Altered expression of the DNA repair- protein, N-methylpurine-DNA glycosylase (MPG), in breast cancer

Sonia R. Cerda; Patrick W. Turk; Ann D. Thor; Sigmund A. Weitzman

doi:10.1016/S0014-5793(98)00697-8

Altered expression of the DNA repair- protein, N-methylpurine-DNA glycosylase (MPG), in breast cancer

Sonia R. Cerda, Patrick W. Turk, Ann D. Thor, Sigmund A. Weitzman^*

^*Corresponding author for this work

Medicine, Hematology Oncology Division

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

40 Scopus citations

Abstract

We examined expression of N-methylpurine-DNA glycosylase (MPG), a DNA repair enzyme that removes N-alkylpurine damage, in normal, malignant, and immortalized breast epithelial cells, and breast cancer cell lines (MDA-MB-231, MCF7, T47D). Northern analysis showed increased expression in cancer versus normal breast epithelial cells (2-24-fold). Southern blots revealed no gene amplification or polymorphisms. Immunofluorescence, immunohistochemistry, and Western blot analysis demonstrated increased MPG protein expression in the tumor cells that correlated with elevated glycosylase activity. Since MPG overexpression has been shown to be paradoxically associated with increased susceptibility to DNA damage, up-regulation of this gene may suggest a functional role in breast carcinogenesis.

Original language	English (US)
Pages (from-to)	12-18
Number of pages	7
Journal	FEBS Letters
Volume	431
Issue number	1
DOIs	https://doi.org/10.1016/S0014-5793(98)00697-8
State	Published - Jul 10 1998

Funding

We gratefully acknowledge Dr. Benilde Jimenez, Meredith Gonzales, and Angela Cisneros for technical assistance with cloning of recombinant proteins, immunofluorescence, and HPLC techniques respectively, and Dr. Jonathan Jones for the use of the Zeiss Photomicroscope III. We are grateful to Dr. S. Mitra (University of Texas Medical Branch) for providing us with the cloned cDNA encoding human MPG; Dr. T. Lukas (Northwestern University Medical Center) for the design of the peptides; and Dr. T. O'Connor (City of Hope, Beckman Research Institute, CA) for supplying us with the purified human MPG protein. This study was supported by the US Army (DAMD17-94-J-4466), the Lynn Sage Cancer Research Foundation, and the National Institute of Health (AG11536).

Keywords

Alkylpurine
Breast cancer
DNA repair
N-methylpurine-DNA glycosylase

ASJC Scopus subject areas

Genetics
Molecular Biology
Biophysics
Structural Biology
Biochemistry
Cell Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/S0014-5793(98)00697-8

Cite this

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title = "Altered expression of the DNA repair- protein, N-methylpurine-DNA glycosylase (MPG), in breast cancer",

abstract = "We examined expression of N-methylpurine-DNA glycosylase (MPG), a DNA repair enzyme that removes N-alkylpurine damage, in normal, malignant, and immortalized breast epithelial cells, and breast cancer cell lines (MDA-MB-231, MCF7, T47D). Northern analysis showed increased expression in cancer versus normal breast epithelial cells (2-24-fold). Southern blots revealed no gene amplification or polymorphisms. Immunofluorescence, immunohistochemistry, and Western blot analysis demonstrated increased MPG protein expression in the tumor cells that correlated with elevated glycosylase activity. Since MPG overexpression has been shown to be paradoxically associated with increased susceptibility to DNA damage, up-regulation of this gene may suggest a functional role in breast carcinogenesis.",

keywords = "Alkylpurine, Breast cancer, DNA repair, N-methylpurine-DNA glycosylase",

author = "Cerda, {Sonia R.} and Turk, {Patrick W.} and Thor, {Ann D.} and Weitzman, {Sigmund A.}",

note = "Funding Information: We gratefully acknowledge Dr. Benilde Jimenez, Meredith Gonzales, and Angela Cisneros for technical assistance with cloning of recombinant proteins, immunofluorescence, and HPLC techniques respectively, and Dr. Jonathan Jones for the use of the Zeiss Photomicroscope III. We are grateful to Dr. S. Mitra (University of Texas Medical Branch) for providing us with the cloned cDNA encoding human MPG; Dr. T. Lukas (Northwestern University Medical Center) for the design of the peptides; and Dr. T. O'Connor (City of Hope, Beckman Research Institute, CA) for supplying us with the purified human MPG protein. This study was supported by the US Army (DAMD17-94-J-4466), the Lynn Sage Cancer Research Foundation, and the National Institute of Health (AG11536).",

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AU - Weitzman, Sigmund A.

N1 - Funding Information: We gratefully acknowledge Dr. Benilde Jimenez, Meredith Gonzales, and Angela Cisneros for technical assistance with cloning of recombinant proteins, immunofluorescence, and HPLC techniques respectively, and Dr. Jonathan Jones for the use of the Zeiss Photomicroscope III. We are grateful to Dr. S. Mitra (University of Texas Medical Branch) for providing us with the cloned cDNA encoding human MPG; Dr. T. Lukas (Northwestern University Medical Center) for the design of the peptides; and Dr. T. O'Connor (City of Hope, Beckman Research Institute, CA) for supplying us with the purified human MPG protein. This study was supported by the US Army (DAMD17-94-J-4466), the Lynn Sage Cancer Research Foundation, and the National Institute of Health (AG11536).

PY - 1998/7/10

Y1 - 1998/7/10

N2 - We examined expression of N-methylpurine-DNA glycosylase (MPG), a DNA repair enzyme that removes N-alkylpurine damage, in normal, malignant, and immortalized breast epithelial cells, and breast cancer cell lines (MDA-MB-231, MCF7, T47D). Northern analysis showed increased expression in cancer versus normal breast epithelial cells (2-24-fold). Southern blots revealed no gene amplification or polymorphisms. Immunofluorescence, immunohistochemistry, and Western blot analysis demonstrated increased MPG protein expression in the tumor cells that correlated with elevated glycosylase activity. Since MPG overexpression has been shown to be paradoxically associated with increased susceptibility to DNA damage, up-regulation of this gene may suggest a functional role in breast carcinogenesis.

AB - We examined expression of N-methylpurine-DNA glycosylase (MPG), a DNA repair enzyme that removes N-alkylpurine damage, in normal, malignant, and immortalized breast epithelial cells, and breast cancer cell lines (MDA-MB-231, MCF7, T47D). Northern analysis showed increased expression in cancer versus normal breast epithelial cells (2-24-fold). Southern blots revealed no gene amplification or polymorphisms. Immunofluorescence, immunohistochemistry, and Western blot analysis demonstrated increased MPG protein expression in the tumor cells that correlated with elevated glycosylase activity. Since MPG overexpression has been shown to be paradoxically associated with increased susceptibility to DNA damage, up-regulation of this gene may suggest a functional role in breast carcinogenesis.

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KW - Breast cancer

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Altered expression of the DNA repair- protein, N-methylpurine-DNA glycosylase (MPG), in breast cancer

Abstract

Funding

Keywords

ASJC Scopus subject areas

UN SDGs

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