当前位置： SCI文献检索 > JOURNAL OF INORGANIC BIOCHEMISTRY期刊下所有文献 > Assessing the contribution of the two protein disulfide isomerases PDIA1 and PDIA3 to cisplatin resistance.

Assessing the contribution of the two protein disulfide isomerases PDIA1 and PDIA3 to cisplatin resistance.

Abstract：

:Intracellular binding of cisplatin to non-DNA partners, such as proteins, has received increasing attention as an additional mode of action and as mechanism of resistance. We investigated two cisplatin-interacting isoforms of protein disulfide isomerase regarding their contribution to acquired cisplatin resistance using sensitive and resistant A2780/A2780cis ovarian cancer cells. Cisplatin cytotoxicity was assessed after knockdown of either protein disulfide isomerase family A member 1 (PDIA1) or protein disulfide isomerase family A member 3 (PDIA3). Whereas PDIA1 knockdown led to increased cytotoxicity in resistant A2780cis cells, PDIA3 knockdown showed no influence on cytotoxicity. Coincubation with propynoic acid carbamoyl methyl amide 31 (PACMA31), a PDIA1 inhibitor, resensitized A2780cis cells to cisplatin treatment. Determination of the combination index revealed that the combination of cisplatin and PACMA31 acts synergistically. Our results warrant further evaluation of PDIA1 as promising target for chemotherapy, and its inhibition by PACMA31 as a new therapeutic approach.

journal_name

J Inorg Biochem

journal_title

Journal of inorganic biochemistry

authors

Kullmann M,Kalayda GV,Hellwig M,Kotz S,Hilger RA,Metzger S,Jaehde U

doi

10.1016/j.jinorgbio.2015.08.028

subject

Has Abstract

pub_date

2015-12-01 00:00:00

pages

247-252

eissn

0162-0134

issn

1873-3344

pii

S0162-0134(15)30073-8

journal_volume

153

pub_type

杂志文章

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