Cloning, molecular and functional characterization of putative phosphoinositide phosphatase, LdPIPh22, of the parasitic protozoan Leishmania donovani

Postgraduate Thesis uoadl:1318157 636 Read counter

Unit:
Κατεύθυνση Βιοχημεία
Library of the School of Science
Deposit date:
2014-02-14
Year:
2014
Author:
Κοτοπούλη Αναστασία
Supervisors info:
Ντία Γαλανοπούλου Αναπλ. Καθηγήτρια ΕΚΠΑ (επιβλέπουσα), Μαίρη Μαυρή, Αναπλ. Καθηγήτρια ΕΚΠΑ, Χαραλαμπία Μπολέτη, Ερευνήτρια Β', Ελληνικό Ινστιτούτο Παστέρ
Original Title:
Κλωνοποίηση, μοριακός και λειτουργικός χαρακτηρισμός της υποθετικής φωσφατάσης φωσφοϊνοσιτιδίων, LdPIPh22, του παρασιτικού πρωτοζώου Leishmania donovani
Languages:
Greek
Translated title:
Cloning, molecular and functional characterization of putative phosphoinositide phosphatase, LdPIPh22, of the parasitic protozoan Leishmania donovani
Summary:
Leishmaniasis is a group of anthropozoonotic diseases with 1.6 million new
cases per year in humans. The causative agent is the infection by parasitic
protozoa of the genus Leishmania. Specific phosphatases of the parasites could
be potential drug targets (inhibitors). Phosphatases, in general, are molecular
targets in the treatment of different diseases, infectious or not, but in the
Leishmania parasite their function is not yet clarified and their regulation
has not been studied. The main aim of this study was the generation of
molecular and cellular tools in order to examine the biochemical and functional
properties of the putative phosphoinositide phosphatase LdPIPh22.
Biochemically, the LdPIPh22 protein was found in protein fractions enriched in
membrane and/or cytoskeletal proteins. The protein had phosphatase activity in
vitro and in mammalian tissue culture cells, it was localized on sites of
dynamic actin polymerization, where phosphoinositides play important role.
Keywords:
Leishmania, Leishmaniasis, Phosphoinositide phosphatases, Anti-parasitic drugs
Index:
Yes
Number of index pages:
17, 19-24
Contains images:
Yes
Number of references:
102
Number of pages:
174
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