Tyrosine sulphation is not required for microvillar expression of intestinal aminopeptidase N

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Tyrosine sulphation is not required for microvillar expression of intestinal aminopeptidase N. / Danielsen, E M.

In: Biochemical Journal, Vol. 254, No. 1, 1988, p. 219-22.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Danielsen, EM 1988, 'Tyrosine sulphation is not required for microvillar expression of intestinal aminopeptidase N', Biochemical Journal, vol. 254, no. 1, pp. 219-22.

APA

Danielsen, E. M. (1988). Tyrosine sulphation is not required for microvillar expression of intestinal aminopeptidase N. Biochemical Journal, 254(1), 219-22.

Vancouver

Danielsen EM. Tyrosine sulphation is not required for microvillar expression of intestinal aminopeptidase N. Biochemical Journal. 1988;254(1):219-22.

Author

Danielsen, E M. / Tyrosine sulphation is not required for microvillar expression of intestinal aminopeptidase N. In: Biochemical Journal. 1988 ; Vol. 254, No. 1. pp. 219-22.

Bibtex

@article{dc563cd0e7bc11ddbf70000ea68e967b,
title = "Tyrosine sulphation is not required for microvillar expression of intestinal aminopeptidase N",
abstract = "The effect of 2,6-dichloro-4-nitrophenol (DCNP), an inhibitor of phenol sulphotransferases (EC 2.8.2.-), on the biosynthesis of aminopeptidase N (EC 3.4.11.2) was studied in organ-cultured pig intestinal mucosal explants. At 50 microM DCNP did not affect protein synthesis but it decreased incorporation of [35S]sulphate into aminopeptidase N and other major microvillar hydrolases by 70-85% compared with controls, indicating an inhibition of their post-translational tyrosine sulphation. In labelling experiments with [35S]methionine from 0.5 to 5 h, DCNP was tested for its possible influence on synthesis, processing and microvillar expression of aminopeptidase N, but no effect on any of these parameters could be detected. It can therefore be concluded that tyrosine sulphation is not required (for instance as a sorting signal) for the targeting of newly synthesized enzymes to the microvillar membrane.",
author = "Danielsen, {E M}",
note = "Keywords: Aminopeptidases; Animals; Antigens, CD13; Electrophoresis, Polyacrylamide Gel; Enzyme Induction; Intestinal Mucosa; Microvilli; Nitrophenols; Organ Culture Techniques; Protein Biosynthesis; Sulfur Radioisotopes; Swine; Tyrosine",
year = "1988",
language = "English",
volume = "254",
pages = "219--22",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd.",
number = "1",

}

RIS

TY - JOUR

T1 - Tyrosine sulphation is not required for microvillar expression of intestinal aminopeptidase N

AU - Danielsen, E M

N1 - Keywords: Aminopeptidases; Animals; Antigens, CD13; Electrophoresis, Polyacrylamide Gel; Enzyme Induction; Intestinal Mucosa; Microvilli; Nitrophenols; Organ Culture Techniques; Protein Biosynthesis; Sulfur Radioisotopes; Swine; Tyrosine

PY - 1988

Y1 - 1988

N2 - The effect of 2,6-dichloro-4-nitrophenol (DCNP), an inhibitor of phenol sulphotransferases (EC 2.8.2.-), on the biosynthesis of aminopeptidase N (EC 3.4.11.2) was studied in organ-cultured pig intestinal mucosal explants. At 50 microM DCNP did not affect protein synthesis but it decreased incorporation of [35S]sulphate into aminopeptidase N and other major microvillar hydrolases by 70-85% compared with controls, indicating an inhibition of their post-translational tyrosine sulphation. In labelling experiments with [35S]methionine from 0.5 to 5 h, DCNP was tested for its possible influence on synthesis, processing and microvillar expression of aminopeptidase N, but no effect on any of these parameters could be detected. It can therefore be concluded that tyrosine sulphation is not required (for instance as a sorting signal) for the targeting of newly synthesized enzymes to the microvillar membrane.

AB - The effect of 2,6-dichloro-4-nitrophenol (DCNP), an inhibitor of phenol sulphotransferases (EC 2.8.2.-), on the biosynthesis of aminopeptidase N (EC 3.4.11.2) was studied in organ-cultured pig intestinal mucosal explants. At 50 microM DCNP did not affect protein synthesis but it decreased incorporation of [35S]sulphate into aminopeptidase N and other major microvillar hydrolases by 70-85% compared with controls, indicating an inhibition of their post-translational tyrosine sulphation. In labelling experiments with [35S]methionine from 0.5 to 5 h, DCNP was tested for its possible influence on synthesis, processing and microvillar expression of aminopeptidase N, but no effect on any of these parameters could be detected. It can therefore be concluded that tyrosine sulphation is not required (for instance as a sorting signal) for the targeting of newly synthesized enzymes to the microvillar membrane.

M3 - Journal article

C2 - 2902847

VL - 254

SP - 219

EP - 222

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 1

ER -

ID: 9881094