Journal article
A functionally atypical amidating enzyme from the human parasite Schistosoma mansoni
The FASEB journal, Vol.18(1), pp.114-121
01/2004
DOI: 10.1096/fj.03-0429com
PMID: 14718392
Abstract
ABSTRACT
Many neuropeptide transmitters require the presence of a carboxy‐terminal α‐amide group for biological activity. Amidation requires conversion of a glycine‐extended peptide intermediate into a C‐terminally amidated product. This post‐translational modification depends on the sequential action of two enzymes (peptidylglycine α‐hydroxylating monooxygenase or PHM, and peptidyl‐α‐hydroxyglycine α‐amidating lyase or PAL) that in most eukaryotes are expressed as separate domains of a single protein (peptidylglycine α‐amidating monooxygenase or PAM). We identified a cDNA encoding PHM in the human parasite Schistosoma mansoni. Transient expression of schistosome PHM (smPHM) revealed functional properties that are different from other PHM proteins;smPHM displays a lower pH‐optimum and, when expressed in mammalian cells, is heavily N‐glycosylated. In adult worms, PHM is found in the trans‐Golgi network and secretory vesicles of both central and peripheral nerves. The widespread occurrence of PHM in the nervous system confirms the important role of amidated neuropeptides in these parasitic flatworms. The differences between schistosome and mammalian PHM suggest that it could be a target for new chemotherapeutics.—FASEB J. 18, 114–121 (2004)
Details
- Title: Subtitle
- A functionally atypical amidating enzyme from the human parasite Schistosoma mansoni
- Creators
- Gunnar R Mair - Queen's University Belfast, Medical Biology CentreMark J Niciu - University of Connecticut Health CenterMichael T Stewart - Queen's University Belfast, Medical Biology CentreGerry Brennan - Queen's University Belfast, Medical Biology CentreHanan Omar - Iowa State UniversityDavid W Halton - Queen's University Belfast, Medical Biology CentreRichard Mains - University of Connecticut Health CenterBetty A Eipper - University of Connecticut Health CenterAaron G Maule - Queen's University Belfast, Medical Biology CentreTim A Day - Iowa State University
- Resource Type
- Journal article
- Publication Details
- The FASEB journal, Vol.18(1), pp.114-121
- DOI
- 10.1096/fj.03-0429com
- PMID
- 14718392
- NLM abbreviation
- FASEB J
- ISSN
- 0892-6638
- eISSN
- 1530-6860
- Publisher
- Federation of American Societies for Experimental Biology
- Number of pages
- 8
- Grant note
- NIH (ROI-AI49162)
- Language
- English
- Date published
- 01/2004
- Academic Unit
- Psychiatry; Iowa Neuroscience Institute
- Record Identifier
- 9984003468502771
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