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Biosynthesis of intestinal microvillar proteins. Processing of N-linked carbohydrate is not required for surface expression

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Standard

Biosynthesis of intestinal microvillar proteins. Processing of N-linked carbohydrate is not required for surface expression. / Danielsen, Erik Michael; Cowell, G M.

I: Biochemical Journal, Bind 240, Nr. 3, 1986, s. 777-82.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Danielsen, EM & Cowell, GM 1986, 'Biosynthesis of intestinal microvillar proteins. Processing of N-linked carbohydrate is not required for surface expression', Biochemical Journal, bind 240, nr. 3, s. 777-82.

APA

Danielsen, E. M., & Cowell, G. M. (1986). Biosynthesis of intestinal microvillar proteins. Processing of N-linked carbohydrate is not required for surface expression. Biochemical Journal, 240(3), 777-82.

Vancouver

Danielsen EM, Cowell GM. Biosynthesis of intestinal microvillar proteins. Processing of N-linked carbohydrate is not required for surface expression. Biochemical Journal. 1986;240(3):777-82.

Author

Danielsen, Erik Michael ; Cowell, G M. / Biosynthesis of intestinal microvillar proteins. Processing of N-linked carbohydrate is not required for surface expression. I: Biochemical Journal. 1986 ; Bind 240, Nr. 3. s. 777-82.

Bibtex

@article{8c43b1306c7a11de8bc9000ea68e967b,
title = "Biosynthesis of intestinal microvillar proteins. Processing of N-linked carbohydrate is not required for surface expression",
abstract = "Castanospermine, an inhibitor of glucosidase I, the initial enzyme in the trimming of N-linked carbohydrate, was used to study the importance of carbohydrate processing in the biosynthesis of microvillar enzymes in organ-cultured pig intestinal explants. For aminopeptidase N (EC 3.4.11.2), aminopeptidase A (EC 3.4.11.7), sucrase-isomaltase (EC 3.2.1.48-10) and maltase-glucoamylase (EC 3.2.1.20), castanospermine caused the formation of novel transient forms of higher Mr than corresponding controls, indicating a blocked removal of glucose residues. For the first three enzymes, the 'mature' (Golgi-processed) forms were similar in size to or slightly smaller than corresponding controls and were, as shown for aminopeptidase N, endoglycosidase-H-sensitive, evidence of a blocked attachment of complex sugars. Maltase-glucoamylase did not undergo conversion into a 'mature' form, suggesting that, unlike other microvillar enzymes, it does not receive post-translational O-linked carbohydrate. Castanospermine suppressed the synthesis of the four enzymes, but did not block their transport to the microvillar membrane, showing that processing of N-linked carbohydrate is not required for microvillar expression. The proteinase inhibitor leupeptin partially restored the suppressed synthesis, indicating that the majority of the wrongly processed enzymes, probably because of conformational instability, become degraded soon after synthesis rather than being transported to the microvillar membrane.",
author = "Danielsen, {Erik Michael} and Cowell, {G M}",
note = "Keywords: Alkaloids; Aminopeptidases; Animals; Antigens, CD13; Carbohydrate Metabolism; Electrophoresis, Polyacrylamide Gel; Indolizines; Intestinal Mucosa; Leupeptins; Membrane Proteins; Microvilli; Organ Culture Techniques; Swine",
year = "1986",
language = "English",
volume = "240",
pages = "777--82",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "3",

}

RIS

TY - JOUR

T1 - Biosynthesis of intestinal microvillar proteins. Processing of N-linked carbohydrate is not required for surface expression

AU - Danielsen, Erik Michael

AU - Cowell, G M

N1 - Keywords: Alkaloids; Aminopeptidases; Animals; Antigens, CD13; Carbohydrate Metabolism; Electrophoresis, Polyacrylamide Gel; Indolizines; Intestinal Mucosa; Leupeptins; Membrane Proteins; Microvilli; Organ Culture Techniques; Swine

PY - 1986

Y1 - 1986

N2 - Castanospermine, an inhibitor of glucosidase I, the initial enzyme in the trimming of N-linked carbohydrate, was used to study the importance of carbohydrate processing in the biosynthesis of microvillar enzymes in organ-cultured pig intestinal explants. For aminopeptidase N (EC 3.4.11.2), aminopeptidase A (EC 3.4.11.7), sucrase-isomaltase (EC 3.2.1.48-10) and maltase-glucoamylase (EC 3.2.1.20), castanospermine caused the formation of novel transient forms of higher Mr than corresponding controls, indicating a blocked removal of glucose residues. For the first three enzymes, the 'mature' (Golgi-processed) forms were similar in size to or slightly smaller than corresponding controls and were, as shown for aminopeptidase N, endoglycosidase-H-sensitive, evidence of a blocked attachment of complex sugars. Maltase-glucoamylase did not undergo conversion into a 'mature' form, suggesting that, unlike other microvillar enzymes, it does not receive post-translational O-linked carbohydrate. Castanospermine suppressed the synthesis of the four enzymes, but did not block their transport to the microvillar membrane, showing that processing of N-linked carbohydrate is not required for microvillar expression. The proteinase inhibitor leupeptin partially restored the suppressed synthesis, indicating that the majority of the wrongly processed enzymes, probably because of conformational instability, become degraded soon after synthesis rather than being transported to the microvillar membrane.

AB - Castanospermine, an inhibitor of glucosidase I, the initial enzyme in the trimming of N-linked carbohydrate, was used to study the importance of carbohydrate processing in the biosynthesis of microvillar enzymes in organ-cultured pig intestinal explants. For aminopeptidase N (EC 3.4.11.2), aminopeptidase A (EC 3.4.11.7), sucrase-isomaltase (EC 3.2.1.48-10) and maltase-glucoamylase (EC 3.2.1.20), castanospermine caused the formation of novel transient forms of higher Mr than corresponding controls, indicating a blocked removal of glucose residues. For the first three enzymes, the 'mature' (Golgi-processed) forms were similar in size to or slightly smaller than corresponding controls and were, as shown for aminopeptidase N, endoglycosidase-H-sensitive, evidence of a blocked attachment of complex sugars. Maltase-glucoamylase did not undergo conversion into a 'mature' form, suggesting that, unlike other microvillar enzymes, it does not receive post-translational O-linked carbohydrate. Castanospermine suppressed the synthesis of the four enzymes, but did not block their transport to the microvillar membrane, showing that processing of N-linked carbohydrate is not required for microvillar expression. The proteinase inhibitor leupeptin partially restored the suppressed synthesis, indicating that the majority of the wrongly processed enzymes, probably because of conformational instability, become degraded soon after synthesis rather than being transported to the microvillar membrane.

M3 - Journal article

C2 - 2881540

VL - 240

SP - 777

EP - 782

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 3

ER -

ID: 13063609