Polyamine homoeostasis as a drug target in pathogenic protozoa: peculiarities and possibilities
(2011) In Biochemical Journal 438. p.229-244- Abstract
- New drugs are urgently needed for the treatment of tropical and subtropical parasitic diseases, such as African sleeping sickness. Chagas' disease, leishmaniasis and malaria. Enzymes in polyamine biosynthesis and thiol metabolism, as well as polyamine transporters, are potential drug targets within these organisms. In the present review, the current knowledge of unique properties of polyamine metabolism in these parasites is outlined. These properties include prozyme regulation of AdoMetDC (S-adenosylmethionine decarboxylase) activity in trypanosomatids, co-expression of ODC (ornithine decarboxylase) and AdoMetDC activities in a single protein in plasmodia, and formation of trypanothione, a unique compound linking polyamine and thiol... (More)
- New drugs are urgently needed for the treatment of tropical and subtropical parasitic diseases, such as African sleeping sickness. Chagas' disease, leishmaniasis and malaria. Enzymes in polyamine biosynthesis and thiol metabolism, as well as polyamine transporters, are potential drug targets within these organisms. In the present review, the current knowledge of unique properties of polyamine metabolism in these parasites is outlined. These properties include prozyme regulation of AdoMetDC (S-adenosylmethionine decarboxylase) activity in trypanosomatids, co-expression of ODC (ornithine decarboxylase) and AdoMetDC activities in a single protein in plasmodia, and formation of trypanothione, a unique compound linking polyamine and thiol metabolism in trypanosomatids. Particularly interesting features within polyamine metabolism in these parasites are highlighted for their potential in selective therapeutic strategies. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2180025
- author
- Birkholtz, Lyn-Marie ; Williams, Marni ; Niemand, Jandeli ; Louw, Abraham I. ; Persson, Lo LU and Heby, Olle
- organization
- publishing date
- 2011
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- alpha-difluoromethylornithine, Leishmania, malaria, ornithine, decarboxylase (ODC), polyamine, S-adenosylmethionine decarboxylase, (AdoMetDC), spermidine synthase, Trypanosoma
- in
- Biochemical Journal
- volume
- 438
- pages
- 229 - 244
- publisher
- Portland Press
- external identifiers
-
- wos:000295195400001
- scopus:80051673618
- pmid:21834794
- ISSN
- 0264-6021
- DOI
- 10.1042/BJ20110362
- language
- English
- LU publication?
- yes
- id
- 5e78eddd-463d-4c4a-b8dc-dad3b7e36a3b (old id 2180025)
- date added to LUP
- 2016-04-01 14:50:10
- date last changed
- 2022-01-28 02:47:48
@article{5e78eddd-463d-4c4a-b8dc-dad3b7e36a3b, abstract = {{New drugs are urgently needed for the treatment of tropical and subtropical parasitic diseases, such as African sleeping sickness. Chagas' disease, leishmaniasis and malaria. Enzymes in polyamine biosynthesis and thiol metabolism, as well as polyamine transporters, are potential drug targets within these organisms. In the present review, the current knowledge of unique properties of polyamine metabolism in these parasites is outlined. These properties include prozyme regulation of AdoMetDC (S-adenosylmethionine decarboxylase) activity in trypanosomatids, co-expression of ODC (ornithine decarboxylase) and AdoMetDC activities in a single protein in plasmodia, and formation of trypanothione, a unique compound linking polyamine and thiol metabolism in trypanosomatids. Particularly interesting features within polyamine metabolism in these parasites are highlighted for their potential in selective therapeutic strategies.}}, author = {{Birkholtz, Lyn-Marie and Williams, Marni and Niemand, Jandeli and Louw, Abraham I. and Persson, Lo and Heby, Olle}}, issn = {{0264-6021}}, keywords = {{alpha-difluoromethylornithine; Leishmania; malaria; ornithine; decarboxylase (ODC); polyamine; S-adenosylmethionine decarboxylase; (AdoMetDC); spermidine synthase; Trypanosoma}}, language = {{eng}}, pages = {{229--244}}, publisher = {{Portland Press}}, series = {{Biochemical Journal}}, title = {{Polyamine homoeostasis as a drug target in pathogenic protozoa: peculiarities and possibilities}}, url = {{http://dx.doi.org/10.1042/BJ20110362}}, doi = {{10.1042/BJ20110362}}, volume = {{438}}, year = {{2011}}, }