CATHEPSIN D : MANY FUNCTIONS OF ONE ASPARTIC PROTEASE

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F08%3A00024162" target="_blank" >RIV/00216224:14310/08:00024162 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
CATHEPSIN D : MANY FUNCTIONS OF ONE ASPARTIC PROTEASE
Original language description
For years, it has been held that cathepsin D (CD) is involved in rather non-specific protein degradation in a strongly acidic milieu of lysosomes. Studies with CD knock-out mice revealed that CD is not necessary for embryonal development, but it is indispensable for postnatal tissue homeostasis. Mutation that abolishes CD enzymatic activity causes neuronal ceroid lipofuscinosis (NCL) characterized by severe neurodegeneration, developmental regression, visual loss and epilepsy in both animals and humans.In the last decade, however, an increasing number of studies demonstrated that enzymatic function of CD is not restricted solely to acidic milieu of lysosomes with important consequences in regulation of apoptosis. In addition to CD enzymatic activity,it has been shown that apoptosis is also regulated by catalytically inactive mutants of CD which suggests that CD interacts with other important molecules and influences cell signaling. Moreover, procathepsin D (pCD), secreted from cancer
Czech name
Katepsin D : mnoho funkcí jediné aspartátové proteázy
Czech description
Tento přehledný článek shrnuje nejnovější poznatky o úloze různých forem katepsinu D ve fyziologických a patofyziologických procesech na úrovni buňky i celého organismu.

Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
FD - Oncology and haematology
OECD FORD branch
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Project
<a href="/en/project/IAA501630801" target="_blank" >IAA501630801: Mechanism of procathepsin D effect on breast cancer cells</a><br>
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year
2008
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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