C-reactive protein, sodium azide, and endothelial connexin43 gap junctions

被引:1
|
作者
Wang, Hsueh-Hsiao [2 ]
Yeh, Hung-I [1 ,2 ,3 ]
Wang, Chi-Young [4 ]
Su, Cheng-Huang [1 ,2 ]
Wu, Yih-Jer [1 ,2 ,5 ]
Tseng, Yuen-Yi [2 ]
Lin, Yi-Chun [2 ]
Tsai, Cheng-Ho [1 ,2 ,3 ]
机构
[1] Mackay Mem Hosp, Taipei 104, Taiwan
[2] Mackay Mem Hosp, Dept Med Res, Taipei 104, Taiwan
[3] Taipei Med Univ, Mackay Jr Coll Nursing, Taipei, Taiwan
[4] Natl Chung Hsing Univ, Dept Vet Med, Taichung 40227, Taiwan
[5] Natl Yang Ming Univ, Inst Tradit Med, Taipei 112, Taiwan
关键词
Connexin43; C-reactive protein; Endothelial cells; Gap junction; Sodium azide; ACTIVATOR INHIBITOR-1 EXPRESSION; IN-VITRO; INTERCELLULAR COMMUNICATION; GENE-EXPRESSION; CELLS; DYSFUNCTION; ATHEROTHROMBOSIS; RELEASE; PATHWAY; ALPHA;
D O I
10.1007/s10565-009-9125-y
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
We investigated the effect of C-reactive protein (CRP) and sodium azide (NaN3) on endothelial Cx43 gap junctions. Human aortic endothelial cells (HAEC) were treated with (a) detoxified CRP, (b) detoxified dialyzed CRP, (c) detoxified dialyzed CRP plus NaN3, (d) NaN3, or (e) dialyzed NaN3. The concentration of CRP in all preparations was fixed to 25 mu g/ml and that of NaN3 in the preparations of (c) to (e) was equivalent to that contained in the 25 mu g/ml CRP purchased commercially. The results showed that both the expression of Cx43 protein and gap junctional communication function post-48-h incubation were reduced and inhibited by the detoxified CRP, NaN3, or detoxified dialyzed CRP plus NaN3, but not by the detoxified dialyzed CRP or dialyzed NaN3. Reverse transcription-polymerase chain reaction analysis of cells treated for 72 h also showed a pattern of transcriptional regulation essentially the same as that for the proteins. We concluded that CRP does not have a significant effect on Cx43 gap junctions of HAEC, but NaN3 inhibited the viability of cells and downregulate their junctions.
引用
收藏
页码:153 / 163
页数:11
相关论文
共 50 条
  • [1] C-reactive protein, sodium azide, and endothelial connexin43 gap junctions
    Hsueh-Hsiao Wang
    Hung-I Yeh
    Chi-Young Wang
    Cheng-Huang Su
    Yih-Jer Wu
    Yuen-Yi Tseng
    Yi-Chun Lin
    Cheng-Ho Tsai
    Cell Biology and Toxicology, 2010, 26 : 153 - 163
  • [2] Protein kinase C-dependent regulation of connexin43 gap junctions and hemichannels
    Alstrom, Jette Skov
    Stroemlund, Line Waring
    Nielsen, Morten Schak
    MacAulay, Nanna
    BIOCHEMICAL SOCIETY TRANSACTIONS, 2015, 43 : 519 - 523
  • [3] Connexin43 Gap Junctions and the Control of Skeletal Remodeling
    Stains, Joseph P.
    FASEB JOURNAL, 2019, 33
  • [4] AGE-BSA down-regulates endothelial connexin43 gap junctions
    Chi-Young Wang
    Hung-Jen Liu
    Heng-Ju Chen
    Yi-Chun Lin
    Hsueh-Hsiao Wang
    Ta-Chuan Hung
    Hung-I Yeh
    BMC Cell Biology, 12
  • [5] AGE-BSA down-regulates endothelial connexin43 gap junctions
    Wang, Chi-Young
    Liu, Hung-Jen
    Chen, Heng-Ju
    Lin, Yi-Chun
    Wang, Hsueh-Hsiao
    Hung, Ta-Chuan
    Yeh, Hung-I
    BMC CELL BIOLOGY, 2011, 12
  • [6] Connexin43 and Bergmann glial gap junctions in cerebellar function
    Tanaka, Mika
    Yamaguchi, Kazuhiko
    Tatsukawa, Tetsuya
    Theis, Martin
    Willecke, Klaus
    Itohara, Shigeyoshi
    FRONTIERS IN NEUROSCIENCE, 2008, 2 (01): : 225 - 233
  • [7] Endocytic processing of connexin43 gap junctions: a morphological study
    Leithe, E
    Brech, A
    Rivedal, E
    BIOCHEMICAL JOURNAL, 2006, 393 : 59 - 67
  • [8] Intercellular permeability and electrical conductance of connexin43 gap junctions
    Ek-Vitorin, JF
    Burt, JM
    MOLECULAR BIOLOGY OF THE CELL, 2002, 13 : 351A - 351A
  • [9] Beyond gap junctions: Connexin43 and bone cell signaling
    Plotkin, Lilian I.
    Bellido, Teresita
    BONE, 2013, 52 (01) : 157 - 166
  • [10] Connexin43 gap junctions exhibit asymmetrical gating properties
    Banach, K
    Weingart, R
    PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY, 1996, 431 (05): : 775 - 785