Heat Shock Pretreatment Influences the Expression of PKC Isoforms during Sepsis

2001 ◽  
Vol 101 (2) ◽  
pp. 202-209 ◽  
Author(s):  
Hsiang-Wen Chen ◽  
Chin Hsu ◽  
Hseng-Kuang Hsu ◽  
Tzong-Shi Lu ◽  
Shu-Jung Wang ◽  
...  
2000 ◽  
Vol 5 (3) ◽  
pp. 188 ◽  
Author(s):  
Hsiang-Wen Chen ◽  
Chin Hsu ◽  
Sheng-I Lue ◽  
Rei-Cheng Yang

2003 ◽  
Vol 12 (5) ◽  
pp. 1165-1177 ◽  
Author(s):  
Karen D. Williams ◽  
Amanda B. Helin ◽  
Joseph Posluszny ◽  
Stephen P. Roberts ◽  
Martin E. Feder

2013 ◽  
Vol 26 (4) ◽  
pp. 365-373 ◽  
Author(s):  
San-Qiang Li ◽  
Dong-Mei Wang ◽  
You-Ju Shu ◽  
Xue-Dong Wan ◽  
Zheng-Shun Xu ◽  
...  

1998 ◽  
Vol 332 (3) ◽  
pp. 703-712 ◽  
Author(s):  
Evelyn T. MAIZELS ◽  
Carl A. PETERS ◽  
Michael KLINE ◽  
Richard E. CUTLER ◽  
Malathy SHANMUGAM ◽  
...  

Small heat-shock proteins (sHSPs) are widely expressed 25–28 kDa proteins whose functions are dynamically regulated by phosphorylation. While recent efforts have clearly delineated a stress-responsive p38 mitogen-activated protein-kinase (MAPK)-dependent kinase pathway culminating in activation of the heat-shock (HSP)-kinases, mitogen-activated protein-kinase-activated protein kinase-2 and -3, not all sHSP phosphorylation events can be explained by the p38 MAPK-dependent pathway. The contribution of protein kinase C (PKC) to sHSP phosphorylation was suggested by early studies but later questioned on the basis of the reported poor ability of purified PKC to phosphorylate sHSP in vitro. The current study re-evaluates the role of PKC in sHSP phosphorylation in the light of the isoform complexity of the PKC family. We evaluated the sHSP phosphorylation status in rat corpora lutea obtained from two stages of pregnancy, mid-pregnancy and late-pregnancy, which express different levels of the novel PKC isoform, PKC-δ. Two-dimensional Western blot analysis showed that HSP-27 was more highly phosphorylated in vivo in corpora lutea of late pregnancy, corresponding to the developmental stage in which PKC-δ is abundant and active. Late-pregnant luteal extracts contained a lipid-sensitive HSP-kinase activity which exactly co-purified with PKC-δ using hydroxyapatite and S-Sepharose column chromatography. To determine whether there might be preferential phosphorylation of sHSP by a particular PKC isoform, purified recombinant PKC isoforms corresponding to those PKC isoforms detected in rat corpora lutea were evaluated for HSP-kinase activity in vitro. Recombinant PKC-δ effectively catalysed the phosphorylation of sHSP in vitro, and PKC-α was 30–50% as effective as an HSP-kinase; other PKCs tested (β1, β2, ε and ζ) were poor HSP-kinases. These results show that select PKC family members can function as direct HSP-kinases in vitro. Moreover, the observation of enhanced luteal HSP-27 phosphorylation in vivo, in late pregnancy, when PKC-δ is abundant and active, suggests that select PKC family members contribute to sHSP phosphorylation events in vivo.


2016 ◽  
Vol 38 (6) ◽  
pp. 627-630 ◽  
Author(s):  
Mohsen Taherdanak ◽  
Omid Jafari ◽  
Elham Vaez ◽  
Hamid Zilouei

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