PMID- 24235130
OWN - NLM
STAT- MEDLINE
DCOM- 20140116
LR  - 20220316
IS  - 1528-0020 (Electronic)
IS  - 0006-4971 (Linking)
VI  - 122
IP  - 20
DP  - 2013 Nov 14
TI  - Asparaginase unveils glutamine-addicted AML.
PG  - 3398-400
LID - 10.1182/blood-2013-09-526392 [doi]
AB  - In this issue of Blood, Willems et al describe the dependence of acute myeloid 
      leukemia (AML) cells on glutamine for maintaining protein synthesis downstream of 
      mammalian target of rapamycin (mTOR) and show that the enzyme asparaginase can be 
      used to target this dependence. Using various AML cell lines, primary samples, 
      and CD341 stem cells from healthy donors, the authors support the notion that 
      asparaginase may offer a therapeutic benefit in AML-not from its well-known 
      enzymatic activity, but from its "off-target" effects on glutamine levels that 
      result in inhibition of downstream mTOR signaling, inhibition of protein 
      synthesis, and ultimately loss of viability.
FAU - Samudio, Ismael
AU  - Samudio I
AD  - TERRY FOX LABORATORY;
FAU - Konopleva, Marina
AU  - Konopleva M
LA  - eng
PT  - Comment
PT  - Journal Article
PL  - United States
TA  - Blood
JT  - Blood
JID - 7603509
RN  - 0RH81L854J (Glutamine)
SB  - IM
CON - Blood. 2013 Nov 14;122(20):3521-32. PMID: 24014241
MH  - Animals
MH  - Female
MH  - Glutamine/*antagonists & inhibitors
MH  - Humans
MH  - Leukemia, Myeloid, Acute/*drug therapy
MH  - Male
EDAT- 2013/11/16 06:00
MHDA- 2014/01/17 06:00
CRDT- 2013/11/16 06:00
PHST- 2013/11/16 06:00 [entrez]
PHST- 2013/11/16 06:00 [pubmed]
PHST- 2014/01/17 06:00 [medline]
AID - S0006-4971(20)36352-7 [pii]
AID - 10.1182/blood-2013-09-526392 [doi]
PST - ppublish
SO  - Blood. 2013 Nov 14;122(20):3398-400. doi: 10.1182/blood-2013-09-526392.