Plasma ammonia concentration after L‐asparaginase therapy in 27 dogs with high‐grade lymphoma or leukemia

Plasma ammonia concentration after L‐asparaginase therapy in 27 dogs with high‐grade lymphoma... AbbreviationsAEadverse eventALTalanine transaminaseALPalkaline phosphatasecPLIcanine pancreatic lipase immunoreactivityGIgastrointestinalL‐aspL‐asparaginaseIntroductionL‐asparaginase (L‐asp) is an enzyme commonly used in both human and veterinary medicine as part of multiagent chemotherapy protocols for lymphoproliferative malignancies. L‐asp works by depleting the peripheral blood of asparagine, a necessary amino acid for survival of lymphoid cells. While normal lymphoid cells are able to produce their own asparagine, neoplastic lymphoid cells cannot, leaving them reliant upon extracellular asparagine reserves. Adverse reactions to L‐asp are not common in dogs; however, previously reported reactions include anaphylaxis, pancreatitis, decreased protein synthesis, coagulopathies, hepatotoxicity, and more recently, hyperammonemic encephalopathy. Hyperammonemic encephalopathy is a rare complication of intensive chemotherapy in people characterized by increased serum ammonia concentration, normal liver function tests, and respiratory alkalosis. Hyperammonemic encephalopathy has been documented in people treated with several chemotherapy agents including cytarabine, vincristine, etoposide, L‐asp, cyclophosphamide, 5‐fluorouracil, and sunitinib. L‐asp has been reported to cause hyperammonemia in people with acute lymphoblastic leukemia and lymphoma. Two mechanisms of action have been described. First, asparagine is deaminated by asparaginase, which leads to the breakdown products of ammonia and aspartic acid, and thus accumulation of ammonia in the plasma. Glutamine metabolism is also diverted to asparagine synthesis, which is immediately deaminated by http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Veterinary Emergency and Critical Care Wiley

Plasma ammonia concentration after L‐asparaginase therapy in 27 dogs with high‐grade lymphoma or leukemia

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Publisher
Wiley Subscription Services, Inc., A Wiley Company
Copyright
Copyright © 2018 Veterinary Emergency and Critical Care Society
ISSN
1479-3261
eISSN
1476-4431
D.O.I.
10.1111/vec.12695
Publisher site
See Article on Publisher Site

Abstract

AbbreviationsAEadverse eventALTalanine transaminaseALPalkaline phosphatasecPLIcanine pancreatic lipase immunoreactivityGIgastrointestinalL‐aspL‐asparaginaseIntroductionL‐asparaginase (L‐asp) is an enzyme commonly used in both human and veterinary medicine as part of multiagent chemotherapy protocols for lymphoproliferative malignancies. L‐asp works by depleting the peripheral blood of asparagine, a necessary amino acid for survival of lymphoid cells. While normal lymphoid cells are able to produce their own asparagine, neoplastic lymphoid cells cannot, leaving them reliant upon extracellular asparagine reserves. Adverse reactions to L‐asp are not common in dogs; however, previously reported reactions include anaphylaxis, pancreatitis, decreased protein synthesis, coagulopathies, hepatotoxicity, and more recently, hyperammonemic encephalopathy. Hyperammonemic encephalopathy is a rare complication of intensive chemotherapy in people characterized by increased serum ammonia concentration, normal liver function tests, and respiratory alkalosis. Hyperammonemic encephalopathy has been documented in people treated with several chemotherapy agents including cytarabine, vincristine, etoposide, L‐asp, cyclophosphamide, 5‐fluorouracil, and sunitinib. L‐asp has been reported to cause hyperammonemia in people with acute lymphoblastic leukemia and lymphoma. Two mechanisms of action have been described. First, asparagine is deaminated by asparaginase, which leads to the breakdown products of ammonia and aspartic acid, and thus accumulation of ammonia in the plasma. Glutamine metabolism is also diverted to asparagine synthesis, which is immediately deaminated by

Journal

Journal of Veterinary Emergency and Critical CareWiley

Published: Jan 1, 2018

Keywords: ; ; ; ; ;

References

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