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编号:11400611
人牙髓细胞DPDP2基因的克隆、测序及序列分析
http://www.100md.com 《第四军医大学学报》 2007年第4期
牙髓,细胞学;牙龈;成纤维细胞;基因文库;序列分析;BLAST分析,,牙髓,细胞学;牙龈;成纤维细胞;基因文库;序列分析;BLAST分析,【关键词】牙髓,细胞学;牙龈;成纤维细胞;基因文库;序列分析;BLAST分析,0引言,1材料和方法,2结果
     Sequence analysis of DPDP2 gene cloned from human dental pulp cells

    WANG ZhongDong1,3, GUO HongYan2, WU JiNan3, LING JunQi1, XIAO MingZhen4, GUO XiMin5, CHAI YuBo6

    1Guanghua Hospital of Stomatology, Sun Yatsen University, Guangzhou 510055, China, 2Department of Stomatology, General Hospital of Chinese Peoples Armed Police Forces, Beijing 100039, China, 3Dental Care Center, Peoples Hospital, Zhongshan, 528400, China, 4School of Stomatology, 6School of Basic Medicine, Fourth Military Medical University, Xian 710033, China, 5Institute of Basic Medical Sciences, Academy of Military Medical Sciences, Beijing 100850, China

    【Abstract】 AIM: To study the function of DPDP2, a new gene cloned from human dental pulp cell (HDPC). METHODS: A modified PCRbased subtractive hybridization technique was used to establish a subtractive cDNA library. Genes differentially expressed in HPDC and human gingival fibroblasts (HGF) were cloned and sequenced. A new gene named DPDP2 was cloned and structural and functional analyses were performed by PC/GENE 6.60 software. RESULTS: The fragment of DPDP2 cloned from the present subtractive cDNA library was 810 bp, containing an incomplete coding region. However, after splicing with an EST sequence named KIAA0265, a 6172 bp complete cDNA sequence was achieved which encodes a 83aa hydrophobic protein with a secondary structure characterized by a helical conformation, an extended conformation and a coil conformation. The secondary structures could assemble a threedimensional structure through folding of α, β or α/β sheets. Antigen epitope analysis implied three possible antigenic determinants:GluAsnLysArgThrGly, LeuIleGluArgLeuLys and GluLeuAlaTrpGluLys. A transmembrane helical structure and a mitochondria transportation structure were also found. Signal peptide analysis further indicated that DPDP2 was a nonsecretory protein. No homogeneous protein was found in Nonredundant SwissProt sequences and PDB protein database. CONCLUSION: DPDP2 encodes a transmembrane protein that has both signal transduction structural features and CKII phosphorylation site, indicating its possible functional relationship with cell mitosis and transcription. ......

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