Targeting Heat Shock Protein 27 in Cancer: A Druggable Target for Cancer Treatment?
Identifieur interne : 000896 ( Pmc/Curation ); précédent : 000895; suivant : 000897Targeting Heat Shock Protein 27 in Cancer: A Druggable Target for Cancer Treatment?
Auteurs : Seul-Ki Choi ; Heejin Kam ; Kye-Young Kim ; Suk In Park ; Yun-Sil LeeSource :
- Cancers [ 2072-6694 ] ; 2019.
Abstract
Heat shock protein 27 (HSP27), induced by heat shock, environmental, and pathophysiological stressors, is a multi-functional protein that acts as a protein chaperone and an antioxidant. HSP27 plays a significant role in the inhibition of apoptosis and actin cytoskeletal remodeling. HSP27 is upregulated in many cancers and is associated with a poor prognosis, as well as treatment resistance, whereby cells are protected from therapeutic agents that normally induce apoptosis. This review highlights the most recent findings and role of HSP27 in cancer, as well as the strategies for using HSP27 inhibitors for therapeutic purposes.
Url:
DOI: 10.3390/cancers11081195
PubMed: 31426426
PubMed Central: 6721579
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Targeting Heat Shock Protein 27 in Cancer: A Druggable Target for Cancer Treatment?</title><author><name sortKey="Choi, Seul Ki" sort="Choi, Seul Ki" uniqKey="Choi S" first="Seul-Ki" last="Choi">Seul-Ki Choi</name></author><author><name sortKey="Kam, Heejin" sort="Kam, Heejin" uniqKey="Kam H" first="Heejin" last="Kam">Heejin Kam</name></author><author><name sortKey="Kim, Kye Young" sort="Kim, Kye Young" uniqKey="Kim K" first="Kye-Young" last="Kim">Kye-Young Kim</name></author><author><name sortKey="Park, Suk In" sort="Park, Suk In" uniqKey="Park S" first="Suk In" last="Park">Suk In Park</name></author><author><name sortKey="Lee, Yun Sil" sort="Lee, Yun Sil" uniqKey="Lee Y" first="Yun-Sil" last="Lee">Yun-Sil Lee</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">31426426</idno><idno type="pmc">6721579</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6721579</idno><idno type="RBID">PMC:6721579</idno><idno type="doi">10.3390/cancers11081195</idno><date when="2019">2019</date><idno type="wicri:Area/Pmc/Corpus">000896</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000896</idno><idno type="wicri:Area/Pmc/Curation">000896</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000896</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Targeting Heat Shock Protein 27 in Cancer: A Druggable Target for Cancer Treatment?</title><author><name sortKey="Choi, Seul Ki" sort="Choi, Seul Ki" uniqKey="Choi S" first="Seul-Ki" last="Choi">Seul-Ki Choi</name></author><author><name sortKey="Kam, Heejin" sort="Kam, Heejin" uniqKey="Kam H" first="Heejin" last="Kam">Heejin Kam</name></author><author><name sortKey="Kim, Kye Young" sort="Kim, Kye Young" uniqKey="Kim K" first="Kye-Young" last="Kim">Kye-Young Kim</name></author><author><name sortKey="Park, Suk In" sort="Park, Suk In" uniqKey="Park S" first="Suk In" last="Park">Suk In Park</name></author><author><name sortKey="Lee, Yun Sil" sort="Lee, Yun Sil" uniqKey="Lee Y" first="Yun-Sil" last="Lee">Yun-Sil Lee</name></author></analytic><series><title level="j">Cancers</title><idno type="eISSN">2072-6694</idno><imprint><date when="2019">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Heat shock protein 27 (HSP27), induced by heat shock, environmental, and pathophysiological stressors, is a multi-functional protein that acts as a protein chaperone and an antioxidant. HSP27 plays a significant role in the inhibition of apoptosis and actin cytoskeletal remodeling. HSP27 is upregulated in many cancers and is associated with a poor prognosis, as well as treatment resistance, whereby cells are protected from therapeutic agents that normally induce apoptosis. This review highlights the most recent findings and role of HSP27 in cancer, as well as the strategies for using HSP27 inhibitors for therapeutic purposes.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Katsogiannou, M" uniqKey="Katsogiannou M">M. Katsogiannou</name></author><author><name sortKey="Andrieu, C" uniqKey="Andrieu C">C. Andrieu</name></author><author><name sortKey="Baylot, V" uniqKey="Baylot V">V. Baylot</name></author><author><name sortKey="Baudot, A" uniqKey="Baudot A">A. Baudot</name></author><author><name sortKey="Dusetti, N J" uniqKey="Dusetti N">N.J. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Cancers (Basel)</journal-id><journal-id journal-id-type="iso-abbrev">Cancers (Basel)</journal-id><journal-id journal-id-type="publisher-id">cancers</journal-id><journal-title-group><journal-title>Cancers</journal-title></journal-title-group><issn pub-type="epub">2072-6694</issn><publisher><publisher-name>MDPI</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">31426426</article-id><article-id pub-id-type="pmc">6721579</article-id><article-id pub-id-type="doi">10.3390/cancers11081195</article-id><article-id pub-id-type="publisher-id">cancers-11-01195</article-id><article-categories><subj-group subj-group-type="heading"><subject>Review</subject></subj-group></article-categories><title-group><article-title>Targeting Heat Shock Protein 27 in Cancer: A Druggable Target for Cancer Treatment?</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Choi</surname><given-names>Seul-Ki</given-names></name></contrib><contrib contrib-type="author"><name><surname>Kam</surname><given-names>Heejin</given-names></name></contrib><contrib contrib-type="author"><name><surname>Kim</surname><given-names>Kye-Young</given-names></name></contrib><contrib contrib-type="author"><name><surname>Park</surname><given-names>Suk In</given-names></name></contrib><contrib contrib-type="author"><contrib-id contrib-id-type="orcid" authenticated="true">https://orcid.org/0000-0002-7538-8850</contrib-id><name><surname>Lee</surname><given-names>Yun-Sil</given-names></name><xref rid="c1-cancers-11-01195" ref-type="corresp">*</xref></contrib></contrib-group><aff id="af1-cancers-11-01195">Graduate School of Pharmaceutical Sciences, College of Pharmacy, Ewha Womans University, Seoul 03760, Korea</aff><author-notes><corresp id="c1-cancers-11-01195"><label>*</label>Correspondence: <email>yslee0425@ewha.ac.kr</email></corresp></author-notes><pub-date pub-type="epub"><day>16</day><month>8</month><year>2019</year></pub-date><pub-date pub-type="collection"><month>8</month><year>2019</year></pub-date><volume>11</volume><issue>8</issue><elocation-id>1195</elocation-id><history><date date-type="received"><day>03</day><month>7</month><year>2019</year></date><date date-type="accepted"><day>07</day><month>8</month><year>2019</year></date></history><permissions><copyright-statement>© 2019 by the authors.</copyright-statement><copyright-year>2019</copyright-year><license license-type="open-access"><license-p>Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/4.0/">http://creativecommons.org/licenses/by/4.0/</ext-link>).</license-p></license></permissions><abstract><p>Heat shock protein 27 (HSP27), induced by heat shock, environmental, and pathophysiological stressors, is a multi-functional protein that acts as a protein chaperone and an antioxidant. HSP27 plays a significant role in the inhibition of apoptosis and actin cytoskeletal remodeling. HSP27 is upregulated in many cancers and is associated with a poor prognosis, as well as treatment resistance, whereby cells are protected from therapeutic agents that normally induce apoptosis. This review highlights the most recent findings and role of HSP27 in cancer, as well as the strategies for using HSP27 inhibitors for therapeutic purposes.</p></abstract><kwd-group><kwd>heat shock protein 27</kwd><kwd>HSP27 inhibitor</kwd><kwd>anti-cancer drugs</kwd><kwd>resistance</kwd></kwd-group></article-meta></front><floats-group><fig id="cancers-11-01195-f001" orientation="portrait" position="float"><label>Figure 1</label><caption><p>Major roles of heat shock protein 27 (HSP27). HSP27 has important functions, including protein folding regulation by chaperone activity, immune response, cancer promotion, inducing resistance to anticancer drugs, aging, biomarkers of several diseases, aggravation of neurodegenerative disease, development, and differentiation [<xref rid="B5-cancers-11-01195" ref-type="bibr">5</xref>,<xref rid="B6-cancers-11-01195" ref-type="bibr">6</xref>,<xref rid="B7-cancers-11-01195" ref-type="bibr">7</xref>,<xref rid="B8-cancers-11-01195" ref-type="bibr">8</xref>].</p></caption><graphic xlink:href="cancers-11-01195-g001"></graphic></fig><fig id="cancers-11-01195-f002" orientation="portrait" position="float"><label>Figure 2</label><caption><p>The structure of heat shock protein 27 (HSP27). The structure of human HSP27 consists of the N-terminal domain, the α-crystallin domain, and the C-terminal domain. The N-terminal domain contains a WDPF motif which is essential for large oligomerization. The C-terminal domain includes an α-crystallin motif that is highly conserved between species and is involved in the formation of small oligomerization. HSP27 phosphorylation sites S15, S78, S82, and T143 are indicated. S15 can be phosphorylated by p38 mitogen-activated protein kinase (MAPK)-activated protein kinase 2 (MK2) and 3 (MK3), and protein kinase C (PKC). S78 can be phosphorylated by MK2, MK3, ribosomal S6 kinase (p70RSK), PKC, and protein kinase G (PKG). S82 can be phosphorylated by MK2, MK3, p70RSK, protein kinase B (PKB), protein kinase D (PKD), and PKG. T143 can be phosphorylated by PKG.</p></caption><graphic xlink:href="cancers-11-01195-g002"></graphic></fig><fig id="cancers-11-01195-f003" orientation="portrait" position="float"><label>Figure 3</label><caption><p>Phosphorylation induced conformational structural switching between different states. Heat shock protein 27 (HSP27) exists as large oligomers when unphosphorylated. At specific serine residues in the mitogen-activated protein kinase (MAPK) pathway, HSP27 switches to smaller oligomers. HSP27 conformational structure changes actively and contributes to maintaining proteostasis.</p></caption><graphic xlink:href="cancers-11-01195-g003"></graphic></fig><fig id="cancers-11-01195-f004" orientation="portrait" position="float"><label>Figure 4</label><caption><p>Role of heat shock protein 27 (HSP27) in different cellular apoptotic processes. HSP27 inhibits apoptosis by integrating with different signaling pathways, including the extrinsic and intrinsic apoptosis pathway. HSP27 inhibits Bcl-2-associated X protein (BAX) by directly binding to death domain associated protein (DAXX) or apoptosis signal-regulating kinase-1 (Ask-1) to inhibit its function, which enhances AKT activity inhibiting BH3 interacting-domain death agonist (BID) or protein kinase C delta type (PKC δ) function. HSP27 inhibits caspase 3, which directly functions in cellular apoptosis. HSP27 contributes to cell survival.</p></caption><graphic xlink:href="cancers-11-01195-g004"></graphic></fig><fig id="cancers-11-01195-f005" orientation="portrait" position="float"><label>Figure 5</label><caption><p>Kaplan–Meier (KM) curves for <italic>HSPB1</italic> (gene name of heat shock protein 27 (HSP27)) in the overall survival of various cancers. Gastric cancer, lung cancer, hepatocellular carcinoma, breast cancer, clear cell renal carcinoma, and rectum adenocarcinoma show high survival rates associated with low HSPB1 expression. <italic>p</italic>-values were calculated using the log-rank test. The Hazard Ratio (HR) is the ratio of the hazard rates corresponding to the conditions described by two levels of an explanatory variable (HR > 1 was considered a higher hazard of death from the <italic>HSPB1</italic>-High group). An independent univariate survival analysis of overall survival (OS) was analyzed based on a merged data set from the Kaplan–Meier Plotter [<xref rid="B76-cancers-11-01195" ref-type="bibr">76</xref>]. Data were derived from <uri xlink:href="http://kmplot.com/analysis/">http://kmplot.com/analysis/</uri> and survival curves were drawn using PRISM software [<xref rid="B77-cancers-11-01195" ref-type="bibr">77</xref>].</p></caption><graphic xlink:href="cancers-11-01195-g005"></graphic></fig><fig id="cancers-11-01195-f006" orientation="portrait" position="float"><label>Figure 6</label><caption><p>Strategies of heat shock protein 27 (HSP27) inhibitors. (<bold>1</bold>) Three small molecule inhibitors (Brivudine (RP101), Quercetin, and cross-linker) bind directly to the HSP27 protein and inhibit the activity of the HSP27 protein. (<bold>2</bold>) Peptide aptamers (PA11 and PA50) bind directly to the HSP27 protein and inhibit oligomerization or dimerization. (<bold>3</bold>) Antisense oligonucleotide (OGX-427) binds to HSP27 mRNA and prevents translation of the HSP27 protein. As a result, the amount of HSP27 protein is reduced.</p></caption><graphic xlink:href="cancers-11-01195-g006"></graphic></fig><fig id="cancers-11-01195-f007" orientation="portrait" position="float"><label>Figure 7</label><caption><p>Altered cross-linking of heat shock protein 27 (HSP27) using small molecules for HSP27 inhibition. Scheme for the mechanism of HSP27-cross-linking by small molecules. Normal dimerization of HSP27 contributes to cancer cell survival, but abnormal dimerization of HSP27 using small molecules causes cancer cell death.</p></caption><graphic xlink:href="cancers-11-01195-g007"></graphic></fig><table-wrap id="cancers-11-01195-t001" orientation="portrait" position="float"><object-id pub-id-type="pii">cancers-11-01195-t001_Table 1</object-id><label>Table 1</label><caption><p>Functions of heat shock protein 27 (HSP27) in various cancer cells (year 2010~).</p></caption><table frame="hsides" rules="groups"><thead><tr><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Cancers</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Effects</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">References</th></tr></thead><tbody><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Liver</td><td align="left" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Promotes proliferation and invasion of hepatocellular carcinoma cells.</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B45-cancers-11-01195" ref-type="bibr">45</xref>,<xref rid="B46-cancers-11-01195" ref-type="bibr">46</xref>]</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Breast</td><td align="left" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Downregulation of HSP27 induces chemo-sensitization to Herceptin and inhibition of cancer cell proliferation.<break></break>HSP27 regulates the EMT process and NFkB activity to contribute to the maintenance of BCSCs.<break></break>Expression of phosphorylated forms of the chaperone <italic>HSPB1</italic> correlates with the amount and percentage of lymph node metastases.<break></break>Down-regulation of HSP27 in human breast cancer cells modulates down-regulation of PTEN.</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B47-cancers-11-01195" ref-type="bibr">47</xref>,<xref rid="B48-cancers-11-01195" ref-type="bibr">48</xref>,<xref rid="B49-cancers-11-01195" ref-type="bibr">49</xref>,<xref rid="B50-cancers-11-01195" ref-type="bibr">50</xref>]</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Colorectal</td><td align="left" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Suppression of HSP27 protein expression enhances 5-FU sensitivity.<break></break>Patients with low HSP27 expression show better survival than those with high HSP27 expression.<break></break>Acquired drug resistance of 5-FU is caused by the enhanced constitutive expression of HSPB1 and its phosphorylated form in colorectal cancer cells.</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B51-cancers-11-01195" ref-type="bibr">51</xref>,<xref rid="B52-cancers-11-01195" ref-type="bibr">52</xref>,<xref rid="B53-cancers-11-01195" ref-type="bibr">53</xref>]</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Melanoma</td><td align="left" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">HSP27 expression is associated with impaired prognosis in melanoma.<break></break>HSP27 is important for tumor dormancy, angiogenesis regulation, and tumor progress in cutaneous melanoma.</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B54-cancers-11-01195" ref-type="bibr">54</xref>,<xref rid="B55-cancers-11-01195" ref-type="bibr">55</xref>]</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Prostate</td><td align="left" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">HSP27 increases PCa cell motility, growth, and survival.<break></break>Downregulation of HSP27 radiosensitizes human prostate cancer cells.<break></break>In patients with prostate cancer, with HSP27 and Twist expression, each is elevated in high-grade prostate cancer tumors.<break></break>DNA methylation of <italic>HSPB1</italic> resulted in a poor outcome in prostate cancer patients.</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B35-cancers-11-01195" ref-type="bibr">35</xref>,<xref rid="B56-cancers-11-01195" ref-type="bibr">56</xref>,<xref rid="B57-cancers-11-01195" ref-type="bibr">57</xref>,<xref rid="B58-cancers-11-01195" ref-type="bibr">58</xref>]</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Glioma</td><td align="left" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Promotes glioma cell proliferation.<break></break>Quantitative proteomic analysis shows that HSP27 is involved in the poor prognosis of GBN.</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B59-cancers-11-01195" ref-type="bibr">59</xref>,<xref rid="B60-cancers-11-01195" ref-type="bibr">60</xref>]</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Lung</td><td align="left" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">HSP27 inhibitor induces chemo-sensitization to anti-cancer drugs.<break></break>Increased HSP27 expression correlates with shorter survival of NSCLC patients.</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B61-cancers-11-01195" ref-type="bibr">61</xref>,<xref rid="B62-cancers-11-01195" ref-type="bibr">62</xref>,<xref rid="B63-cancers-11-01195" ref-type="bibr">63</xref>]</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Gastric</td><td align="left" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Meta-analysis of gastric cancer is strongly dependent on the overexpression of HSP27.</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B64-cancers-11-01195" ref-type="bibr">64</xref>,<xref rid="B65-cancers-11-01195" ref-type="bibr">65</xref>]</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Rectal</td><td align="left" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">High expression of HSP27 represents poor survival in rectal cancer.</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B66-cancers-11-01195" ref-type="bibr">66</xref>]</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Pancreatic</td><td align="left" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Downregulation of HSP27 sensitizes to gemcitabine in the gastric cancer cell line by regulating the expression of Snail.<break></break>HSP27 phosphorylation status contributes to gemcitabine resistance.</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B67-cancers-11-01195" ref-type="bibr">67</xref>,<xref rid="B68-cancers-11-01195" ref-type="bibr">68</xref>]</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Kidney</td><td align="left" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Abnormal HSP27 phosphorylation is observed in renal cancers, as well as in other kidney diseases.<break></break>In ccRCC patients, high serum HSP27 is associated with high-grade (Grade 3–4) tumors.<break></break>TGF-β1/p38/HSP27 signaling pathway inhibits cancer invasion and metastasis in RCC.</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">[<xref rid="B69-cancers-11-01195" ref-type="bibr">69</xref>,<xref rid="B70-cancers-11-01195" ref-type="bibr">70</xref>,<xref rid="B71-cancers-11-01195" ref-type="bibr">71</xref>]</td></tr></tbody></table><table-wrap-foot><fn><p>PTEN, phosphatase and tensin homolog; EMT, epithelial-mesenchymal transition; BCSC, breast cancer stem cell; NFkB, nuclear factor kappa-light-chain-enhancer of activated B cells; 5-FU, fluorouracil; PCa, prostate cancer; NSCLC, non-small cell lung cancer; GBN, glioblastoma; ccRCC, clear cell renal cell carcinoma; RCC, renal cell carcinoma; TGF-β1, transforming growth factor beta.</p></fn></table-wrap-foot></table-wrap><table-wrap id="cancers-11-01195-t002" orientation="portrait" position="float"><object-id pub-id-type="pii">cancers-11-01195-t002_Table 2</object-id><label>Table 2</label><caption><p>Structure and mechanism of action of small-molecule heat shock protein 27 (HSP27) inhibitors.</p></caption><table frame="hsides" rules="groups"><thead><tr><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Name</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Structure</th><th align="center" valign="middle" style="border-top:solid thin;border-bottom:solid thin" rowspan="1" colspan="1">Mechanism</th></tr></thead><tbody><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">RP101</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1"><inline-graphic xlink:href="cancers-11-01195-i001.jpg"></inline-graphic></td><td align="left" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Inhibits HSP27 protein by π-stacking binding to Phe29 and Phe33 of HSP27 [<xref rid="B80-cancers-11-01195" ref-type="bibr">80</xref>].</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Quercetin</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1"><inline-graphic xlink:href="cancers-11-01195-i002.jpg"></inline-graphic></td><td align="left" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">No exact mechanism associated with HSP27.</td></tr><tr><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">J2 (Cross linker)</td><td align="center" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1"><inline-graphic xlink:href="cancers-11-01195-i003.jpg"></inline-graphic></td><td align="left" valign="middle" style="border-bottom:solid thin" rowspan="1" colspan="1">Forms a covalent bond between the cysteine thiol group of HSP27 [<xref rid="B63-cancers-11-01195" ref-type="bibr">63</xref>].</td></tr></tbody></table></table-wrap></floats-group></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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