PMID- 23834360
OWN - NLM
STAT- MEDLINE
DCOM- 20140411
LR  - 20130913
IS  - 1748-1716 (Electronic)
IS  - 1748-1708 (Linking)
VI  - 209
IP  - 2
DP  - 2013 Oct
TI  - Changes in phosphorylated heat-shock protein 27 in response to acute ureteral 
      obstruction in rats.
PG  - 167-78
LID - 10.1111/apha.12135 [doi]
AB  - AIM: In vivo, renal medullary interstitial cells (RMICs) and collecting duct 
      principal cells (mpkCCD cells) are subjected to inflammatory, oxidative and 
      mechanical stress as a result of unilateral ureteral obstruction (UUO). Because 
      heat-shock protein (HSP) 27 and HSP70 are induced by cellular stresses and play a 
      role in cytoprotection, we hypothesized that HSP27 and HSP70 are increased in 
      rats subjected to acute UUO and in RMICs and mpkCCD cells exposed to 
      inflammatory, oxidative or mechanical stress. METHODS: Rats were subjected to 
      acute UUO for 6 h and 12 h. To examine the expression of HSP27, phosphorylated 
      HSP27 (pHSP27) and HSP70 in response to inflammatory, oxidative and mechanical 
      stress in vitro, we exposed RMICs and mpkCCD cells to interleukin 1beta (IL-1beta), 
      hydrogen peroxide (H2 O2 ), and stretch stimulation over time. RESULTS: The 
      phosphorylated form of HSP27 (pHSP27) was increased in the renal inner medulla 
      (IM) after 6-h and 12-h UUO, while HSP27 and HSP70 were unchanged. Furthermore, 
      after 6 h and 12 h of UUO, the expression of inflammatory (IL-1beta) and oxidative 
      [haem oxygenase 1 (HO-1)] markers was induced. Exposure to inflammatory, 
      oxidative and mechanical stress changed HSP27 and pHSP27 expression in RMICs but 
      not in mpkCCD cells, while HSP70 was not affected by any of the stress 
      conditions. Exposure of RMICs to oxidative and mechanical stress induced HSP27 
      phosphorylation via a p38-dependent mechanism. CONCLUSION: These data demonstrate 
      that, in response to acute UUO, different forms of cellular stresses modulate 
      HSP27 expression and phosphorylation in RMICs. This may affect the ability of 
      renal cells to mount an effective cytoprotective response.
CI  - (c) 2013 Scandinavian Physiological Society. Published by John Wiley & Sons Ltd.
FAU - Carlsen, I
AU  - Carlsen I
AD  - The Water and Salt Research Center, Aarhus University, Aarhus, Denmark; Institute 
      of Clinical Medicine, Aarhus University Hospital-Skejby, Aarhus, Denmark.
FAU - Nilsson, L
AU  - Nilsson L
FAU - Frokiaer, J
AU  - Frokiaer J
FAU - Norregaard, R
AU  - Norregaard R
LA  - eng
PT  - Journal Article
DEP - 20130709
PL  - England
TA  - Acta Physiol (Oxf)
JT  - Acta physiologica (Oxford, England)
JID - 101262545
RN  - 0 (HSP27 Heat-Shock Proteins)
RN  - 0 (HSP70 Heat-Shock Proteins)
RN  - 0 (Hspb1 protein, rat)
SB  - IM
MH  - Animals
MH  - HSP27 Heat-Shock Proteins/analysis/*biosynthesis
MH  - HSP70 Heat-Shock Proteins/analysis/biosynthesis
MH  - Immunoblotting
MH  - Immunohistochemistry
MH  - Kidney Medulla/*metabolism
MH  - Kidney Tubules, Collecting/*metabolism
MH  - Male
MH  - Oxidative Stress/physiology
MH  - Phosphorylation
MH  - Polymerase Chain Reaction
MH  - Rats
MH  - Rats, Wistar
MH  - Stress, Mechanical
MH  - Ureteral Obstruction/*metabolism
OTO - NOTNLM
OT  - HSP27
OT  - renal medullary interstitial cells
OT  - unilateral ureteral obstruction
EDAT- 2013/07/10 06:00
MHDA- 2014/04/12 06:00
CRDT- 2013/07/10 06:00
PHST- 2012/07/13 00:00 [received]
PHST- 2012/09/18 00:00 [revised]
PHST- 2013/05/31 00:00 [revised]
PHST- 2013/06/05 00:00 [accepted]
PHST- 2013/07/10 06:00 [entrez]
PHST- 2013/07/10 06:00 [pubmed]
PHST- 2014/04/12 06:00 [medline]
AID - 10.1111/apha.12135 [doi]
PST - ppublish
SO  - Acta Physiol (Oxf). 2013 Oct;209(2):167-78. doi: 10.1111/apha.12135. Epub 2013 
      Jul 9.