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2‐D DIGE ‐LC/MS/MS analysis of proteins which interact with heat shock factor 1 in liver during sepsis
Author(s) -
Jao HsiaoChing,
Lai YunWei
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.lb100
Subject(s) - hsf1 , heat shock protein , sepsis , hsp70 , heat shock factor , protein subunit , hsp60 , biology , microbiology and biotechnology , heat shock , chemistry , biochemistry , immunology , gene
Heat shock factor 1 (HSF1) is the major transcriptional factor for heat shock proteins. In sepsis animal model, there was much higher mortality rate in HSF1 knock out animals. HSF1 does play an important survival role in sepsis. Via experimental sepsis model by cecum ligation and puncture (CLP), there was increased HSF1 expression in nuclear fraction of hepatocytes during early sepsis, and decreased during late sepsis. In respecto of protein‐protein interaction with HSF1, nuclear proteins were immunoprecipitated with anti‐HSF1 antibody and analyzed by 2‐D difference gel electrophoresis (DIGE). There were 23 proteins dots revealed by Decyder BVA with significant changes in sepsis. 7 protein dots of them have been identified by LC/MS/MS, including protein dots 267 (grp75), protein dots363 (HSP60), protein dots 417 (ATPase F1 alpha subunit), protein dots 435 (Lipoamide acyltransferase component of branched‐chain alpha‐deto acid dehydrogenase complex), protein dots 572 (Purine‐rich single‐stranded DNA‐binding protein alpha isoform 1), protein dots 621 (2‐oxoisovalerate dehydrogenase beta subunit) and protein dots 651 (peroxisomal trans‐2‐enoyl‐CoA reductase). These proteins interacted with HSF1 may participate in heat shock protective mechanism during sepsis.