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제114회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Expression and Structural Studies of FAS1 Domains of Human Periostin, an Extracellular Matrix Protein Involved in Cancer Metastasis and Chronic Allergic Inflammatory Diseases

2014년 8월 28일 16시 43분 15초
BIO.P-646 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
10월 15일 (수요일) 16:00~19:00
저자 및
윤효숙, 이철원*
전남대학교 화학과, Korea
Periostin, a component of the extracellular matrix expressed by fibroblasts in normal tissues and stroma of primary tumor, is associated with asthma, chronic allergic inflammation and metastatic colony formation. The four internal repeat fasciclin I (FAS1) domains of periostin play an important role in cell adhesion and tumor metastasis by binding with integrins. At the N-terminus, periostin has a cysteine-rich EMILIN (EMI) domain involved in protein-protein interactions. We successfully refolded EMI domain having a correct three intramolecular disulfide bonds in a proper redox buffer condition. The gene of the FAS1 domains of human periostin were systemically constructed and their expression were tested using E. coli expression system. Although all FAS1 domains were well expressed, but only FAS1_II and IV were soluble fractions after cell lysis. The structural characteristics of FAS1 domains studied by circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy. CD studies clearly showed that FAS1_II and IV domains were composed of α-helix and β-sheet structure, which is consistent with a previously determined FAS1 domain from Drosophila melanogaster. NMR studies showed that FAS1_II and IV domains are well folded. We obtained backbone resonance assignment of FAS1_IV domain of human periostin using triple resonance NMR spectroscopy : HNCA, HN(CO)CA, HNCACB, CBCA(CO)NH. These results suggest that human periostin domain especially FAS1_IV is good target for further biochemical and structural studies.