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2016 ; 11
(9
): e0162698
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SPARC Regulates Transforming Growth Factor Beta Induced (TGFBI) Extracellular
Matrix Deposition and Paclitaxel Response in Ovarian Cancer Cells
#MMPMID27622658
Tumbarello DA
; Andrews MR
; Brenton JD
PLoS One
2016[]; 11
(9
): e0162698
PMID27622658
show ga
TGFBI has been shown to sensitize ovarian cancer cells to the cytotoxic effects
of paclitaxel via an integrin receptor-mediated mechanism that modulates
microtubule stability. Herein, we determine that TGFBI localizes within organized
fibrillar structures in mesothelial-derived ECM. We determined that suppression
of SPARC expression by shRNA decreased the deposition of TGFBI in
mesothelial-derived ECM, without affecting its overall protein expression or
secretion. Conversely, overexpression of SPARC increased TGFBI deposition. A
SPARC-YFP fusion construct expressed by the Met5a cell line co-localized with
TGFBI in the cell-derived ECM. Interestingly, in vitro produced SPARC was capable
of precipitating TGFBI from cell lysates dependent on an intact SPARC
carboxy-terminus with in vitro binding assays verifying a direct interaction. The
last 37 amino acids of SPARC were shown to be required for the TGFBI interaction
while expression of a SPARC-YFP construct lacking this region (aa 1-256) did not
interact and co-localize with TGFBI in the ECM. Furthermore, ovarian cancer cells
have a reduced motility and decreased response to the chemotherapeutic agent
paclitaxel when plated on ECM derived from mesothelial cells lacking SPARC
compared to control mesothelial-derived ECM. In conclusion, SPARC regulates the
fibrillar ECM deposition of TGFBI through a novel interaction, subsequently
influencing cancer cell behavior.
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