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

Research output: Contribution to journalArticlepeer-review

159 Scopus citations


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 languageEnglish
Pages (from-to)207-214
Number of pages8
JournalCancer Letters
Issue number2
StatePublished - 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.


  • Breast cancer tissues
  • Phospholipase D
  • Tumorigenesis


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