Associations between hepatitis C viremia and low serum triglyceride and cholesterol levels: A community-based study
- 作者：Chia-Yen Dai ; Wan-Long Chuang ; Chi-Kung Ho ; Ming-Yen Hsieh ; Jee-Fu Huang ; Li-Po Lee ; Nai-Jen Hou ; Zu-Yau Lin ; Shinn-Cherng Chen ; Ming-Yuh Hsieh ; Liang-Yen Wang ; Jun-Fa Tsai ; Wen-Yu Chang ; Ming-Lung Yu
- 关键词：anti-HCV ; HCV RNA ; Cholesterol ; Triglyceride ; Viremia
- 刊名：Journal of Hepatology
- 出版年：2008
- 期刊代码：162_01688278
- 类别：med
- 出版时间：July 2008
- 卷：49
- 期：1
- 页码：9-16
- 文件大小：163 K
摘要
Membrane microdomains (MDs), or lipid rafts, are recently identified dynamic membrane domains on which various signal-transductions are performed. Intracellular Ca2+-binding proteins participate in the Ca2+ signaling through interaction with various proteins. Neurocalcin 
(NC) is a member of neuronal calcium sensor (NCS) protein family and shows Ca2+-dependent binding to the cell membrane through N-terminal myristoyl moiety. Since NC was identified as a Ca2+-dependent binding protein to neuronal MDs, its binding proteins may participate in the signal-transduction on the MDs. In an immunoprecipitate using anti-NC antibody, alsin (ALS2), a protein product of one of the responsive genes for amyotrophic lateral sclerosis, was detected through LC–MS/MS. Specific antibody to alsin was produced and immunoprecipitation using this antibody showed co-sedimentation of NC. Some part of alsin bound to brain-derived MD fraction in the presence of Ca2+ ions and eluted out by the chelation of Ca2+ ions, as in the case of NC. Immunostaining of cultured neurons showed broad distribution of alsin and NC, and membrane association of these proteins were increased through Ca2+ loading by maitotoxin. These results suggest that alsin binds cell membrane in a Ca2+-dependent manner through NC and regulates membrane dynamics.
(NC) is a member of neuronal calcium sensor (NCS) protein family and shows Ca2+-dependent binding to the cell membrane through N-terminal myristoyl moiety. Since NC was identified as a Ca2+-dependent binding protein to neuronal MDs, its binding proteins may participate in the signal-transduction on the MDs. In an immunoprecipitate using anti-NC antibody, alsin (ALS2), a protein product of one of the responsive genes for amyotrophic lateral sclerosis, was detected through LC–MS/MS. Specific antibody to alsin was produced and immunoprecipitation using this antibody showed co-sedimentation of NC. Some part of alsin bound to brain-derived MD fraction in the presence of Ca2+ ions and eluted out by the chelation of Ca2+ ions, as in the case of NC. Immunostaining of cultured neurons showed broad distribution of alsin and NC, and membrane association of these proteins were increased through Ca2+ loading by maitotoxin. These results suggest that alsin binds cell membrane in a Ca2+-dependent manner through NC and regulates membrane dynamics.