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学科主题: 临床医学
题名:
Identification of proteins that interact with alpha A-crystallin using a human proteome microarray
作者: Fan, Qi1; Huang, Lv-Zhen2; Zhu, Xiang-Jia1; Zhang, Ke-Ke1; Ye, Hong-Fei1; Luo, Yi1; Sun, Xing-Huai1; Zhou, Peng3; Lu, Yi1
刊名: MOLECULAR VISION
发表日期: 2014-01-14
卷: 20, 页:117-124
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Biochemistry & Molecular Biology ; Ophthalmology
研究领域[WOS]: Biochemistry & Molecular Biology ; Ophthalmology
关键词[WOS]: LENS EPITHELIAL-CELLS ; B-CRYSTALLIN ; ACTIN ; MOUSE ; TRANSPARENCY ; STABILIZES ; CATARACT ; PREVENTS ; BINDING ; TISSUES
英文摘要:

Purpose: To identify proteins interacting with alpha A-crystallin (CRYAA) and to investigate the potential role that these protein interactions play in the function of CRYAA using a human proteome (HuProt) microarray.

Methods: The active full-length CRYAA protein corresponding to amino acids 1-173 of CRYAA was recombined. A HuProt microarray composed of 17,225 human full-length proteins with N-terminal glutathione S-transferase (GST) tags was used to identify protein-protein interactions. The probes were considered detectable when the signal to noise ratio (SNR) was over 1.2. The identified proteins were subjected to subsequent bioinformatics analysis using the DAVID database.

Results: The HuProt microarray results showed that the signals of 343 proteins were higher in the recombinant CRYAA group than in the control group. The SNR of 127 proteins was >= 1.2. The SNR of the following eight proteins was > 3.0: hematopoietic cell-specific Lyn substrate 1 (HCLS1), Kelch domain-containing 6 (KLHDC6), sarcoglycan delta (SGCD), KIAA1706 protein (KIAA1706), RNA guanylyltransferase and 5′-phosphatase (RNGTT), chromosome 10 open reading frame 57 (C10orf57), chromosome 9 open reading frame 52 (C9orf52), and plasminogen activator, urokinase receptor (PLAUR). The bioinformatics analysis revealed 127 proteins associated with phosphoproteins, alternative splicing, acetylation, DNA binding, the nuclear lumen, ribonucleotide binding, the cell cycle, WD40 repeats, protein transport, transcription factor activity, GTP binding, and cellular response to stress. Functional annotation clustering showed that they belong to cell cycle, organelle or nuclear lumen, protein transport, and DNA binding and repair clusters. CRYAA interacted with these proteins to maintain their solubility and decrease the accumulation of denatured target proteins. The protein-protein interactions may help CRYAA carry out multifaceted functions.

Conclusions: One-hundred and twenty-seven of 17,225 human full-length proteins were identified that interact with CRYAA. The advent of microarray analysis enables a better understanding of the functions of CRYAA as a molecular chaperone.

语种: 英语
所属项目编号: 81200669 ; 81270989 ; 81100653 ; 20120071120089 ; 201302015
项目资助者: National Natural Science Foundation of China (NSFC) ; Doctoral Program of Higher Education of China (RFDP) ; Ministry of Public Health Research ; Fudan University
WOS记录号: WOS:000331825400002
Citation statistics:
内容类型: 期刊论文
URI标识: http://ir.bjmu.edu.cn/handle/400002259/58311
Appears in Collections:北京大学第二临床医学院_眼科_期刊论文

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作者单位: 1.Pkwy Hlth Hong Qiao Med Ctr, Dept Ophthalmol, Shanghai, Peoples R China
2.Fudan Univ, Eye & ENT Hosp, Dept Ophthalmol, Shanghai 200031, Peoples R China
3.Peking Univ, Peoples Hosp, Dept Ophthalmol, Beijing 100871, Peoples R China

Recommended Citation:
Fan, Qi,Huang, Lv-Zhen,Zhu, Xiang-Jia,et al. Identification of proteins that interact with alpha A-crystallin using a human proteome microarray[J]. MOLECULAR VISION,2014,20:117-124.
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