Cited by 404Cancer, Lipids, and MetabolismLipid metabolism and biosynthesisCancer, Hypoxia, and Metabolism

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ATP citrate lyase: activation and therapeutic implications in non-small cell lung cancer

Migita, Toshiro, Narita, Tadahito, Nomura, Kimie, Miyagi, Erika, Inazuka, Fumika, Matsuura, Masaaki, Ushijima, Masaru, Mashima, Tetsuo, Seimiya, Hiroyuki, Satoh, Yukitoshi, Okumura, Sakae, Nakagawa, Ken, Ishikawa, Yuichi·2008·Cancer Research

DOI 10.1158/0008-5472.can-08-1235

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Abstract

Enhanced glucose and lipid metabolism is one of the most common properties of malignant cells. ATP citrate lyase (ACLY) is a key enzyme of de novo fatty acid synthesis responsible for generating cytosolic acetyl-CoA and oxaloacetate. To evaluate its role in lung cancer progression, we here analyzed ACLY expression in a subset of human lung adenocarcinoma cell lines and showed a relationship with the phosphatidyl-inositol-3 kinase–Akt pathway. The introduction of constitutively active Akt into cells enhanced the phosphorylation of ACLY, whereas dominant-negative Akt caused attenuation. In human lung adenocarcinoma samples, ACLY activity was found to be significantly higher than in normal lung tissue. Immunohistochemical analysis further showed phosphorylated ACLY overexpression in 162 tumors, well-correlating with stage, differentiation grade, and a poorer prognosis. Finally, to show the therapeutic potential and mechanism of ACLY inhibition for lung cancer treatment, we assessed the effect of RNA interference targeting ACLY on lipogenesis and cell proliferation in A549 cells. ACLY inhibition resulted in growth arrest in vitro and in vivo. Interestingly, increased intracellular lipids were found in ACLY knockdown cells, whereas de novo lipogenesis was inhibited. Supplementation of insulin could rescue the proliferative arrest elicited by ACLY inhibition; however, in contrast, fatty acid palmitate induced cell death. Taken together, these findings suggest that ACLY is involved in lung cancer pathogenesis associated with metabolic abnormality and might offer a novel therapeutic target. [Cancer Res 2008;68(20):8547–54]

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Authors: Migita, T., Narita, T., Nomura, K., Miyagi, E., Inazuka, F., Matsuura, M., Ushijima, M., Mashima, T., Seimiya, H., Satoh, Y., Okumura, S., Nakagawa, K., & Ishikawa, Y.
Affiliations: 1Pathology and Divisions of
Zenyaku Kogyo (Japan) (JP)
2Cancer Genomics, The Cancer Institute,
3Bioinformatics Group, Genome Center,
4Division of Molecular Biotherapy, Cancer Chemotherapy Center,
The Cancer Institute Hospital (JP)
ORCID: Migita, Toshiro
Ushijima, Masaru
Mashima, Tetsuo
Seimiya, Hiroyuki
Satoh, Yukitoshi
Nakagawa, Ken
Ishikawa, Yuichi
Venue: Cancer Research
Publisher: American Association for Cancer Research (AACR)
Published: 2008-10-15
Volume: 68
Issue: 20
Pages: 8547-8554
ISSN: 0008-5472 (ISSN-L)
1538-7445
DOI: 10.1158/0008-5472.can-08-1235
OpenAlex: W2136765222
Cited by: 403
References: 45
Citations by year: 2026: 17 · 2025: 16 · 2024: 32 · 2023: 26 · 2022: 36 · 2021: 48 · 2020: 34 · 2019: 24 · 2018: 25 · 2017: 21 · 2016: 17 · 2015: 21 · 2014: 20 · 2013: 22 · 2012: 17
FWCI: 2.93
Type: journal article
Language: en
Open access: closed
Locations: Cancer Research (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
Keywords: ATP citrate lyase, non-small cell lung cancer, lung adenocarcinoma, de novo lipogenesis, lipogenesis, Akt signaling, PI3K/Akt signaling, acetyl-CoA, cancer metabolism, RNA interference, insulin, palmitate, cell proliferation, prognostic factors, therapeutic target
MeSH terms: Adenocarcinoma, Animals, ATP Citrate (pro-S)-Lyase, Carcinoma, Non-Small-Cell Lung, Enzyme Activation, Humans, Lung Neoplasms, Phosphorylation, Prognosis, Cell Line, Tumor, Proto-Oncogene Proteins c-akt, Mice

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ATP citrate lyase: activation and therapeutic implications in non-small cell lung cancer

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