PMID- 23311438
OWN - NLM
STAT- MEDLINE
DCOM- 20130924
LR  - 20130404
IS  - 1460-9568 (Electronic)
IS  - 0953-816X (Linking)
VI  - 37
IP  - 7
DP  - 2013 Apr
TI  - Effect of stroke on arginase expression and localization in the rat brain.
PG  - 1193-202
LID - 10.1111/ejn.12111 [doi]
AB  - Because arginase and nitric oxide (NO) synthases (NOS) compete to degrade 
      l-arginine, arginase plays a crucial role in the modulation of NO production. 
      Moreover, the arginase 1 isoform is a marker of M2 phenotype macrophages that 
      play a key role in tissue remodeling and resolution of inflammation. While NO has 
      been extensively investigated in ischemic stroke, the effect of stroke on the 
      arginase pathway is unknown. The present study focuses on arginase 
      expression/activity and localization before and after (1, 8, 15 and 30 days) the 
      photothrombotic ischemic stroke model. This model results in a cortical lesion 
      that reaches maximal volume at day 1 post-stroke and then decreases as a result 
      of astrocytic scar formation. Before stroke, arginase 1 and 2 expressions were 
      restricted to neurons. Stroke resulted in up-regulation of arginase 1 and 
      increased arginase activity in the region centered on the lesion where 
      inflammatory cells are present. These changes were associated with an early and 
      long-lasting arginase 1 up-regulation in activated macrophages and astrocytes and 
      a delayed arginase 1 down-regulation in neurons at the vicinity of the lesion. A 
      linear positive correlation was observed between expressions of arginase 1 and 
      glial fibrillary acidic protein as a marker of activated astrocytes. Moreover, 
      the pattern of arginase 1 and brain-derived neurotrophic factor (BDNF) 
      expressions in activated astrocytes was similar. Unlike arginase 1, arginase 2 
      expression was not changed by stroke. In conclusion, increased arginase 1 
      expression is not restricted to macrophages in inflammation elicited by stroke 
      but also occurs in activated astrocytes where it may contribute to 
      neuroplasticity through the control of BDNF production.
CI  - (c) 2013 Federation of European Neuroscience Societies and Blackwell Publishing 
      Ltd.
FAU - Quirie, Aurore
AU  - Quirie A
AD  - Faculte de Pharmacie, Unite INSERM U1093 Cognition, Action et Plasticite 
      Sensorimotrice, Dijon, France.
FAU - Demougeot, Celine
AU  - Demougeot C
FAU - Bertrand, Nathalie
AU  - Bertrand N
FAU - Mossiat, Claude
AU  - Mossiat C
FAU - Garnier, Philippe
AU  - Garnier P
FAU - Marie, Christine
AU  - Marie C
FAU - Prigent-Tessier, Anne
AU  - Prigent-Tessier A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130113
PL  - France
TA  - Eur J Neurosci
JT  - The European journal of neuroscience
JID - 8918110
RN  - 0 (Brain-Derived Neurotrophic Factor)
RN  - 0 (Glial Fibrillary Acidic Protein)
RN  - EC 3.5.3.1 (Arginase)
SB  - IM
MH  - Animals
MH  - Arginase/genetics/*metabolism
MH  - Astrocytes/metabolism
MH  - Brain/*enzymology/metabolism
MH  - Brain-Derived Neurotrophic Factor/genetics/metabolism
MH  - Cerebral Infarction/enzymology/metabolism
MH  - Gene Expression
MH  - Glial Fibrillary Acidic Protein/genetics/metabolism
MH  - Macrophages/metabolism
MH  - Male
MH  - Neurons/metabolism
MH  - Rats
MH  - Rats, Wistar
MH  - Stroke/*enzymology/metabolism
EDAT- 2013/01/15 06:00
MHDA- 2013/09/26 06:00
CRDT- 2013/01/15 06:00
PHST- 2012/06/04 00:00 [received]
PHST- 2012/10/30 00:00 [revised]
PHST- 2012/11/28 00:00 [accepted]
PHST- 2013/01/15 06:00 [entrez]
PHST- 2013/01/15 06:00 [pubmed]
PHST- 2013/09/26 06:00 [medline]
AID - 10.1111/ejn.12111 [doi]
PST - ppublish
SO  - Eur J Neurosci. 2013 Apr;37(7):1193-202. doi: 10.1111/ejn.12111. Epub 2013 Jan 
      13.