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Home > Mathematics and Science books > Biology, life sciences > Biochemistry > Subcellular Localisation of Growth Suppressor Protein Deleted in Liver Cancer 2 (Dlc2)
Subcellular Localisation of Growth Suppressor Protein Deleted in Liver Cancer 2 (Dlc2)

Subcellular Localisation of Growth Suppressor Protein Deleted in Liver Cancer 2 (Dlc2)


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About the Book

This dissertation, "Subcellular Localisation of Growth Suppressor Protein Deleted in Liver Cancer 2 (DLC2)" by Chi-heng, David, Ng, 吳志恒, was obtained from The University of Hong Kong (Pokfulam, Hong Kong) and is being sold pursuant to Creative Commons: Attribution 3.0 Hong Kong License. The content of this dissertation has not been altered in any way. We have altered the formatting in order to facilitate the ease of printing and reading of the dissertation. All rights not granted by the above license are retained by the author. Abstract: Abstract of thesis entitled Subcellular localisation of growth suppressor protein Deleted in Liver Cancer 2 (DLC2) Submitted by David Chi Heng NG For the degree of Master of Philosophy at The University of Hong Kong in May 2005 Hepatocellular carcinoma (HCC) is one leading cause of cancer death in Asia and in the world. Hepatocarcinogenesis is a multistage process, in which chromosomal aberrations frequently occur on chromosome 1p, 8p, 13q, 16p and 17p, leading to alteration of genes that govern cell growth and tumour suppression. Deleted in liver cancer 2 (DLC2) is a candidate tumour suppressor on chromosome 13 frequently found to be deleted in HCC. DLC2 is a multifunctional protein containing sterile alpha motif (SAM), GTPase-activating protein (GAP) and StAR-related lipid transfer (START) domains. In this study, I characterised a newly identified isoform of DLC2, namely DLC2-γ, which lacks the 5'-SAM domain due to alternative splicing. I also defined the subcellular localization pattern of DLC2 in hepatoma cell line Huh-7. Both DLC2-α and DLC2-γ can suppress Ras-induced activation of serum response element, suggesting that the RhoGAP domain is functional in both isoforms. DLC2-α and DLC2-γ localised to punctate structures in the cytosol. A truncation mutant of DLC2 containing the START domain only, named DLC2-START, showed a localization pattern identical to that of DLC2, indicating that the START domain could mediate organelle targeting or tethering. Co-localisation studies revealed that DLC2 and DLC2-START proteins localized to mitochondria. In addition, the DLC2-containing cytoplasmic speckles were distributed around lipid droplets. Expression of full-length DLC2-α and DLC2-γ induces dissolution of actin stress fibres, whereas DLC2-START alone was insufficient for this activity. Taken together, I have provided the first evidence for expression of DLC2-α and DLC2-γ in cultured hepatoma cells, for DLC2-induced dissolution of actin stress fibres, and for mitochondrial localization and lipid-droplet association of DLC2. My findings have implications in liver physiology and carcinogenesis. An abstract of exactly 272 words DOI: 10.5353/th_b3202831 Subjects: Antioncogenes Liver - Cancer - Genetic aspects


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Product Details
  • ISBN-13: 9781361234877
  • Publisher: Open Dissertation Press
  • Publisher Imprint: Open Dissertation Press
  • Height: 279 mm
  • No of Pages: 86
  • Weight: 222 gr
  • ISBN-10: 1361234873
  • Publisher Date: 26 Jan 2017
  • Binding: Paperback
  • Language: English
  • Spine Width: 5 mm
  • Width: 216 mm


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