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Formation of the alpha 1-microglobulin chromophore in mammalian and insect cells: a novel post-translational mechanism?

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Formation of the alpha 1-microglobulin chromophore in mammalian and insect cells: a novel post-translational mechanism? / Akerström, B; Bratt, T; Enghild, J J.

In: F E B S Letters, Vol. 362, No. 1, 1995, p. 50-4.

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@article{d9f802e0865311dda5a8000ea68e967b,
title = "Formation of the alpha 1-microglobulin chromophore in mammalian and insect cells: a novel post-translational mechanism?",
abstract = "alpha 1-Microglobulin is an immunosuppressive plasma protein synthesized by the liver. The isolated protein is yellow-brown, but the hypothetical chromophore has not yet been identified. In this work, it is shown that a human liver cell line, HepG2, grown in a completely synthetic and serum-free medium, secretes alpha 1-microglobulin which is also yellow-brown, suggesting a de novo synthesis of the chromophore by the cells. alpha 1-Microglobulin isolated from the culture medium of insect cells transfected with the gene for rat alpha 1-microglobulin is also yellow-brown, suggesting that the gene carries information about the chromophore. Reduction and alkylation or removal of N- or O-linked carbohydrates by glycosidase treatment did not reduce the colour intensity of the protein. An internal dodecapeptide (amino acid positions 70-81 in human alpha 1-microglobulin) was also yellow-brown. The latter results indicate that the chromophore is linked to the polypeptide. In conclusion, the results suggest that the alpha 1-microglobulin gene carries information activating a post-translational protein modification mechanism which is present in mammalian and insect cells.",
keywords = "Alkylation, Alpha-Globulins, Amino Acid Sequence, Animals, Cell Line, Glycosylation, Humans, Molecular Sequence Data, Moths, Oxidation-Reduction, Peptides, Pigments, Biological, Protein Processing, Post-Translational, Tumor Cells, Cultured",
author = "B Akerstr{\"o}m and T Bratt and Enghild, {J J}",
year = "1995",
language = "English",
volume = "362",
pages = "50--4",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd.",
number = "1",

}

RIS

TY - JOUR

T1 - Formation of the alpha 1-microglobulin chromophore in mammalian and insect cells: a novel post-translational mechanism?

AU - Akerström, B

AU - Bratt, T

AU - Enghild, J J

PY - 1995

Y1 - 1995

N2 - alpha 1-Microglobulin is an immunosuppressive plasma protein synthesized by the liver. The isolated protein is yellow-brown, but the hypothetical chromophore has not yet been identified. In this work, it is shown that a human liver cell line, HepG2, grown in a completely synthetic and serum-free medium, secretes alpha 1-microglobulin which is also yellow-brown, suggesting a de novo synthesis of the chromophore by the cells. alpha 1-Microglobulin isolated from the culture medium of insect cells transfected with the gene for rat alpha 1-microglobulin is also yellow-brown, suggesting that the gene carries information about the chromophore. Reduction and alkylation or removal of N- or O-linked carbohydrates by glycosidase treatment did not reduce the colour intensity of the protein. An internal dodecapeptide (amino acid positions 70-81 in human alpha 1-microglobulin) was also yellow-brown. The latter results indicate that the chromophore is linked to the polypeptide. In conclusion, the results suggest that the alpha 1-microglobulin gene carries information activating a post-translational protein modification mechanism which is present in mammalian and insect cells.

AB - alpha 1-Microglobulin is an immunosuppressive plasma protein synthesized by the liver. The isolated protein is yellow-brown, but the hypothetical chromophore has not yet been identified. In this work, it is shown that a human liver cell line, HepG2, grown in a completely synthetic and serum-free medium, secretes alpha 1-microglobulin which is also yellow-brown, suggesting a de novo synthesis of the chromophore by the cells. alpha 1-Microglobulin isolated from the culture medium of insect cells transfected with the gene for rat alpha 1-microglobulin is also yellow-brown, suggesting that the gene carries information about the chromophore. Reduction and alkylation or removal of N- or O-linked carbohydrates by glycosidase treatment did not reduce the colour intensity of the protein. An internal dodecapeptide (amino acid positions 70-81 in human alpha 1-microglobulin) was also yellow-brown. The latter results indicate that the chromophore is linked to the polypeptide. In conclusion, the results suggest that the alpha 1-microglobulin gene carries information activating a post-translational protein modification mechanism which is present in mammalian and insect cells.

KW - Alkylation

KW - Alpha-Globulins

KW - Amino Acid Sequence

KW - Animals

KW - Cell Line

KW - Glycosylation

KW - Humans

KW - Molecular Sequence Data

KW - Moths

KW - Oxidation-Reduction

KW - Peptides

KW - Pigments, Biological

KW - Protein Processing, Post-Translational

KW - Tumor Cells, Cultured

M3 - Journal article

C2 - 7535251

VL - 362

SP - 50

EP - 54

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 1

ER -