PMID- 22244880
OWN - NLM
STAT- MEDLINE
DCOM- 20120717
LR  - 20211021
IS  - 1872-6240 (Electronic)
IS  - 0006-8993 (Print)
IS  - 0006-8993 (Linking)
VI  - 1438
DP  - 2012 Feb 15
TI  - Oxygen-glucose deprivation (OGD) and interleukin-1 (IL-1) differentially modulate 
      cathepsin B/L mediated generation of neuroprotective perlecan LG3 by neurons.
PG  - 65-74
LID - 10.1016/j.brainres.2011.12.027 [doi]
AB  - Brain extracellular matrix (ECM) is highly degraded after cerebral ischemia. The 
      perlecan c-terminal fragment LG3 is generated at increased levels by proteolytic 
      processing as long as 3 days after ischemia. It has previously been shown that 
      oxygen-glucose deprivation (OGD), reperfusion and interleukin-1 alpha (IL-1alpha) 
      stimulate brain cells to yield increased levels of LG3. This LG3, in turn, is 
      neuroprotective against OGD, and may therefore represent one of the brain's 
      defenses against ischemic injury. Here, we investigate whether, in neurons, this 
      increased LG3 is the result of increased perlecan generation and cellular 
      release, increased protease release (to generate LG3 from previous 
      extracellularly deposited perlecan) or both. We found that pre-synthesized 
      perlecan may be exocytosed by neurons during OGD and de novo synthesis of 
      perlecan is increased during reperfusion, even 24 h after OGD. Furthermore, while 
      cathepsin L activity was seen to be marginally important to generate LG3 during 
      normoxic conditions, cathepsin B activity was found to be important to generate 
      increased levels of LG3 following OGD and reperfusion. On the other hand, IL-1alpha 
      treatment raised levels of cathepsin L in neuronal media, and both cathepsin L 
      and cathepsin B were demonstrated to be important for increasing LG3 levels after 
      IL-1alpha treatment.
CI  - Copyright (c) 2011 Elsevier B.V. All rights reserved.
FAU - Saini, Maxim G
AU  - Saini MG
AD  - Department of Molecular and Cellular Medicine, Texas A&M College of Medicine, 
      College Station, TX, USA.
FAU - Bix, Gregory J
AU  - Bix GJ
LA  - eng
GR  - R01 NS065842/NS/NINDS NIH HHS/United States
GR  - R01 NS065842-01A1/NS/NINDS NIH HHS/United States
GR  - R01 NS065842-02/NS/NINDS NIH HHS/United States
GR  - R01NS065842-01A01/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20111220
PL  - Netherlands
TA  - Brain Res
JT  - Brain research
JID - 0045503
RN  - 0 (Heparan Sulfate Proteoglycans)
RN  - 0 (Interleukin-1)
RN  - 0 (Neuroprotective Agents)
RN  - 0 (Peptide Fragments)
RN  - 143972-95-6 (perlecan)
RN  - EC 3.4.22.1 (Cathepsin B)
RN  - EC 3.4.22.1 (Ctsb protein, mouse)
RN  - EC 3.4.22.15 (Cathepsin L)
RN  - EC 3.4.22.15 (Ctsl protein, mouse)
RN  - IY9XDZ35W2 (Glucose)
RN  - S88TT14065 (Oxygen)
SB  - IM
MH  - Animals
MH  - Cathepsin B/*metabolism
MH  - Cathepsin L/*metabolism
MH  - Cell Hypoxia
MH  - Cells, Cultured
MH  - Cerebral Cortex/cytology/embryology
MH  - Exocytosis
MH  - Glucose/*metabolism
MH  - Heparan Sulfate Proteoglycans/*metabolism
MH  - Interleukin-1/*metabolism
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Neurons/*metabolism
MH  - Neuroprotective Agents/metabolism
MH  - Oxygen/*metabolism
MH  - Peptide Fragments/metabolism
PMC - PMC3273646
MID - NIHMS346199
EDAT- 2012/01/17 06:00
MHDA- 2012/07/18 06:00
PMCR- 2013/02/15
CRDT- 2012/01/17 06:00
PHST- 2011/10/11 00:00 [received]
PHST- 2011/11/24 00:00 [revised]
PHST- 2011/12/13 00:00 [accepted]
PHST- 2012/01/17 06:00 [entrez]
PHST- 2012/01/17 06:00 [pubmed]
PHST- 2012/07/18 06:00 [medline]
PHST- 2013/02/15 00:00 [pmc-release]
AID - S0006-8993(11)02228-1 [pii]
AID - 10.1016/j.brainres.2011.12.027 [doi]
PST - ppublish
SO  - Brain Res. 2012 Feb 15;1438:65-74. doi: 10.1016/j.brainres.2011.12.027. Epub 2011 
      Dec 20.