Heat Shock Proteins: Mediators of Atherosclerotic Development

被引:19
作者
Deniset, Justin F.
Pierce, Grant N. [1 ]
机构
[1] St Boniface Hosp Res Ctr, Inst Cardiovasc Sci, Winnipeg, MB R2H 2A6, Canada
关键词
Atherosclerosis; cardiovascular disease; cell proliferation; heat shock factor; immune; inflammation; VASCULAR SMOOTH-MUSCLE; NITRIC-OXIDE SYNTHASE; TRANSCRIPTIONAL ACTIVATION DOMAIN; OXIDATIVE STRESS; IN-VIVO; MOLECULAR CHAPERONES; CHLAMYDIA-PNEUMONIAE; ENDOTHELIAL-CELLS; DNA-BINDING; HEAT-SHOCK-PROTEIN-60; EXPRESSION;
D O I
10.2174/1389450116666150416115423
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
Heat shock proteins play important housekeeping roles in a variety of cells within the body during normal control conditions. The many different functions for heat shock proteins in the cell depend upon the specific heat shock protein involved. Each protein is nominally differentiated based upon its molecular size. However, in addition to their role in normal cell function, heat shock proteins may play an even more important role as pro-survival proteins conserved through evolution to protect the cell from a variety of stresses. The ability of a cell to withstand these environmental stresses is critical to its capacity to adapt and remain viable. Loss of this ability may lead to pathological states. Abnormal localization, structure or function of the heat shock proteins has been associated with many pathologies, including those involving heart disease. Heat shock proteins like HSP60 and HSP70 in particular have been identified as playing important roles in inflammation and immune reactions. Inflammation has been identified recently as an important pathological risk factor for heart disease. It is perhaps not surprising therefore, that heat shock protein family has been increasingly identified as an important intracellular pathway associated with inflammatory-mediated heart conditions including atherosclerosis. This paper reviews the evidence in support of a role for heat shock proteins in cardiovascular disease and the potential to target these proteins to alter the progression of atherosclerotic disease.
引用
收藏
页码:816 / 826
页数:11
相关论文
共 166 条
  • [1] THE HUMAN HEAT-SHOCK PROTEIN HSP70 INTERACTS WITH HSF, THE TRANSCRIPTION FACTOR THAT REGULATES HEAT-SHOCK GENE-EXPRESSION
    ABRAVAYA, K
    MYERS, MP
    MURPHY, SP
    MORIMOTO, RI
    [J]. GENES & DEVELOPMENT, 1992, 6 (07) : 1153 - 1164
  • [2] HSP90 interacts with and regulates the activity of heat shock factor 1 in Xenopus oocytes
    Ali, A
    Bharadwaj, S
    O'Carroll, R
    Ovsenek, N
    [J]. MOLECULAR AND CELLULAR BIOLOGY, 1998, 18 (09) : 4949 - 4960
  • [3] Autoreactive HSP60 epitope-specific T-cells in early human atherosclerotic lesions
    Almanzar, Giovanni
    Oelinger, Robert
    Leuenberger, Julianna
    Onestingel, Elisabeth
    Rantner, Barbara
    Zehm, Sarah
    Cardini, Benno
    van der Zee, Ruurd
    Grundtman, Cecilia
    Wick, Georg
    [J]. JOURNAL OF AUTOIMMUNITY, 2012, 39 (04) : 441 - 450
  • [4] Anckar J, 2007, ADV EXP MED BIOL, V594, P78
  • [5] Regulation of HSF1 Function in the Heat Stress Response: Implications in Aging and Disease
    Anckar, Julius
    Sistonen, Lea
    [J]. ANNUAL REVIEW OF BIOCHEMISTRY, VOL 80, 2011, 80 : 1089 - 1115
  • [6] Hsp110 is a nucleotide-activated exchange factor for Hsp70
    Andreasson, Claes
    Fiaux, Jocelyne
    Rampelt, Heike
    Mayer, Matthias P.
    Bukau, Bernd
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (14) : 8877 - 8884
  • [7] Prevalence of intimal heat shock protein 60 homologues in unstable angina and correlation with anti-heat shock protein antibody titers
    Andrie, Rene P.
    Bauriedel, Gerhard
    Braun, Peter
    Hoepp, Hans W.
    Nickenig, Georg
    Skowasch, Dirk
    [J]. BASIC RESEARCH IN CARDIOLOGY, 2011, 106 (04) : 657 - 665
  • [8] HEAT-SHOCK GENE-REGULATION BY NASCENT POLYPEPTIDES AND DENATURED PROTEINS - HSP70 AS A POTENTIAL AUTOREGULATORY FACTOR
    BALER, R
    WELCH, WJ
    VOELLMY, R
    [J]. JOURNAL OF CELL BIOLOGY, 1992, 117 (06) : 1151 - 1159
  • [9] The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions
    Basha, E
    Lee, GJ
    Breci, LA
    Hausrath, AC
    Buan, NR
    Giese, KC
    Vierling, E
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (09) : 7566 - 7575
  • [10] Review: Mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones
    Ben-Zvi, AP
    Goloubinoff, P
    [J]. JOURNAL OF STRUCTURAL BIOLOGY, 2001, 135 (02) : 84 - 93