Hexose-6-phosphate dehydrogenase determines the reaction direction of 11beta-hydroxysteroid dehydrogenase type 1 as an oxoreductase

Atanas Atanasov; Lyubomir Nashev; Alex Odermatt; Christoph Frick; Roberto Schweizer

Hexose-6-phosphate dehydrogenase determines the reaction direction of 11beta-hydroxysteroid dehydrogenase type 1 as an oxoreductase

Atanas Atanasov, Lyubomir Nashev, Alex Odermatt, Christoph Frick, Roberto Schweizer

Veröffentlichungen: Beitrag in Fachzeitschrift › Artikel › Peer Reviewed

Abstract

The impact of hexose-6-phosphate dehydrogenase (H6PDH) on 11beta-hydroxysteroid dehydrogenase (11beta-HSD) type 1 activity was investigated upon coexpression in HEK-293 cells. Confocal microscopy analysis indicated colocalisation of both enzymes at the lumenal side of the endoplasmic reticulum (ER) membrane. Functional analysis in intact cells revealed fivefold stimulation of 11beta-HSD1 oxoreductase activity and sixfold decrease of dehydrogenase activity upon coexpression with H6PDH, without changing kinetic parameters in cell lysates. Thus, H6PDH directly determines the reaction direction of 11beta-HSD1 in intact cells as an oxoreductase without changing intrinsic catalytic properties of 11beta-HSD1 by regenerating NADPH in the ER-lumen

Originalsprache	Englisch
Seiten (von - bis)	129-133
Seitenumfang	5
Fachzeitschrift	FEBS Letters
Jahrgang	571
Ausgabenummer	1-3
Publikationsstatus	Veröffentlicht - 2004

ÖFOS 2012

106023 Molekularbiologie
301114 Zellbiologie

Zugriff auf Dokument

http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15280030

Zitationsweisen

@article{987857daa4964c569b3a94c542ef7866,

title = "Hexose-6-phosphate dehydrogenase determines the reaction direction of 11beta-hydroxysteroid dehydrogenase type 1 as an oxoreductase",

abstract = "The impact of hexose-6-phosphate dehydrogenase (H6PDH) on 11beta-hydroxysteroid dehydrogenase (11beta-HSD) type 1 activity was investigated upon coexpression in HEK-293 cells. Confocal microscopy analysis indicated colocalisation of both enzymes at the lumenal side of the endoplasmic reticulum (ER) membrane. Functional analysis in intact cells revealed fivefold stimulation of 11beta-HSD1 oxoreductase activity and sixfold decrease of dehydrogenase activity upon coexpression with H6PDH, without changing kinetic parameters in cell lysates. Thus, H6PDH directly determines the reaction direction of 11beta-HSD1 in intact cells as an oxoreductase without changing intrinsic catalytic properties of 11beta-HSD1 by regenerating NADPH in the ER-lumen",

author = "Atanas Atanasov and Lyubomir Nashev and Alex Odermatt and Christoph Frick and Roberto Schweizer",

year = "2004",

language = "English",

volume = "571",

pages = "129--133",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Wiley-Blackwell",

number = "1-3",

}

TY - JOUR

T1 - Hexose-6-phosphate dehydrogenase determines the reaction direction of 11beta-hydroxysteroid dehydrogenase type 1 as an oxoreductase

AU - Atanasov, Atanas

AU - Nashev, Lyubomir

AU - Odermatt, Alex

AU - Frick, Christoph

AU - Schweizer, Roberto

PY - 2004

Y1 - 2004

N2 - The impact of hexose-6-phosphate dehydrogenase (H6PDH) on 11beta-hydroxysteroid dehydrogenase (11beta-HSD) type 1 activity was investigated upon coexpression in HEK-293 cells. Confocal microscopy analysis indicated colocalisation of both enzymes at the lumenal side of the endoplasmic reticulum (ER) membrane. Functional analysis in intact cells revealed fivefold stimulation of 11beta-HSD1 oxoreductase activity and sixfold decrease of dehydrogenase activity upon coexpression with H6PDH, without changing kinetic parameters in cell lysates. Thus, H6PDH directly determines the reaction direction of 11beta-HSD1 in intact cells as an oxoreductase without changing intrinsic catalytic properties of 11beta-HSD1 by regenerating NADPH in the ER-lumen

AB - The impact of hexose-6-phosphate dehydrogenase (H6PDH) on 11beta-hydroxysteroid dehydrogenase (11beta-HSD) type 1 activity was investigated upon coexpression in HEK-293 cells. Confocal microscopy analysis indicated colocalisation of both enzymes at the lumenal side of the endoplasmic reticulum (ER) membrane. Functional analysis in intact cells revealed fivefold stimulation of 11beta-HSD1 oxoreductase activity and sixfold decrease of dehydrogenase activity upon coexpression with H6PDH, without changing kinetic parameters in cell lysates. Thus, H6PDH directly determines the reaction direction of 11beta-HSD1 in intact cells as an oxoreductase without changing intrinsic catalytic properties of 11beta-HSD1 by regenerating NADPH in the ER-lumen

M3 - Article

SN - 0014-5793

VL - 571

SP - 129

EP - 133

JO - FEBS Letters

JF - FEBS Letters

IS - 1-3

ER -

Hexose-6-phosphate dehydrogenase determines the reaction direction of 11beta-hydroxysteroid dehydrogenase type 1 as an oxoreductase

Abstract

ÖFOS 2012

Zugriff auf Dokument

Fingerprint

Zitationsweisen