Abstract：
:Heat shock protein 110 (HSP110) is induced by different stresses and, through its anti-apoptotic and chaperoning properties, helps cells survive these adverse situations. In colon cancers, HSP110 is abnormally abundant. We have recently shown that colorectal cancer patients with microsatellite instability (MSI) had an improved response to chemotherapy because they harbor an HSP110-inactivating mutation (HSP110DE9). In this work, we used patient biopsies, human colorectal cancer cells grown in vitro and in vivo (xenografts), and intestinal crypts to demonstrate that HSP110 is also involved in colon cancer growth. We showed that HSP110 induces colon cancer cell proliferation and that this effect is associated with STAT3 activation, specifically an increase in STAT3 phosphorylation, nuclear translocation and transcription factor activity. STAT3 inhibition blocks the proliferative effect of HSP110. From a molecular standpoint, we demonstrated that HSP110 directly binds to STAT3, thereby facilitating its phosphorylation by JAK2. Finally, we showed a correlation between HSP110 expression and STAT3 phosphorylation in colon cancer patient samples. Thus, the expression of HSP110 in colon cancer contributes to STAT3-dependent tumor growth and the frequent inactivating mutation of this chaperone is probably an important event underlying the improved prognosis in colon cancer displaying MSI.
journal_name
Oncogenejournal_title
Oncogeneauthors
Berthenet K,Bokhari A,Lagrange A,Marcion G,Boudesco C,Causse S,De Thonel A,Svrcek M,Goloudina AR,Dumont S,Hammann A,Biard DS,Demidov ON,Seigneuric R,Duval A,Collura A,Jego G,Garrido Cdoi
10.1038/onc.2016.403subject
Has Abstractpub_date
2017-04-20 00:00:00pages
2328-2336issue
16eissn
0950-9232issn
1476-5594pii
onc2016403journal_volume
36pub_type
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