RT Book, Section
A1 Chabner, Bruce A.
A2 Chabner, Bruce A.
A2 Longo, Dan L.
SR Print(0)
ID 1127646575
T1 l-Asparaginase
T2 Harrison's Manual of Oncology, 2e
YR 2016
FD 2016
PB McGraw-Hill Education
PP New York, NY
SN 9780071793254
LK hemonc.mhmedical.com/content.aspx?aid=1127646575
RD 2024/04/19
AB Most  anticancer  drugs  are  small  synthetic  molecules  designed  to  inhibit  enzymes  or  to  interact  with  DNA.  Newer  drugs  may  also  be  proteins,  such  as  monoclonal  antibodies  or  cytokines  (interferon,  IL-2)  that  interact  with  cell  surface  receptors.  l-asparaginase  (L-ASP)  is  unique  as  a  bacterial  enzyme  that  hydrolyzes  an  essential  amino  acid,  L-asparagine,  and  through  that  action,  kills  tumor  cells.  Its  efficacy  is  based  on  the  observation  that  some  lymphoid  malignancies  are  unable  to  synthesize  asparagine  and  must  derive  it  from  the  blood  stream.  Enzyme  purified  from  Escherichia  coli  (1)  is  now  an  essential  component  of  the  regimen  for  remission  induction  and  consolidation  for  childhood  acute  lymphocytic  leukemia  (ALL).  While  enzymatic  activity  is  highly  specific  for  asparagine  hydrolysis,  asparagine  depletion  not  only  kills  tumor  cells  but  also  leads  to  a  broad  range  of  toxicities  resulting  from  inhibition  of  the  synthesis  of  clotting  factors,  insulin,  and  other  essential  proteins.