Overexpression of phospholipase C-γ1 suppresses UVC-induced apoptosis through inhibition of c-fos accumulation and c-Jun N-terminal kinase activation in PC12 cells

Young Han Lee; Seong Yong Kim; Jae Ryong Kim; Ki Young Kim; Myung Jong Kim; Sung Ho Ryu; Pann Ghill Suh; Jung Hye Kim

doi:10.1016/S1388-1981(99)00128-6

Overexpression of phospholipase C-γ1 suppresses UVC-induced apoptosis through inhibition of c-fos accumulation and c-Jun N-terminal kinase activation in PC12 cells

Young Han Lee, Seong Yong Kim, Jae Ryong Kim, Ki Young Kim, Myung Jong Kim, Sung Ho Ryu, Pann Ghill Suh, Jung Hye Kim

Neurology

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

Ultraviolet-C (UVC) irradiation induces DNA damage and UVC-irradiated cells undergo cell growth arrest to repair the damaged DNA or the induction of apoptosis to prevent the risk of neoplastic transformation. Phospholipase C-γ1 (PLC-γ1) is a mediator of growth factor induced-signal cascade, catalyzing the hydrolysis of phosphatidyl 4,5-bisphosphate to generate second messengers, diacylglycerol and inositol 1,4,5-trisphosphate (IP₃). PLC-γ1 is activated by phosphorylation of tyrosine residues upon occupation of cell surface receptors by growth factors and plays an important role in controlling cellular proliferation and differentiation. In this study, we found that PLC-γ1 was tyrosine phosphorylated within 2.5 min after UVC irradiation. To investigate the role of UVC-induced tyrosine phosphorylation of PLC-γ1, we compared the effect of UVC between PLC-γ1 overexpressing cells and empty vector transfected cells. Overexpression of PLC-γ1 inhibited UVC-induced sub-diploid peak and DNA fragmentation. Northern blot analysis revealed that UVC-induced c-fos mRNA accumulation was inhibited in PLC-γ1 overexpressing cells, while c-jun expression was not affected. In addition, UVC-induced activation of c-Jun N-terminal kinase (JNK) was significantly suppressed in PLC-γ1 overexpressing cells. These results suggest that PLC-γ1 may associate with the protective function against the UVC-induced cell death progression via the inhibition of accumulation of c-fos mRNA and the inhibition of JNK kinase activity. Copyright (C) 1999 Elsevier Science B.V.

Original language	English (US)
Pages (from-to)	235-243
Number of pages	9
Journal	Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Volume	1440
Issue number	2-3
DOIs	https://doi.org/10.1016/S1388-1981(99)00128-6
State	Published - Sep 22 1999

Keywords

Apoptosis
Phospholipase C-γ1
Ultraviolet-C
c-Jun N-terminal kinase

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1016/S1388-1981(99)00128-6

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Lee, Y. H., Kim, S. Y., Kim, J. R., Young Kim, K., Kim, M. J., Ryu, S. H., Suh, P. G., & Kim, J. H. (1999). Overexpression of phospholipase C-γ1 suppresses UVC-induced apoptosis through inhibition of c-fos accumulation and c-Jun N-terminal kinase activation in PC12 cells. Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, 1440(2-3), 235-243. https://doi.org/10.1016/S1388-1981(99)00128-6

@article{374451cf42964107a4b51e7262546705,

title = "Overexpression of phospholipase C-γ1 suppresses UVC-induced apoptosis through inhibition of c-fos accumulation and c-Jun N-terminal kinase activation in PC12 cells",

abstract = "Ultraviolet-C (UVC) irradiation induces DNA damage and UVC-irradiated cells undergo cell growth arrest to repair the damaged DNA or the induction of apoptosis to prevent the risk of neoplastic transformation. Phospholipase C-γ1 (PLC-γ1) is a mediator of growth factor induced-signal cascade, catalyzing the hydrolysis of phosphatidyl 4,5-bisphosphate to generate second messengers, diacylglycerol and inositol 1,4,5-trisphosphate (IP3). PLC-γ1 is activated by phosphorylation of tyrosine residues upon occupation of cell surface receptors by growth factors and plays an important role in controlling cellular proliferation and differentiation. In this study, we found that PLC-γ1 was tyrosine phosphorylated within 2.5 min after UVC irradiation. To investigate the role of UVC-induced tyrosine phosphorylation of PLC-γ1, we compared the effect of UVC between PLC-γ1 overexpressing cells and empty vector transfected cells. Overexpression of PLC-γ1 inhibited UVC-induced sub-diploid peak and DNA fragmentation. Northern blot analysis revealed that UVC-induced c-fos mRNA accumulation was inhibited in PLC-γ1 overexpressing cells, while c-jun expression was not affected. In addition, UVC-induced activation of c-Jun N-terminal kinase (JNK) was significantly suppressed in PLC-γ1 overexpressing cells. These results suggest that PLC-γ1 may associate with the protective function against the UVC-induced cell death progression via the inhibition of accumulation of c-fos mRNA and the inhibition of JNK kinase activity. Copyright (C) 1999 Elsevier Science B.V.",

keywords = "Apoptosis, Phospholipase C-γ1, Ultraviolet-C, c-Jun N-terminal kinase",

author = "Lee, {Young Han} and Kim, {Seong Yong} and Kim, {Jae Ryong} and {Young Kim}, Ki and Kim, {Myung Jong} and Ryu, {Sung Ho} and Suh, {Pann Ghill} and Kim, {Jung Hye}",

note = "Funding Information: We thank Dr. Y.M. Park (Department of Biology, Inchon University, Korea) for hsp70 cDNA and Dr. J.K. Shin (Dana-Farber Cancer Institute, Harvard Medical School, USA) for c-fos, c-jun and GAPDH cDNAs, and Dr. S.G. Rhee (National Heart, Lung and Blood Institute, NIH, USA) for purified GST-c-Jun protein. The authors wish to acknowledge the financial support of the Korea Research Foundation from the program of 1997.",

year = "1999",

month = sep,

day = "22",

doi = "10.1016/S1388-1981(99)00128-6",

language = "English (US)",

volume = "1440",

pages = "235--243",

journal = "Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids",

issn = "1388-1981",

publisher = "Elsevier",

number = "2-3",

}

Lee, YH, Kim, SY, Kim, JR, Young Kim, K, Kim, MJ, Ryu, SH, Suh, PG & Kim, JH 1999, 'Overexpression of phospholipase C-γ1 suppresses UVC-induced apoptosis through inhibition of c-fos accumulation and c-Jun N-terminal kinase activation in PC12 cells', Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, vol. 1440, no. 2-3, pp. 235-243. https://doi.org/10.1016/S1388-1981(99)00128-6

Overexpression of phospholipase C-γ1 suppresses UVC-induced apoptosis through inhibition of c-fos accumulation and c-Jun N-terminal kinase activation in PC12 cells. / Lee, Young Han; Kim, Seong Yong; Kim, Jae Ryong et al.
In: Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, Vol. 1440, No. 2-3, 22.09.1999, p. 235-243.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Overexpression of phospholipase C-γ1 suppresses UVC-induced apoptosis through inhibition of c-fos accumulation and c-Jun N-terminal kinase activation in PC12 cells

AU - Lee, Young Han

AU - Kim, Seong Yong

AU - Kim, Jae Ryong

AU - Young Kim, Ki

AU - Kim, Myung Jong

AU - Ryu, Sung Ho

AU - Suh, Pann Ghill

AU - Kim, Jung Hye

N1 - Funding Information: We thank Dr. Y.M. Park (Department of Biology, Inchon University, Korea) for hsp70 cDNA and Dr. J.K. Shin (Dana-Farber Cancer Institute, Harvard Medical School, USA) for c-fos, c-jun and GAPDH cDNAs, and Dr. S.G. Rhee (National Heart, Lung and Blood Institute, NIH, USA) for purified GST-c-Jun protein. The authors wish to acknowledge the financial support of the Korea Research Foundation from the program of 1997.

PY - 1999/9/22

Y1 - 1999/9/22

N2 - Ultraviolet-C (UVC) irradiation induces DNA damage and UVC-irradiated cells undergo cell growth arrest to repair the damaged DNA or the induction of apoptosis to prevent the risk of neoplastic transformation. Phospholipase C-γ1 (PLC-γ1) is a mediator of growth factor induced-signal cascade, catalyzing the hydrolysis of phosphatidyl 4,5-bisphosphate to generate second messengers, diacylglycerol and inositol 1,4,5-trisphosphate (IP3). PLC-γ1 is activated by phosphorylation of tyrosine residues upon occupation of cell surface receptors by growth factors and plays an important role in controlling cellular proliferation and differentiation. In this study, we found that PLC-γ1 was tyrosine phosphorylated within 2.5 min after UVC irradiation. To investigate the role of UVC-induced tyrosine phosphorylation of PLC-γ1, we compared the effect of UVC between PLC-γ1 overexpressing cells and empty vector transfected cells. Overexpression of PLC-γ1 inhibited UVC-induced sub-diploid peak and DNA fragmentation. Northern blot analysis revealed that UVC-induced c-fos mRNA accumulation was inhibited in PLC-γ1 overexpressing cells, while c-jun expression was not affected. In addition, UVC-induced activation of c-Jun N-terminal kinase (JNK) was significantly suppressed in PLC-γ1 overexpressing cells. These results suggest that PLC-γ1 may associate with the protective function against the UVC-induced cell death progression via the inhibition of accumulation of c-fos mRNA and the inhibition of JNK kinase activity. Copyright (C) 1999 Elsevier Science B.V.

AB - Ultraviolet-C (UVC) irradiation induces DNA damage and UVC-irradiated cells undergo cell growth arrest to repair the damaged DNA or the induction of apoptosis to prevent the risk of neoplastic transformation. Phospholipase C-γ1 (PLC-γ1) is a mediator of growth factor induced-signal cascade, catalyzing the hydrolysis of phosphatidyl 4,5-bisphosphate to generate second messengers, diacylglycerol and inositol 1,4,5-trisphosphate (IP3). PLC-γ1 is activated by phosphorylation of tyrosine residues upon occupation of cell surface receptors by growth factors and plays an important role in controlling cellular proliferation and differentiation. In this study, we found that PLC-γ1 was tyrosine phosphorylated within 2.5 min after UVC irradiation. To investigate the role of UVC-induced tyrosine phosphorylation of PLC-γ1, we compared the effect of UVC between PLC-γ1 overexpressing cells and empty vector transfected cells. Overexpression of PLC-γ1 inhibited UVC-induced sub-diploid peak and DNA fragmentation. Northern blot analysis revealed that UVC-induced c-fos mRNA accumulation was inhibited in PLC-γ1 overexpressing cells, while c-jun expression was not affected. In addition, UVC-induced activation of c-Jun N-terminal kinase (JNK) was significantly suppressed in PLC-γ1 overexpressing cells. These results suggest that PLC-γ1 may associate with the protective function against the UVC-induced cell death progression via the inhibition of accumulation of c-fos mRNA and the inhibition of JNK kinase activity. Copyright (C) 1999 Elsevier Science B.V.

KW - Apoptosis

KW - Phospholipase C-γ1

KW - Ultraviolet-C

KW - c-Jun N-terminal kinase

UR - http://www.scopus.com/inward/record.url?scp=0032831817&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032831817&partnerID=8YFLogxK

U2 - 10.1016/S1388-1981(99)00128-6

DO - 10.1016/S1388-1981(99)00128-6

M3 - Article

C2 - 10521707

AN - SCOPUS:0032831817

SN - 1388-1981

VL - 1440

SP - 235

EP - 243

JO - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

JF - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids

IS - 2-3

ER -

Overexpression of phospholipase C-γ1 suppresses UVC-induced apoptosis through inhibition of c-fos accumulation and c-Jun N-terminal kinase activation in PC12 cells

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