| Literature DB >> 28322796 |
Yuka Aoyama1, Sayaka Sobue1, Naoki Mizutani1, Chisato Inoue1, Yoshiyuki Kawamoto1, Yuji Nishizawa1, Masatoshi Ichihara1, Mamoru Kyogashima2, Motoshi Suzuki3, Yoshinoti Nozawa4, Takashi Murate5.
Abstract
Taxoids are anti-cancer drugs frequently used to treat solid tumors, but they are sometimes ineffective and tumors may become resistant to their action. Here, we examined the involvement of sphingolipid metabolic enzymes in paclitaxel (PTX) resistance using a human prostate cancer cell line, PC3, and its PTX-resistant subline, PC3-PR. PTX (20 nM) suppressed cell proliferation and increased various ceramide species in PC3, but not PC3-PR, cells. PC3-PR contained higher S1P levels than did PC3, regardless of PTX treatment. Western blotting revealed that PC3-PR cells expressed higher levels of sphingosine kinase 1 (SPHK1) and glucosylceramide synthase (GCS) but lower levels of acid sphingomyelinase (ASMase) and neutral sphingomyelinase 2 than did PC3 cells. Inhibition of SPHK1 using siRNA or a pharmacological inhibitor decreased S1P levels in PC3-PR cells and inhibited proliferation in the presence or absence of PTX, suggesting that SPHK1 is at least partially responsible for PTX resistance. Similarly, GCS inhibitors (PDMP and PPMP) increased cellular ceramides and suppressed the proliferation of PC3-PR. However, inhibition of proteasome function or histone deacetylase activity increased SMase and ceramide levels and suppressed PC3-PR proliferation. These results suggest that modulation of metabolic enzyme expression and alteration of the sphingolipid rheostat protects cancer cells against PTX.Entities:
Keywords: Glucosylceramide synthase; Human prostate cancer cell line; Paclitaxel resistance; SPHK1; Sphingolipid rheostat; Sphingomyelinase
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Year: 2017 PMID: 28322796 DOI: 10.1016/j.bbrc.2017.03.084
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575