Lack of induction of tissue transglutaminase but activation of the preexisting enzyme in c-Myc-induced apoptosis of CHO cells

Zoltán Balajthy, Noémi Kedei, Laszlo Nagy, Peter J.A. Davies, László Fésüs

Research output: Contribution to journalArticle

Abstract

The intracellular activity and expression of tissue transglutaminase, which crosslinks proteins through ε(γ-glutamyl)lysine isodipeptide bond, was investigated in CHO cells and those stably transfected with either inducible c-Myc (which leads to apoptosis) or with c-myc and the apoptosis inhibitor Bcl-2. Protein-bound cross-link content was significantly higher when apoptosis was induced by c-Myc while the concomitant presence of Bcl-2 markedly reduced both apoptosis and enzymatic protein cross-linking. The expression of tissue transglutaminase did not change following the initiation of apoptosis by c-Myc or when it was blocked by Bcl-2. Studying transiently co-transfected elements of the mouse tissue transglutaminase promoter linked to a reporter enzyme revealed their overall repression in cells expressing c-Myc. This repression was partially suspended in cells also carrying Bcl-2. Our data suggest that tissue transglutaminase is not induced when c-Myc initiates apoptosis but the pre-existing endogenous enzyme is activated.

Original languageEnglish (US)
Pages (from-to)280-284
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume236
Issue number2
DOIs
StatePublished - Jul 18 1997
Externally publishedYes

Fingerprint

Enzyme Activation
CHO Cells
Chemical activation
Apoptosis
Enzymes
Proteins
Lysine
transglutaminase 2
Cells

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Lack of induction of tissue transglutaminase but activation of the preexisting enzyme in c-Myc-induced apoptosis of CHO cells. / Balajthy, Zoltán; Kedei, Noémi; Nagy, Laszlo; Davies, Peter J.A.; Fésüs, László.

In: Biochemical and Biophysical Research Communications, Vol. 236, No. 2, 18.07.1997, p. 280-284.

Research output: Contribution to journalArticle

@article{74d28245bada4273ac282ed8d36e2bd2,
title = "Lack of induction of tissue transglutaminase but activation of the preexisting enzyme in c-Myc-induced apoptosis of CHO cells",
abstract = "The intracellular activity and expression of tissue transglutaminase, which crosslinks proteins through ε(γ-glutamyl)lysine isodipeptide bond, was investigated in CHO cells and those stably transfected with either inducible c-Myc (which leads to apoptosis) or with c-myc and the apoptosis inhibitor Bcl-2. Protein-bound cross-link content was significantly higher when apoptosis was induced by c-Myc while the concomitant presence of Bcl-2 markedly reduced both apoptosis and enzymatic protein cross-linking. The expression of tissue transglutaminase did not change following the initiation of apoptosis by c-Myc or when it was blocked by Bcl-2. Studying transiently co-transfected elements of the mouse tissue transglutaminase promoter linked to a reporter enzyme revealed their overall repression in cells expressing c-Myc. This repression was partially suspended in cells also carrying Bcl-2. Our data suggest that tissue transglutaminase is not induced when c-Myc initiates apoptosis but the pre-existing endogenous enzyme is activated.",
author = "Zolt{\'a}n Balajthy and No{\'e}mi Kedei and Laszlo Nagy and Davies, {Peter J.A.} and L{\'a}szl{\'o} F{\'e}s{\"u}s",
year = "1997",
month = "7",
day = "18",
doi = "10.1006/bbrc.1997.6969",
language = "English (US)",
volume = "236",
pages = "280--284",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Lack of induction of tissue transglutaminase but activation of the preexisting enzyme in c-Myc-induced apoptosis of CHO cells

AU - Balajthy, Zoltán

AU - Kedei, Noémi

AU - Nagy, Laszlo

AU - Davies, Peter J.A.

AU - Fésüs, László

PY - 1997/7/18

Y1 - 1997/7/18

N2 - The intracellular activity and expression of tissue transglutaminase, which crosslinks proteins through ε(γ-glutamyl)lysine isodipeptide bond, was investigated in CHO cells and those stably transfected with either inducible c-Myc (which leads to apoptosis) or with c-myc and the apoptosis inhibitor Bcl-2. Protein-bound cross-link content was significantly higher when apoptosis was induced by c-Myc while the concomitant presence of Bcl-2 markedly reduced both apoptosis and enzymatic protein cross-linking. The expression of tissue transglutaminase did not change following the initiation of apoptosis by c-Myc or when it was blocked by Bcl-2. Studying transiently co-transfected elements of the mouse tissue transglutaminase promoter linked to a reporter enzyme revealed their overall repression in cells expressing c-Myc. This repression was partially suspended in cells also carrying Bcl-2. Our data suggest that tissue transglutaminase is not induced when c-Myc initiates apoptosis but the pre-existing endogenous enzyme is activated.

AB - The intracellular activity and expression of tissue transglutaminase, which crosslinks proteins through ε(γ-glutamyl)lysine isodipeptide bond, was investigated in CHO cells and those stably transfected with either inducible c-Myc (which leads to apoptosis) or with c-myc and the apoptosis inhibitor Bcl-2. Protein-bound cross-link content was significantly higher when apoptosis was induced by c-Myc while the concomitant presence of Bcl-2 markedly reduced both apoptosis and enzymatic protein cross-linking. The expression of tissue transglutaminase did not change following the initiation of apoptosis by c-Myc or when it was blocked by Bcl-2. Studying transiently co-transfected elements of the mouse tissue transglutaminase promoter linked to a reporter enzyme revealed their overall repression in cells expressing c-Myc. This repression was partially suspended in cells also carrying Bcl-2. Our data suggest that tissue transglutaminase is not induced when c-Myc initiates apoptosis but the pre-existing endogenous enzyme is activated.

UR - http://www.scopus.com/inward/record.url?scp=0031577328&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031577328&partnerID=8YFLogxK

U2 - 10.1006/bbrc.1997.6969

DO - 10.1006/bbrc.1997.6969

M3 - Article

C2 - 9240425

AN - SCOPUS:0031577328

VL - 236

SP - 280

EP - 284

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -