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Activation of Prn-p gene and stable transfection of Prn-p cDNA in leukemia MEL and neuroblastoma N2a cells increased production of PrP(C) but not prevented DNA fragmentation initiated by serum deprivation

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Activation of Prn-p gene and stable transfection of Prn-p cDNA in leukemia MEL and neuroblastoma N2a cells increased production of PrP(C) but not prevented DNA fragmentation initiated by serum deprivation. / Gougoumas, Dimitrios D; Vizirianakis, Ioannis S; Triviai, Ioanna N; Tsiftsoglou, Asterios S.

In: J CELL PHYSIOL, Vol. 211, No. 2, 05.2007, p. 551-9.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Gougoumas, DD, Vizirianakis, IS, Triviai, IN & Tsiftsoglou, AS 2007, 'Activation of Prn-p gene and stable transfection of Prn-p cDNA in leukemia MEL and neuroblastoma N2a cells increased production of PrP(C) but not prevented DNA fragmentation initiated by serum deprivation', J CELL PHYSIOL, vol. 211, no. 2, pp. 551-9. https://doi.org/10.1002/jcp.20969

APA

Gougoumas, D. D., Vizirianakis, I. S., Triviai, I. N., & Tsiftsoglou, A. S. (2007). Activation of Prn-p gene and stable transfection of Prn-p cDNA in leukemia MEL and neuroblastoma N2a cells increased production of PrP(C) but not prevented DNA fragmentation initiated by serum deprivation. J CELL PHYSIOL, 211(2), 551-9. https://doi.org/10.1002/jcp.20969

Vancouver

Gougoumas DD, Vizirianakis IS, Triviai IN, Tsiftsoglou AS. Activation of Prn-p gene and stable transfection of Prn-p cDNA in leukemia MEL and neuroblastoma N2a cells increased production of PrP(C) but not prevented DNA fragmentation initiated by serum deprivation. J CELL PHYSIOL. 2007 May;211(2):551-9. https://doi.org/10.1002/jcp.20969

Bibtex

@article{85d47878b1234e5384b46af5843c7365,
title = "Activation of Prn-p gene and stable transfection of Prn-p cDNA in leukemia MEL and neuroblastoma N2a cells increased production of PrP(C) but not prevented DNA fragmentation initiated by serum deprivation",
abstract = "Prion protein (PrP(C)) via its isoform PrP(SC) is involved in the pathogenesis of transmissible spongiform encephalopathies (TSEs). We observed that murine erythroleukemia (MEL) cells arrested in phase G(1) undergo transcriptional activation of Prn-p gene. Here, we explored the potential role of activation of Prn-p gene and cytosolic accumulation of PrP(C) in growth arrest, differentiation, and apoptotic DNA fragmentation by stably transfecting MEL and N2a cells with Prn-p cDNA. Stably transfected MEL cells (clones # 6, 12, 20, 38, and 42) were assessed for growth and differentiation, while clones N2a13 and N2a8 of N2a cells for growth and apoptosis by flow cytometry using Annexin V and propidium iodide (PI). Our results indicate that (a) Induction of terminal differentiation of stably transfected MEL cells led to growth arrest, activation of Prn-p gene, concomitant expression of transfected Prn-p cDNA, suppression of bax gene, cytosolic accumulation of PrP(C), and DNA fragmentation. The latter was also induced in non-differentiated MEL cells growing under serum-free conditions; (b) similarly, serum deprivation promoted growth arrest, apoptosis/necrosis associated with DNA fragmentation in parental N2a and N2a13 cells that produced relative high level of PrP(C) and not PrP(SC). These data indicate that activation of Prn-p gene and expression of transfected Prn-p cDNA in cells of both hematopoietic and neuronal origin occurred concomitantly, and led to cytosolic accumulation of PrP(C) and DNA damage induced by serum deprivation. PrP(C) production failed to protect DNA fragmentation induced by serum deprivation. The question how does PrP(C) contribute to growth arrest and DNA fragmentation is discussed.",
keywords = "Animals, Apoptosis, Cell Differentiation, Cell Line, Tumor, Cell Proliferation, Culture Media, Serum-Free, Cytosol, DNA Fragmentation, Dimethyl Sulfoxide, Flow Cytometry, Gene Expression Regulation, Neoplastic, Leukemia, Erythroblastic, Acute, Mice, Neuroblastoma, PrPC Proteins, Prion Proteins, Prions, RNA, Messenger, Time Factors, Transcriptional Activation, Transfection, Up-Regulation, bcl-2-Associated X Protein, Journal Article",
author = "Gougoumas, {Dimitrios D} and Vizirianakis, {Ioannis S} and Triviai, {Ioanna N} and Tsiftsoglou, {Asterios S}",
note = "(c) 2007 Wiley-Liss, Inc.",
year = "2007",
month = may,
doi = "10.1002/jcp.20969",
language = "English",
volume = "211",
pages = "551--9",
journal = "J CELL PHYSIOL",
issn = "0021-9541",
publisher = "Wiley-Liss Inc.",
number = "2",

}

RIS

TY - JOUR

T1 - Activation of Prn-p gene and stable transfection of Prn-p cDNA in leukemia MEL and neuroblastoma N2a cells increased production of PrP(C) but not prevented DNA fragmentation initiated by serum deprivation

AU - Gougoumas, Dimitrios D

AU - Vizirianakis, Ioannis S

AU - Triviai, Ioanna N

AU - Tsiftsoglou, Asterios S

N1 - (c) 2007 Wiley-Liss, Inc.

PY - 2007/5

Y1 - 2007/5

N2 - Prion protein (PrP(C)) via its isoform PrP(SC) is involved in the pathogenesis of transmissible spongiform encephalopathies (TSEs). We observed that murine erythroleukemia (MEL) cells arrested in phase G(1) undergo transcriptional activation of Prn-p gene. Here, we explored the potential role of activation of Prn-p gene and cytosolic accumulation of PrP(C) in growth arrest, differentiation, and apoptotic DNA fragmentation by stably transfecting MEL and N2a cells with Prn-p cDNA. Stably transfected MEL cells (clones # 6, 12, 20, 38, and 42) were assessed for growth and differentiation, while clones N2a13 and N2a8 of N2a cells for growth and apoptosis by flow cytometry using Annexin V and propidium iodide (PI). Our results indicate that (a) Induction of terminal differentiation of stably transfected MEL cells led to growth arrest, activation of Prn-p gene, concomitant expression of transfected Prn-p cDNA, suppression of bax gene, cytosolic accumulation of PrP(C), and DNA fragmentation. The latter was also induced in non-differentiated MEL cells growing under serum-free conditions; (b) similarly, serum deprivation promoted growth arrest, apoptosis/necrosis associated with DNA fragmentation in parental N2a and N2a13 cells that produced relative high level of PrP(C) and not PrP(SC). These data indicate that activation of Prn-p gene and expression of transfected Prn-p cDNA in cells of both hematopoietic and neuronal origin occurred concomitantly, and led to cytosolic accumulation of PrP(C) and DNA damage induced by serum deprivation. PrP(C) production failed to protect DNA fragmentation induced by serum deprivation. The question how does PrP(C) contribute to growth arrest and DNA fragmentation is discussed.

AB - Prion protein (PrP(C)) via its isoform PrP(SC) is involved in the pathogenesis of transmissible spongiform encephalopathies (TSEs). We observed that murine erythroleukemia (MEL) cells arrested in phase G(1) undergo transcriptional activation of Prn-p gene. Here, we explored the potential role of activation of Prn-p gene and cytosolic accumulation of PrP(C) in growth arrest, differentiation, and apoptotic DNA fragmentation by stably transfecting MEL and N2a cells with Prn-p cDNA. Stably transfected MEL cells (clones # 6, 12, 20, 38, and 42) were assessed for growth and differentiation, while clones N2a13 and N2a8 of N2a cells for growth and apoptosis by flow cytometry using Annexin V and propidium iodide (PI). Our results indicate that (a) Induction of terminal differentiation of stably transfected MEL cells led to growth arrest, activation of Prn-p gene, concomitant expression of transfected Prn-p cDNA, suppression of bax gene, cytosolic accumulation of PrP(C), and DNA fragmentation. The latter was also induced in non-differentiated MEL cells growing under serum-free conditions; (b) similarly, serum deprivation promoted growth arrest, apoptosis/necrosis associated with DNA fragmentation in parental N2a and N2a13 cells that produced relative high level of PrP(C) and not PrP(SC). These data indicate that activation of Prn-p gene and expression of transfected Prn-p cDNA in cells of both hematopoietic and neuronal origin occurred concomitantly, and led to cytosolic accumulation of PrP(C) and DNA damage induced by serum deprivation. PrP(C) production failed to protect DNA fragmentation induced by serum deprivation. The question how does PrP(C) contribute to growth arrest and DNA fragmentation is discussed.

KW - Animals

KW - Apoptosis

KW - Cell Differentiation

KW - Cell Line, Tumor

KW - Cell Proliferation

KW - Culture Media, Serum-Free

KW - Cytosol

KW - DNA Fragmentation

KW - Dimethyl Sulfoxide

KW - Flow Cytometry

KW - Gene Expression Regulation, Neoplastic

KW - Leukemia, Erythroblastic, Acute

KW - Mice

KW - Neuroblastoma

KW - PrPC Proteins

KW - Prion Proteins

KW - Prions

KW - RNA, Messenger

KW - Time Factors

KW - Transcriptional Activation

KW - Transfection

KW - Up-Regulation

KW - bcl-2-Associated X Protein

KW - Journal Article

U2 - 10.1002/jcp.20969

DO - 10.1002/jcp.20969

M3 - SCORING: Journal article

C2 - 17186498

VL - 211

SP - 551

EP - 559

JO - J CELL PHYSIOL

JF - J CELL PHYSIOL

SN - 0021-9541

IS - 2

ER -