Patt1, a novel protein acetyltransferase that is highly expressed in liver and downregulated in hepatocellular carcinoma, enhances apoptosis of hepatoma cells

Liu, Zhen; Liu, Yang; Wang, Huiqiang; Ge, Xinjian; Jin, Qihuang; Ding, Gui‐Rong; Hu, Yanan; Zhou, Ben; Chen, Zhongjian; Ge, Xuemei; Zhang, Baohua; Man, Xiao-hua; Zhai, Qiwei

doi:10.1016/j.biocel.2009.08.009

Cited by 35 publications

(54 citation statements)

References 38 publications

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“…Histone acetyltransferase p300 has been reported to stimulate ChREBP transactivation through histone acetylation, thus to activate lipogenesis ( 20 ). Our previous study demonstrates that Patt1 locates in both nucleus and cytoplasm and exhibits histone acetyltransferase activity ( 28 ). Similarly, in this study, we found that acetylation of histone H4 (Lys8) was significantly decreased in the liver of Patt1 LKO mice (supplementary Fig.…”

Section: Discussionsupporting

confidence: 76%

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Liver Patt1 deficiency protects male mice from age-associated but not high-fat diet-induced hepatic steatosis

Liu

Zhou

Zhang

et al. 2012

Journal of Lipid Research

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Section: Discussionsupporting

confidence: 76%

“…Patt1 is a newly identifi ed acetyltransferase belonging to the GCN5-related N -acetyltransferase (GNAT) family, and it is highly expressed in mouse liver ( 28 ). To investigate the role of Patt1 in liver, we used a Cre-loxP strategy to delete Patt1 specifi cally in liver.…”

Section: Enzyme Activity Measurementsmentioning

confidence: 99%

Liver Patt1 deficiency protects male mice from age-associated but not high-fat diet-induced hepatic steatosis

Liu

Zhou

Zhang

et al. 2012

Journal of Lipid Research

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“…Although NatD is downregulated in hepatocellular carcinoma, its overexpression enhances apoptosis in cancerous cells [163]. Depletion of NatD further demonstrated the involvement of NatD in protecting cancer cells from drug-induced apoptosis.…”

Section: Natc D E and F In Tumor Developmentmentioning

confidence: 96%

“…NatD is downregulated in hepatocellular carcinoma, and shown to protect cells from drug induced apoptosis [163]. NatD Nt-acetylates histone H4, thereby regulating arginine methylation and ribosomal DNA silencing, and might act as a sensor for cell growth [106].…”

Section: Natc D E and F In Tumor Developmentmentioning

confidence: 99%

The world of protein acetylation

Drazic

Myklebust

Ree

et al. 2016

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

612

532

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Acetylation is one of the major post-translational protein modifications in the cell, with manifold effects on the protein level as well as on the metabolome level. The acetyl group, donated by the metabolite acetyl-coenzyme A, can be co- or post-translationally attached to either the α-amino group of the N-terminus of proteins or to the ε-amino group of lysine residues. These reactions are catalyzed by various N-terminal and lysine acetyltransferases. In case of lysine acetylation, the reaction is enzymatically reversible via tightly regulated and metabolism-dependent mechanisms. The interplay between acetylation and deacetylation is crucial for many important cellular processes. In recent years, our understanding of protein acetylation has increased significantly by global proteomics analyses and in depth functional studies. This review gives a general overview of protein acetylation and the respective acetyltransferases, and focuses on the regulation of metabolic processes and physiological consequences that come along with protein acetylation.

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“…In addition, their recent studies have revealed a novel class of antagonists for the FFA receptor G protein-coupled receptor 40 and a pair of windmill-shaped enantiomers from Lindera aggregata possessing an ability to improve insulin sensitivity (25,26). During the studies on protein acetyltransferases, Dr. Zhai's laboratory found that p300/CBP-associated factor acetylates b-catenin and improves its stability (27) and identified a novel protein acetyltransferase Patt1 that is highly expressed in the liver and enhances apoptosis of hepatoma cells (28).…”

Section: Nutritional Interventionmentioning

confidence: 97%

Research Advances at the Institute for Nutritional Sciences at Shanghai, China

Chen

Lin

Liu

et al. 2011

Advances in Nutrition

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Nutrition-related health issues have emerged as a major threat to public health since the rebirth of the economy in China starting in the 1980s. To meet this challenge, the Chinese Academy of Sciences established the Institute for Nutritional Sciences (INS) at Shanghai, China ≈ 8 y ago. The mission of the INS is to apply modern technologies and concepts in nutritional research to understand the molecular mechanism and provide means of intervention in the combat against nutrition-related diseases, including type 2 diabetes, metabolic syndrome, obesity, cardiovascular diseases, and many types of cancers. Through diligent and orchestrated efforts by INS scientists, graduate students, and research staff in the past few years, the INS has become the leading institution in China in the areas of basic nutritional research and metabolic regulation. Scientists at the INS have made important progress in many areas, including the characterization of genetic and nutritional properties of the Chinese population, metabolic control associated with nutrient sensing, molecular mechanisms underlying glucose and lipid metabolism, regulation of metabolism by adipokines and inflammatory pathways, disease intervention using functional foods or extracts of Chinese herbs, and many biological studies related to carcinogenesis. The INS will continue its efforts in understanding the optimal nutritional needs for Chinese people and the molecular causes associated with metabolic diseases, thus paving the way for effective and individualized intervention in the future. This review highlights the major research endeavors undertaken by INS scientists in recent years.

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Patt1, a novel protein acetyltransferase that is highly expressed in liver and downregulated in hepatocellular carcinoma, enhances apoptosis of hepatoma cells

Cited by 35 publications

References 38 publications

Liver Patt1 deficiency protects male mice from age-associated but not high-fat diet-induced hepatic steatosis

Liver Patt1 deficiency protects male mice from age-associated but not high-fat diet-induced hepatic steatosis

The world of protein acetylation

Research Advances at the Institute for Nutritional Sciences at Shanghai, China

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