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The α- to γ-enolase switch : the role and regulation of γ-enolase during oligodendrocyte differentiation
ID
Horvat, Selena
(
Avtor
),
ID
Pečar Fonović, Urša
(
Avtor
),
ID
Mitrović, Ana
(
Avtor
),
ID
Zidar, Nace
(
Avtor
),
ID
Kos, Janko
(
Avtor
),
ID
Pišlar, Anja
(
Avtor
)
PDF - Predstavitvena datoteka,
prenos
(10,32 MB)
MD5: C19F402E6B5203DB7CC39C55B645C054
URL - Izvorni URL, za dostop obiščite
https://www.sciencedirect.com/science/article/pii/S014181302501013X
Galerija slik
Izvleček
The glycolytic enzyme γ-enolase is a highly specific neuronal marker that is known to replace ubiquitously expressed α-enolase in the brain. Moreover, γ-enolase has been shown to exert neurotrophic activity, which is regulated by cathepsin X, a lysosomal peptidase. This study investigates the role of γ-enolase and its regulation by cathepsin X during the differentiation of oligodendrocytes, which are essential for normal brain function. We established a differentiation protocol for the human oligodendroglioma (HOG) cell line and demonstrated for the first time that an α- to γ-enolase switch occurs during HOG cell differentiation. This switch was confirmed by the expression of specific markers underscoring the role of γ-enolase in oligodendrocyte differentiation. Moreover, γ-enolase overexpression enhanced oligodendrocyte differentiation, while silencing of γ-enolase by siRNA significantly decreased maturation marker. Further, the regulatory role of cysteine peptidase cathepsin X on γ-enolase function was found. Silencing cathepsin X significantly changed cell morphology, enhanced oligodendrocyte differentiation, altered the expression of oligodendrocyte markers, and increased levels of the active form of γ-enolase. Inhibiting cathepsin X similarly changed cell morphology and enhanced oligodendrocyte differentiation. These findings suggest that cathepsin X modulates γ-enolase activity and thereby influences oligodendrocyte differentiation and thus neuronal function.
Jezik:
Angleški jezik
Ključne besede:
oligodendrocytes
,
differentiation
,
γ-enolase
,
α-enolase
,
cathepsin X
Vrsta gradiva:
Članek v reviji
Tipologija:
1.01 - Izvirni znanstveni članek
Organizacija:
FFA - Fakulteta za farmacijo
Status publikacije:
Objavljeno
Različica publikacije:
Objavljena publikacija
Leto izida:
2025
Št. strani:
15 str.
Številčenje:
Vol. 301, art. 140464
PID:
20.500.12556/RUL-167011
UDK:
579
ISSN pri članku:
1879-0003
DOI:
10.1016/j.ijbiomac.2025.140464
COBISS.SI-ID:
224856579
Datum objave v RUL:
03.02.2025
Število ogledov:
333
Število prenosov:
38
Metapodatki:
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Objavi na:
Gradivo je del revije
Naslov:
International journal of biological macromolecules
Skrajšan naslov:
Int. j. biol. macromol.
Založnik:
Elsevier
ISSN:
1879-0003
COBISS.SI-ID:
107163139
Licence
Licenca:
CC BY 4.0, Creative Commons Priznanje avtorstva 4.0 Mednarodna
Povezava:
http://creativecommons.org/licenses/by/4.0/deed.sl
Opis:
To je standardna licenca Creative Commons, ki daje uporabnikom največ možnosti za nadaljnjo uporabo dela, pri čemer morajo navesti avtorja.
Sekundarni jezik
Jezik:
Slovenski jezik
Ključne besede:
oligodendrociti
,
diferenciacija
,
γ-enolaza
,
α-enolaza
,
katepsin X
Projekti
Financer:
ARIS - Javna agencija za znanstvenoraziskovalno in inovacijsko dejavnost Republike Slovenije
Številka projekta:
P4-0127
Naslov:
Farmacevtska biotehnologija: znanost za zdravje
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