Characterization of Gut-associated Cathepsin D Hemoglobinase from Tick Ixodes ricinus (IrCD1)
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F12%3A00377766" target="_blank" >RIV/60077344:_____/12:00377766 - isvavai.cz</a>
Alternative codes found
RIV/61388963:_____/12:00377766
Result on the web
<a href="http://dx.doi.org/10.1074/jbc.M112.347922" target="_blank" >http://dx.doi.org/10.1074/jbc.M112.347922</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1074/jbc.M112.347922" target="_blank" >10.1074/jbc.M112.347922</a>
Alternative languages
Result language
angličtina
Original language name
Characterization of Gut-associated Cathepsin D Hemoglobinase from Tick Ixodes ricinus (IrCD1)
Original language description
To identify the gut-associated tick aspartic hemoglobinase, this work focuses on the functional diversity of multiple Ixodes ricinus cathepsin D forms (IrCDs). Out of three encoding genes representing Ixodes scapularis genome paralogs, IrCD1 is the mostdistinct enzyme with a shortened propeptide region and a unique pattern of predicted post-translational modifications. IrCD1 gene transcription is induced by tick feeding and is restricted to the gut tissue. The hemoglobinolytic role of IrCD1 was furthersupported by immunolocalization of IrCD1 in the vesicles of tick gut cells. Properties of recombinantly expressed rIrCD1 are consistent with the endo-lysosomal environment because the zymogen is autoactivated and remains optimally active in acidic conditions. Hemoglobin cleavage pattern of rIrCD1 is identical to that produced by the native enzyme. The preference for hydrophobic residues at the P1 and P1' position was confirmed by screening a novel synthetic tetradecapeptidyl substrate l
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EB - Genetics and molecular biology
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Biological Chemistry
ISSN
0021-9258
e-ISSN
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Volume of the periodical
287
Issue of the periodical within the volume
25
Country of publishing house
US - UNITED STATES
Number of pages
12
Pages from-to
21152-21163
UT code for WoS article
000306416800036
EID of the result in the Scopus database
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