Overexpression of phospholipase D1 in human breast cancer tissues

Dong Young Noh; Soo Jung Ahn; Ryung Ah Lee; In Ae Park; Jae Ho Kim; Pann Ghill Suh; Sung Ho Ryu; Kweon Haeng Lee; Joong Soo Han

doi:10.1016/S0304-3835(00)00612-1

Overexpression of phospholipase D1 in human breast cancer tissues

Dong Young Noh, Soo Jung Ahn, Ryung Ah Lee, In Ae Park, Jae Ho Kim, Pann Ghill Suh, Sung Ho Ryu, Kweon Haeng Lee, Joong Soo Han

Department of Surgery

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

159 Scopus citations

Abstract

Phospholipase D (PLD) catalyzes the hydrolysis of phosphatidylcholine (PC) to produce phosphatidic acid (PA) and choline. PLD is a major enzyme implicated in important cellular processes, such as cell proliferation. We designed this study to investigate the expression of PLD in human breast carcinomas and non-malignant tissues using RT-PCR, Western blot analysis, immunohistochemistry and an Arf-dependent PLD activity assay. We examined about 550 bp of PCR product and 120 kDa of PLD protein. Our results showed that PLD protein and mRNA levels were overexpressed in 14 of 17 breast cancer tissues. We also observed increased expression by immunohistochemistry and Arf-dependent PLD activity in microsomes of human breast tumors, which correlated well with PLD expression. PLD expression was elevated in human breast tumors compared with normal breast tissues. These results implicate a possible role of PLD in human breast tumorigenesis and suggest that PLD may be useful as a marker for malignant disease in the breast. (C) 2000 Elsevier Science Ireland Ltd.

Original language	English
Pages (from-to)	207-214
Number of pages	8
Journal	Cancer Letters
Volume	161
Issue number	2
DOIs	https://doi.org/10.1016/S0304-3835(00)00612-1
State	Published - 20 Dec 2000

Bibliographical note

Funding Information:
Supported by grants 96-0403-02-01-3 from Korea Science and Engineering Foundation (KOSEF). D.Y. Noh and S.J. Ahn contributed equally to this work. The authors would like to thank Dr S.G. Rhee (Laboratory of Cell Signaling, National Institute of Health, Bethesda, MD) for his kind discussions.

Keywords

Breast cancer tissues
Phospholipase D
Tumorigenesis

UN SDGs

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

Access to Document

10.1016/S0304-3835(00)00612-1

Cite this

@article{0160872ddbb5437bbae03339664faedf,

title = "Overexpression of phospholipase D1 in human breast cancer tissues",

abstract = "Phospholipase D (PLD) catalyzes the hydrolysis of phosphatidylcholine (PC) to produce phosphatidic acid (PA) and choline. PLD is a major enzyme implicated in important cellular processes, such as cell proliferation. We designed this study to investigate the expression of PLD in human breast carcinomas and non-malignant tissues using RT-PCR, Western blot analysis, immunohistochemistry and an Arf-dependent PLD activity assay. We examined about 550 bp of PCR product and 120 kDa of PLD protein. Our results showed that PLD protein and mRNA levels were overexpressed in 14 of 17 breast cancer tissues. We also observed increased expression by immunohistochemistry and Arf-dependent PLD activity in microsomes of human breast tumors, which correlated well with PLD expression. PLD expression was elevated in human breast tumors compared with normal breast tissues. These results implicate a possible role of PLD in human breast tumorigenesis and suggest that PLD may be useful as a marker for malignant disease in the breast. (C) 2000 Elsevier Science Ireland Ltd.",

keywords = "Breast cancer tissues, Phospholipase D, Tumorigenesis",

author = "Noh, {Dong Young} and Ahn, {Soo Jung} and Lee, {Ryung Ah} and Park, {In Ae} and Kim, {Jae Ho} and Suh, {Pann Ghill} and Ryu, {Sung Ho} and Lee, {Kweon Haeng} and Han, {Joong Soo}",

note = "Funding Information: Supported by grants 96-0403-02-01-3 from Korea Science and Engineering Foundation (KOSEF). D.Y. Noh and S.J. Ahn contributed equally to this work. The authors would like to thank Dr S.G. Rhee (Laboratory of Cell Signaling, National Institute of Health, Bethesda, MD) for his kind discussions.",

year = "2000",

month = dec,

day = "20",

doi = "10.1016/S0304-3835(00)00612-1",

language = "English",

volume = "161",

pages = "207--214",

journal = "Cancer Letters",

issn = "0304-3835",

publisher = "Elsevier Ireland Ltd",

number = "2",

}

TY - JOUR

T1 - Overexpression of phospholipase D1 in human breast cancer tissues

AU - Noh, Dong Young

AU - Ahn, Soo Jung

AU - Lee, Ryung Ah

AU - Park, In Ae

AU - Kim, Jae Ho

AU - Suh, Pann Ghill

AU - Ryu, Sung Ho

AU - Lee, Kweon Haeng

AU - Han, Joong Soo

N1 - Funding Information: Supported by grants 96-0403-02-01-3 from Korea Science and Engineering Foundation (KOSEF). D.Y. Noh and S.J. Ahn contributed equally to this work. The authors would like to thank Dr S.G. Rhee (Laboratory of Cell Signaling, National Institute of Health, Bethesda, MD) for his kind discussions.

PY - 2000/12/20

Y1 - 2000/12/20

N2 - Phospholipase D (PLD) catalyzes the hydrolysis of phosphatidylcholine (PC) to produce phosphatidic acid (PA) and choline. PLD is a major enzyme implicated in important cellular processes, such as cell proliferation. We designed this study to investigate the expression of PLD in human breast carcinomas and non-malignant tissues using RT-PCR, Western blot analysis, immunohistochemistry and an Arf-dependent PLD activity assay. We examined about 550 bp of PCR product and 120 kDa of PLD protein. Our results showed that PLD protein and mRNA levels were overexpressed in 14 of 17 breast cancer tissues. We also observed increased expression by immunohistochemistry and Arf-dependent PLD activity in microsomes of human breast tumors, which correlated well with PLD expression. PLD expression was elevated in human breast tumors compared with normal breast tissues. These results implicate a possible role of PLD in human breast tumorigenesis and suggest that PLD may be useful as a marker for malignant disease in the breast. (C) 2000 Elsevier Science Ireland Ltd.

AB - Phospholipase D (PLD) catalyzes the hydrolysis of phosphatidylcholine (PC) to produce phosphatidic acid (PA) and choline. PLD is a major enzyme implicated in important cellular processes, such as cell proliferation. We designed this study to investigate the expression of PLD in human breast carcinomas and non-malignant tissues using RT-PCR, Western blot analysis, immunohistochemistry and an Arf-dependent PLD activity assay. We examined about 550 bp of PCR product and 120 kDa of PLD protein. Our results showed that PLD protein and mRNA levels were overexpressed in 14 of 17 breast cancer tissues. We also observed increased expression by immunohistochemistry and Arf-dependent PLD activity in microsomes of human breast tumors, which correlated well with PLD expression. PLD expression was elevated in human breast tumors compared with normal breast tissues. These results implicate a possible role of PLD in human breast tumorigenesis and suggest that PLD may be useful as a marker for malignant disease in the breast. (C) 2000 Elsevier Science Ireland Ltd.

KW - Breast cancer tissues

KW - Phospholipase D

KW - Tumorigenesis

UR - http://www.scopus.com/inward/record.url?scp=0034695165&partnerID=8YFLogxK

U2 - 10.1016/S0304-3835(00)00612-1

DO - 10.1016/S0304-3835(00)00612-1

M3 - Article

C2 - 11090971

AN - SCOPUS:0034695165

SN - 0304-3835

VL - 161

SP - 207

EP - 214

JO - Cancer Letters

JF - Cancer Letters

IS - 2

ER -

Overexpression of phospholipase D1 in human breast cancer tissues

Abstract

Bibliographical note

Keywords

UN SDGs

Access to Document

Fingerprint

Cite this