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1,3Fucosyltransferase VI is expressed in HepG2 cells and codistributed with 1,4galactosyltransferase I in the Golgi apparatus and monensin-induced swollen vesicles


Borsig, L; Imbach, T; Hochli, M; Berger, E G (1999). 1,3Fucosyltransferase VI is expressed in HepG2 cells and codistributed with 1,4galactosyltransferase I in the Golgi apparatus and monensin-induced swollen vesicles. Glycobiology, 9(11):1273-1280.

Abstract

The major α1,3fucosyltransferase activity in plasma, liver, and kidney is related to fucosyltransferase VI which is encoded by the FUT6 gene. Here we demonstrate the presence of α1,3fucosyltransferase VI (α3-FucT VI) in the human HepG2 hepatoma cell line by specific activity assays, detection of transcripts, and the use of specific antibodies. First, FucT activity in HepG2 cell lysates was shown to prefer sialyl-N-acetyllactosamine as acceptor substrate indicating expression of α3-FucT VI. RT-PCR analysis further confirmed the exclusive presence of the α3-FucT VI transcripts among the five human α3-FucTs cloned to date. α3-FucT VI was colocalized with β1,4galactosyltransferase I (β4-GalT I) to the Golgi apparatus by dual confocal immunostaining. Pulse/chase analysis of metabolically labeled α3-FucT VI showed maturation of α3-FucT VI from the early 43 kDa form to the mature, endoglycosidase H-resistant form of 47 kDa which was detected after 2 h of chase. α3-FucT VI was released to the medium and accounted for 50% of overall cell-associated and released enzyme activity. Release occurred by proteolytical cleavage which produced a soluble form of 43 kDa. Monensin treatment segregated α3-FucT VI from the Golgi apparatus to swollen peripheral vesicles where it was colocalized with β4-GalT I while α2,6(N)sialyltransferase remained associated with the Golgi apparatus. Both constitutive secretion of α3-FucT VI and its monensin-induced relocation to vesicles analogous to β4-GalT I suggest a similar post-Golgi pathway of both α3-FucT VI and β4-GalT I

Abstract

The major α1,3fucosyltransferase activity in plasma, liver, and kidney is related to fucosyltransferase VI which is encoded by the FUT6 gene. Here we demonstrate the presence of α1,3fucosyltransferase VI (α3-FucT VI) in the human HepG2 hepatoma cell line by specific activity assays, detection of transcripts, and the use of specific antibodies. First, FucT activity in HepG2 cell lysates was shown to prefer sialyl-N-acetyllactosamine as acceptor substrate indicating expression of α3-FucT VI. RT-PCR analysis further confirmed the exclusive presence of the α3-FucT VI transcripts among the five human α3-FucTs cloned to date. α3-FucT VI was colocalized with β1,4galactosyltransferase I (β4-GalT I) to the Golgi apparatus by dual confocal immunostaining. Pulse/chase analysis of metabolically labeled α3-FucT VI showed maturation of α3-FucT VI from the early 43 kDa form to the mature, endoglycosidase H-resistant form of 47 kDa which was detected after 2 h of chase. α3-FucT VI was released to the medium and accounted for 50% of overall cell-associated and released enzyme activity. Release occurred by proteolytical cleavage which produced a soluble form of 43 kDa. Monensin treatment segregated α3-FucT VI from the Golgi apparatus to swollen peripheral vesicles where it was colocalized with β4-GalT I while α2,6(N)sialyltransferase remained associated with the Golgi apparatus. Both constitutive secretion of α3-FucT VI and its monensin-induced relocation to vesicles analogous to β4-GalT I suggest a similar post-Golgi pathway of both α3-FucT VI and β4-GalT I

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Item Type:Journal Article, refereed, original work
Communities & Collections:National licences > 142-005
Dewey Decimal Classification:610 Medicine & health
Language:English
Date:1 November 1999
Deposited On:25 Sep 2018 14:14
Last Modified:26 Apr 2019 13:20
Publisher:Oxford University Press
ISSN:0959-6658
OA Status:Green
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.1093/glycob/9.11.1273
Related URLs:https://www.swissbib.ch/Search/Results?lookfor=nationallicenceoxford101093glycob9111273 (Library Catalogue)

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