Hsiao-Yun Lee

Publications (2)7.96 Total impact

• Article: Proteome reference map of Drosophila melanogaster head.

  Tian-Ren Lee, Shun-Hong Huang, Chi-Ching Lee, Hsiao-Yun Lee, Hsin-Tzu Chan, Kuo-Sen Lin, Hong-Lin Chan, Ping-Chiang Lyu
  [show abstract] [hide abstract]
  ABSTRACT: Drosophila melanogaster has been used as a genetic model organism to understand the fundamental molecular mechanisms in human biology including memory formation that has been reported involving protein synthesis and/or post-translational modification. In this study, we employed a proteomic platform based on fluorescent 2DE and MALDI-TOF MS to build a standard D. melanogaster head proteome map for proteome-proteome comparison. In order to facilitate the comparison, an interactive database has been constructed for systematically integrating and analyzing the proteomes from different conditions and further implicated to study human diseases related to D. melanogaster model. In summary, the fundamental head proteomic database and bioinformatic analysis will be useful for further elucidating the biological mechanisms such as memory formation and neurodegenerative diseases.
  Proteomics 05/2012; 12(11):1875-8. · 4.43 Impact Factor
• Article: Proteomic analysis of a drosophila IBMPFD model reveals potential pathogenic mechanisms.

  Hsin-Tzu Chan, Tian-Ren Lee, Shun-Hong Huang, Hsiao-Yun Lee, Tzu-kang Sang, Hong-Lin Chan, Ping-Chiang Lyu
  [show abstract] [hide abstract]
  ABSTRACT: IBMPFD, Inclusion body myopathy associated with Paget's disease of bone and frontotemporal dementia, is a hereditary degenerative disorder due to single missense mutations in VCP (Valosin-Containing Protein). The mechanisms of how mutations of VCP lead to IBMPFD remain mysterious. Here we utilize two-dimensional difference gel electrophoresis (2D-DIGE) combined with mass spectrometry to study the IBMPFD disorder at the protein level. With this set-up, we are able to employ comparative proteomics to analyze IBMPFD disease using Drosophila melanogaster as our disease model organism. Head proteome of transgenic D. melanogaster expressing wild type VCP is compared, respectively, with the head proteome of transgenic mutant type VCPs that correspond to human IBMPFD disease alleles (TER94(A229E), TER94(R188Q), and TER94(R152H)). Of all the proteins identified, a significant fraction of proteins altered in TER94(A229E) and TER94(R188Q) mutants belong to the same functional categories, i.e. apoptosis and metabolism. Among these, Drosophila transferrin is observed to be significantly up-regulated in mutant flies expressing TER94(A229E). A knock-down experiment suggests that fly transferrin might be a potential modifier in IBMPFD disease. The molecular analysis of IBMPFD disease may benefit from the proteomics approach which combines the advantages of high throughput analysis and the focus on protein levels.
  Molecular BioSystems 04/2012; 8(6):1730-41. · 3.53 Impact Factor