differentiation of keratinocytes.
PIAO, LONGZHEN,PARK, JISOO,LI, YUWEN,SHIN, SANGHEE,SHIN, SOYEON,KONG, GYEYEONG,SHRESTHA, ROBIN,TRAN, QUANGDON,HUR, GANG MIN,KIM, JEONG-LAN,PARK, JONGSUN UNKNOWN 2014 INTERNATIONAL JOURNAL OF MOLECULAR MEDICINE Vol.33 No.5
Antipsychotic drugs are regularly used for the treatment of many types of psychiatric disorders. The administration of second-generation antipsychotics is often associated with weight gain and the development of diabetes mellitus; however, the molecular mechanisms underlying the effects of these drugs remain poorly understood. Leptin and insulin play key roles in the regulation of energy balance and glucose homeostasis, and resistance to the actions of these hormones can occur with obesity and inflammation, resulting in the pathogenesis of obesity and type 2 diabetes. In this study, the effects of risperidone on the insulin-induced protein kinase B (PKB) phosphorylation and leptin-stimulated signal transducer and activator of transcription 3 (STAT3) phosphorylation were investigated in the human SH-SY5Y neuroblastoma cell line. The treatment of these cells with risperidone induced the activation of extracellular signal-related kinase (ERK) by cellular cyclic adenosine 3-monophosphate (cAMP)-dependent protein kinase (also known as protein kinase A; PKA) and the mechanisms involved include the induction of suppressor of cytokine signaling 3 (SOCS3) and suppressor of cytokine signaling 6 (SOCS6) expression. The risperidone-induced ERK activation induced an upregulation of SOCS3 and SOCS6 mRNA expression levels. Taken together, these results suggest that risperidone modulates SOCS3 and SOCS6 expression through adenylate cyclase-mediated ERK activation, which, in turn, leads to an inhibition of insulin-induced PKB phosphorylation and leptin-stimulated STAT3 phosphorylation. Eventually, these effects result in excessive body weight gain due to the inhibition of both the leptin and insulin signaling pathways.
Attenuation of Leptin and insulin Signaling by Risperidone via the SOCSs
Piao, Longzhen,Yang, Keum-Jin,Shin, Sanghee,Shin, Eulsoon,Li, Yuwen,Park, Kyung-Ah,Byun, Hee-Sun,Won, Min-Ho,Choi, Byung Lyul,Lee, Hyunji,Hur, Gang-Min,Seok, Jeong-Ho,Kim, Jeong-Lan,Park, Jongsun 충남대학교 형질전환복제돼지연구센터 2007 논문집 Vol. No.10
Longzhen Piao,Sanghee Shin,Keum-Jin Yang,Jisoo Park,Eulsoon Shin,Yuwen Li,Kyung Ah Park,Hee Sun Byun,Minho Won,Choong Jae Lee,Gang Min Hur,Jeong Ho Seok,Ju-Duck Kim,Chang Deok Kim,Jeung-Hoon Lee,Jongs 한국독성학회 2006 Toxicological Research Vol.22 No.3
The survival and growth of epithelial cells depends on adhesion to the extracellular matrix. An adhesion signal may regulate the initiation of differentiation, since epidermal keratinocytes differentiate as they leave the basement membrane. A metabolically dead cornified cell envelope is the end point of epidermal differentiation so that this process may be viewed as a specialized form of programmed cell death. In order to investigate the precise cellular signaling events leading to terminal differentiation of keratinocytes, we have utilized HaCaT cells to monitor the biological consequences of Ca²? stimulation and numerous downstream signaling pathways, including activation of the extracellular signal-regulated protein kinase (ERK) pathway and activation of phosphatidylinositol 3-kinase (PI3K). The results presented in this study show that Ca²? function as potent agents for the differentiation of HaCaT keratinocytes, and this differentiation depends on the activation of ERK, Protein kinase B (PKB) and p70 ribosomal protein S6 kinase (p70S6K). Finally, the results show that the expression of Activator protein 1 (AP-1; c-Jun and c-Fos) increased following Ca²?-mediated differentiation of HaCaT cells, suggesting that ERK-mediated AP-1 expression is critical for initiating the terminal differentiation of keratinocytes.
Piao, Longzhen,Shin, Sang-Hee,Yang, Keum-Jin,Park, Ji-Soo,Shin, Eul-Soon,Li, Yuwen,Park, Kyung-Ah,Byun, Hee-Sun,Won, Min-Ho,Lee, Choong-Jae,Hur, Gang-Min,Seok, Jeong-Ho,Kim, Ju-Duck,Kim, Chang-Deok,Le 충남대학교 암연구소 2007 암연구소 업적집 Vol.6 No.-
The survival and growth of epithelial cells depends on adhesion to the extracellular matrix. An adhesion signal may regulate the initiation of differentiation, since epidermal kerati-nocytes differentiate as they leave the basement membrane. A metabolically dead comified cell envelope is the end point of epidermal differentiation so that this process may be viewed as a specialized form of programmed cell death. In order to investigate the precise cellular signaling events leading to terminal differentiation of keratinocytes, we have utilized HaCaT cells to monitor the biological consequences of Ca^(2+) stimulation and numerous downstream signaling pathways, including activation of the extracellular signal-regulated protein kinase (ERK) pathway and activation of phosphatidylinositol 3-kinase (PI3K). The results presented in this study show that Ca^(2+) function as potent agents for the differentiation of HaCaT keratinocytes, and this differentiation depends on the activation of ERK, Protein kinase B (PKB) and p70 ribosomal protein S6 kinase (p70S6K). Finally, the results show that the expression of Activator protein 1 (AP-1; c-Jun and c-Fos) increased following Ca^(2+)-mediated differentiation of HaCaT cells, suggesting that ERK-mediated AP-1 expression is critical for initiating the terminal, differentiation of keratinocytes.
Li, Yuwen,Piao, Longzhen,Yang, Keum-Jin,Shin, Sang-Hee,Shin, Eul-Soon,Park, Kyung-Ah,Byun, Hee-Sun,Won, Min-Ho,Choi, Byung-Lyul,Lee, Hyun-Ji,Kim, Young-Rae,Hong, Jang-Hee,Hur, Gang-Min,Kim, Jeong-Lan Korean Society of ToxicologyKorea Environmental Mu 2008 Toxicological Research Vol.25 No.4
DNA-dependent protein kinase(DNA-PK) is involved in joining DNA double-strand breaks induced by ionizing radiation or V(D)J recombination and is activated by DNA ends and composed of a DNA binding subunit, Ku, and a catalytic subunit, DNA-PKcs. It has been suggested that DNA-PK might be $2^{nd}$ upstream kinase for protein kinase B(PKB). In this report, we showed that Ser473 phosphorylation in the hydrophobic-motif of PKB is blocked in DNA-PK knockout mouse embryonic fibroblast cells(MEFs) following insulin stimulation, while there is no effect on Ser473 phosphorylation in DNA-PK wild type MEF cells. The observation is further confirmed in human glioblastoma cells expressing a mutant form of DNA-PK(M059J) and a wild-type of DNA-PK(M059K), indicating that DNA-PK is indeed important for PKB activation. Furthermore, the treatment of cells with doxorubicin, DNA-damage inducing agent, leads to PKB phosphorylation on Ser473 in control MEF cells while there is no response in DNA-PK knockout MEF cells. Together, these results proposed that DNA-PK has a potential role in insulin signaling as well as DNA-repair signaling pathway.
Yuwen Li,Longzhen Piao,Keum-Jin Yang,Sanghee Shin,Eulsoon Shin,Kyung Ah Park,Hee Sun Byun,Minho Won,Byung Lyul Choi,Hyunji Lee,Young-Rae Kim,Jang Hee Hong,Gang Min Hur,Jeong-Lan Kim,Jae Youl Cho,Jeong 한국독성학회 2008 Toxicological Research Vol.24 No.3
DNA-dependent protein kinase (DNA-PK) is involved in joining DNA double-strand breaks induced by ionizing radiation or V(D)J recombination and is activated by DNA ends and composed of a DNA binding subunit, Ku, and a catalytic subunit, DNA-PKcs. It has been suggested that DNA-PK might be 2nd upstream kinase for protein kinase B (PKB). In this report, we showed that Ser473 phosphorylation in the hydrophobic-motif of PKB is blocked in DNA-PK knockout mouse embryonic fibroblast cells (MEFs) following insulin stimulation, while there is no effect on Ser473 phosphorylation in DNA-PK wild type MEF cells. The observation is further confirmed in human glioblastoma cells expressing a mutant form of DNA-PK (M059J) and a wild-type of DNA-PK (M059K), indicating that DNA-PK is indeed important for PKB activation. Furthermore, the treatment of cells with doxorubicin, DNA-damage inducing agent, leads to PKB phosphorylation on Ser473 in control MEF cells while there is no response in DNA-PK knockout MEF cells. Together, these results proposed that DNA-PK has a potential role in insulin signaling as well as DNA-repair signaling pathway.