Difference between revisions of "Heat shock proteins"

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<h3>Chaperone-dependent  autophagy</h3>
 
<h3>Chaperone-dependent  autophagy</h3>
<div class="links"> </div>
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<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/17404494">PMID: 17404494</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/16874031">PMID: 16874031</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/20694452">PMID: 20694452</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/20060297">PMID: 20060297</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/20570967">PMID: 20570967</a><br /></div>
 
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</div>(...)<!--Pop-up for: DNA repair !Pop-up-->
 
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<h3>DNA repair</h3>
 
<h3>DNA repair</h3>
<div class="links"> </div>
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<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/14627201">PMID: 14627201</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/11579749">PMID: 11579749</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/11518492">PMID: 11518492</a><br /></div>
 
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<h3>MST-1</h3>
 
<h3>MST-1</h3>
<div class="links"> </div>
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<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/12384512">PMID: 12384512</a><br /></div>
 
</div>(...)<!--Pop-up for: Glycated proteins !Pop-up-->
 
</div>(...)<!--Pop-up for: Glycated proteins !Pop-up-->
 
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<h3>Glycated proteins</h3>
 
<h3>Glycated proteins</h3>
<div class="links"> </div>
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<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11744333">PMID: 11744333</a><br /></div>
 
</div>(...)<!--Pop-up for: necrosis !Pop-up-->
 
</div>(...)<!--Pop-up for: necrosis !Pop-up-->
 
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<h3>necrosis</h3>
 
<h3>necrosis</h3>
<div class="links"> </div>
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<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11058573">PMID: 11058573</a><br /></div>
 
</div>(...)<!--Pop-up for: Heat shock proteins  (HSP100, HSP90, HSP70, HSP60, HSP40, small HSPs) !Pop-up-->
 
</div>(...)<!--Pop-up for: Heat shock proteins  (HSP100, HSP90, HSP70, HSP60, HSP40, small HSPs) !Pop-up-->
 
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<h3>Heat shock proteins  (HSP100, HSP90, HSP70, HSP60, HSP40, small HSPs)</h3>
 
<h3>Heat shock proteins  (HSP100, HSP90, HSP70, HSP60, HSP40, small HSPs)</h3>
<div class="links"> </div>
+
<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/2427013">PMID: 2427013</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/18432918">PMID: 18432918</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/11226747">PMID: 11226747</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/12750521">PMID: 12750521</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/17525527">PMID: 17525527</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/11530097">PMID: 11530097</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/17584980">PMID: 17584980</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/17038477">PMID: 17038477</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/16483782">PMID: 16483782</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/19546513">PMID: 19546513</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/12575825">PMID: 12575825</a><br /></div>
 
</div>(...)<!--Pop-up for: Heat shock !Pop-up-->
 
</div>(...)<!--Pop-up for: Heat shock !Pop-up-->
 
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<h3>Heat shock</h3>
 
<h3>Heat shock</h3>
<div class="links"> </div>
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<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/8451637">PMID: 8451637</a><br /></div>
 
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</div>(...)<!--Pop-up for: Mature protein with  unstable or improper  conformation !Pop-up-->
 
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<h3>Mature protein with  unstable or improper  conformation</h3>
 
<h3>Mature protein with  unstable or improper  conformation</h3>
<div class="links"> </div>
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<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/14685250">PMID: 14685250</a><br /></div>
 
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</div>(...)<!--Pop-up for: Regulation of proliferation  and differentiation of cells !Pop-up-->
 
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<h3>Regulation of proliferation  and differentiation of cells</h3>
 
<h3>Regulation of proliferation  and differentiation of cells</h3>
<div class="links"> </div>
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<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/14986858">PMID: 14986858</a><br /></div>
 
</div>(...)<!--Pop-up for: Expression of heat  shock proteins genes !Pop-up-->
 
</div>(...)<!--Pop-up for: Expression of heat  shock proteins genes !Pop-up-->
 
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<h3>Expression of heat  shock proteins genes</h3>
 
<h3>Expression of heat  shock proteins genes</h3>
<div class="links"> </div>
+
<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11839944">PMID: 11839944</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/11123263">PMID: 11123263</a><br /></div>
 
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<h3>Signal transduction</h3>
 
<h3>Signal transduction</h3>
<div class="links"> </div>
+
<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11457815">PMID: 11457815</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/11836257">PMID: 11836257</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/14686091">PMID: 14686091</a><br /></div>
 
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<h3>SIRT-1</h3>
 
<h3>SIRT-1</h3>
<div class="links"> </div>
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<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/19229036">PMID: 19229036</a><br /></div>
 
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</div>(...)<!--Pop-up for: Protein refolding !Pop-up-->
 
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<h3>Protein refolding</h3>
 
<h3>Protein refolding</h3>
<div class="links"> </div>
+
<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11580258">PMID: 11580258</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/10631262">PMID: 10631262</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/12475174">PMID: 12475174</a><br /></div>
 
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</div>(...)<!--Pop-up for: Posttranslational translocation of proteins  in endoplasmic reticulum and mitochondria !Pop-up-->
 
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<h3>Posttranslational translocation of proteins  in endoplasmic reticulum and mitochondria</h3>
 
<h3>Posttranslational translocation of proteins  in endoplasmic reticulum and mitochondria</h3>
<div class="links"> </div>
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<div class="links"><a href=" ">Posttranslational translocation of proteins  in endoplasmic reticulum and mitochondria</a><br /></div>
 
</div>(...)<!--Pop-up for: Nuclear import / export !Pop-up-->
 
</div>(...)<!--Pop-up for: Nuclear import / export !Pop-up-->
 
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<h3>Nuclear import / export</h3>
 
<h3>Nuclear import / export</h3>
<div class="links"> </div>
+
<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/14684748">PMID: 14684748</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/14555980">PMID: 14555980</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/16203861">PMID: 16203861</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/10805742">PMID: 10805742</a><br /></div>
 
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</div>(...)<!--Pop-up for: protein aggregates !Pop-up-->
 
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<h3>protein aggregates</h3>
 
<h3>protein aggregates</h3>
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<div class="links"></div>
 
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<h3>JNK</h3>
 
<h3>JNK</h3>
<div class="links"> </div>
+
<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11752668">PMID: 11752668</a><br /></div>
 
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</div>(...)<!--Pop-up for: HSF-1 !Pop-up-->
 
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<h3>HSF-1</h3>
 
<h3>HSF-1</h3>
<div class="links"> </div>
+
<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11839944">PMID: 11839944</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/12750521">PMID: 12750521</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/11123263">PMID: 11123263</a><br /></div>
 
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</div>(...)<!--Pop-up for: Free radicals !Pop-up-->
 
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<h3>Free radicals</h3>
 
<h3>Free radicals</h3>
<div class="links"> </div>
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<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11579749">PMID: 11579749</a><br /></div>
 
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</div>(...)<!--Pop-up for: Fever  !Pop-up-->
 
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<h3>Fever </h3>
 
<h3>Fever </h3>
<div class="links"> </div>
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<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11913069">PMID: 11913069</a><br /></div>
 
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</div>(...)<!--Pop-up for: immunity !Pop-up-->
 
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<h3>immunity</h3>
 
<h3>immunity</h3>
<div class="links"> </div>
+
<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11790532">PMID: 11790532</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/11913069">PMID: 11913069</a><br /></div>
 
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</div>(...)<!--Pop-up for: Protein aggregates !Pop-up-->
 
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<h3>Protein aggregates</h3>
 
<h3>Protein aggregates</h3>
<div class="links"> </div>
+
<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/14617181">PMID: 14617181</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/14663482">PMID: 14663482</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/21045566">PMID: 21045566</a><br /></div>
 
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</div>(...)<!--Pop-up for: Assembly of  active telomerase !Pop-up-->
 
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<h3>Assembly of  active telomerase</h3>
 
<h3>Assembly of  active telomerase</h3>
<div class="links"> </div>
+
<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11274138">PMID: 11274138</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/16714764">PMID: 16714764</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/11406554">PMID: 11406554</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/12135483">PMID: 12135483</a><br /></div>
 
</div>(...)<!--Pop-up for: Immature newly  synthesized proteins !Pop-up-->
 
</div>(...)<!--Pop-up for: Immature newly  synthesized proteins !Pop-up-->
 
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<h3>Immature newly  synthesized proteins</h3>
 
<h3>Immature newly  synthesized proteins</h3>
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</div>(...)<!--Pop-up for: Proteasomal degradation  of damaged proteins !Pop-up-->
 
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<h3>Proteasomal degradation  of damaged proteins</h3>
 
<h3>Proteasomal degradation  of damaged proteins</h3>
<div class="links"> </div>
+
<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11359866">PMID: 11359866</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/12039443">PMID: 12039443</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/20694452">PMID: 20694452</a><br /></div>
 
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</div>(...)<!--Pop-up for: inflammation !Pop-up-->
 
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<h3>inflammation</h3>
 
<h3>inflammation</h3>
<div class="links"> </div>
+
<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11864840">PMID: 11864840</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/11864934">PMID: 11864934</a><br /></div>
 
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</div>(...)<!--Pop-up for: FOXO !Pop-up-->
 
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<h3>FOXO</h3>
 
<h3>FOXO</h3>
<div class="links"> </div>
+
<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/15784720">PMID: 15784720</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/14976264">PMID: 14976264</a><br /></div>
 
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</div>(...)<!--Pop-up for: Inhibitors of energy  metabolism !Pop-up-->
 
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<h3>Inhibitors of energy  metabolism</h3>
 
<h3>Inhibitors of energy  metabolism</h3>
<div class="links"> </div>
+
<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11145923">PMID: 11145923</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/15516594">PMID: 15516594</a><br /></div>
 
</div>(...)<!--Pop-up for: Intracellular stress !Pop-up-->
 
</div>(...)<!--Pop-up for: Intracellular stress !Pop-up-->
 
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<h3>Intracellular stress</h3>
 
<h3>Intracellular stress</h3>
<div class="links"> </div>
+
<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/15169835">PMID: 15169835</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/16610360">PMID: 16610360</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/22371371">PMID: 22371371</a><br /></div>
 
</div>(...)<!--Pop-up for: Maintaining stable  functional conformation of proteins !Pop-up-->
 
</div>(...)<!--Pop-up for: Maintaining stable  functional conformation of proteins !Pop-up-->
 
<div class="1HXDPJWX4-1V78X3P-101" style="display:none;">
 
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<h3>Maintaining stable  functional conformation of proteins</h3>
 
<h3>Maintaining stable  functional conformation of proteins</h3>
<div class="links"> </div>
+
<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/16076838">PMID: 16076838</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/11146277">PMID: 11146277</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/11839944">PMID: 11839944</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/11018092">PMID: 11018092</a><br /></div>
 
</div>(...)<!--Pop-up for: Denatured proteins !Pop-up-->
 
</div>(...)<!--Pop-up for: Denatured proteins !Pop-up-->
 
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<h3>Denatured proteins</h3>
 
<h3>Denatured proteins</h3>
<div class="links"> </div>
+
<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11960972">PMID: 11960972</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/14685250">PMID: 14685250</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/10631262">PMID: 10631262</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/17544402">PMID: 17544402</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/22371371">PMID: 22371371</a><br /></div>
 
</div>(...)<!--Pop-up for: oxidized proteins !Pop-up-->
 
</div>(...)<!--Pop-up for: oxidized proteins !Pop-up-->
 
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<h3>oxidized proteins</h3>
 
<h3>oxidized proteins</h3>
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<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11839944">PMID: 11839944</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/19248813">PMID: 19248813</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/11359866">PMID: 11359866</a><br /></div>
 
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<h3>Heavy metals</h3>
 
<h3>Heavy metals</h3>
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<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11741035">PMID: 11741035</a><br /></div>
 
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<h3>apoptosis</h3>
 
<h3>apoptosis</h3>
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<div class="links"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11511077">PMID: 11511077</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/16610360">PMID: 16610360</a><br /><a href="http://www.ncbi.nlm.nih.gov/pubmed/14663482">PMID: 14663482</a><br /></div>
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</div>(.//.)<h1>Heat shock proteins</h1>
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<p>Heat-shock proteins (HSPs), or stress proteins, are present in all organisms and in all cells of all organisms. They are highly conserved across species. Selected HSPs, also known as chaperones, play crucial roles in folding/unfolding of proteins, assembly of multiprotein complexes, transport/sorting of proteins into correct subcellular compartments, cell-cycle control and signaling, and protection of cells against stress/apoptosis. More recently, HSPs have been implicated in antigen presentation with the role of chaperoning and transferring antigenic peptides to the class I and class II molecules of the major histocompatibility complexes. In addition, extracellular HSPs can stimulate professional antigen-presenting cells of the immune system, such as macrophages and dendritic cells. </p>
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<p>Mammalian HSPs have been classified into four major families according to their molecular size: HSP100, HSP90, HSP70, HSP60, HSP40 and the small HSPs. Each family of HSPs is composed of members expressed either constitutively or regulated inducibly, and/or targeted to different sub-cellular compartments. For example HSP60, HSC70 or HSP90 are constitutively expressed in mammalian cells while others, HSP27 and HSP70, are strongly induced by different stresses, such as heat, oxidative stress, or anticancer drugs. Recently, it has been recognized that HSPs also regulate apoptosis. HSP27 and HSP70 are antiapoptotic, while HSP60 and HSP10 are proapoptotic. </p>
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<p>The transcription factor HSF1 initiates the prolific induction of HSP when cells are exposed to protein damage. Increased protein damage during aging may be exacerbated by a declining heat shock response, reduced levels of heat shock proteins (HSPs), and the resultant loss of protein quality control. Age-dependent waning of the heat shock response is a general effect found in neuronal tissues, skeletal and cardiac muscle and liver. Cells lose the capacity to activate the transcriptional pathways leading to HSP synthesis. In neuronal tissues, decline in protein quality control was widely predicted, as the etiology of a number of diseases involve aggregation-prone proteins that form inclusion bodies whose occurrence is linked to pathology. These diseases include the most frequent neurodegenerative disorder, Alzheimer's disease, an ailment whose pathological symptoms are linked to accumulation of at least two types of inclusion formed from aggregation of the amyloid-β peptide and the cytoskeletal protein tau.</p>(.//.)<!-- Do not edit!  -->
 
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Revision as of 15:17, 17 June 2015

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

Heat shock proteins

Heat-shock proteins (HSPs), or stress proteins, are present in all organisms and in all cells of all organisms. They are highly conserved across species. Selected HSPs, also known as chaperones, play crucial roles in folding/unfolding of proteins, assembly of multiprotein complexes, transport/sorting of proteins into correct subcellular compartments, cell-cycle control and signaling, and protection of cells against stress/apoptosis. More recently, HSPs have been implicated in antigen presentation with the role of chaperoning and transferring antigenic peptides to the class I and class II molecules of the major histocompatibility complexes. In addition, extracellular HSPs can stimulate professional antigen-presenting cells of the immune system, such as macrophages and dendritic cells.

Mammalian HSPs have been classified into four major families according to their molecular size: HSP100, HSP90, HSP70, HSP60, HSP40 and the small HSPs. Each family of HSPs is composed of members expressed either constitutively or regulated inducibly, and/or targeted to different sub-cellular compartments. For example HSP60, HSC70 or HSP90 are constitutively expressed in mammalian cells while others, HSP27 and HSP70, are strongly induced by different stresses, such as heat, oxidative stress, or anticancer drugs. Recently, it has been recognized that HSPs also regulate apoptosis. HSP27 and HSP70 are antiapoptotic, while HSP60 and HSP10 are proapoptotic.

The transcription factor HSF1 initiates the prolific induction of HSP when cells are exposed to protein damage. Increased protein damage during aging may be exacerbated by a declining heat shock response, reduced levels of heat shock proteins (HSPs), and the resultant loss of protein quality control. Age-dependent waning of the heat shock response is a general effect found in neuronal tissues, skeletal and cardiac muscle and liver. Cells lose the capacity to activate the transcriptional pathways leading to HSP synthesis. In neuronal tissues, decline in protein quality control was widely predicted, as the etiology of a number of diseases involve aggregation-prone proteins that form inclusion bodies whose occurrence is linked to pathology. These diseases include the most frequent neurodegenerative disorder, Alzheimer's disease, an ailment whose pathological symptoms are linked to accumulation of at least two types of inclusion formed from aggregation of the amyloid-β peptide and the cytoskeletal protein tau.