Growth hormone action in rat insulinoma cells expressing truncated growth hormone receptors

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Standard

Growth hormone action in rat insulinoma cells expressing truncated growth hormone receptors. / Møldrup, Annette; Allevato, G; Dyrberg, Thomas; Billestrup, N; Nielsen, Jens Høiriis.

I: The Journal of Biological Chemistry, Bind 266, Nr. 26, 15.09.1991, s. 17441-5.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Møldrup, A, Allevato, G, Dyrberg, T, Billestrup, N & Nielsen, JH 1991, 'Growth hormone action in rat insulinoma cells expressing truncated growth hormone receptors', The Journal of Biological Chemistry, bind 266, nr. 26, s. 17441-5.

APA

Møldrup, A., Allevato, G., Dyrberg, T., Billestrup, N., & Nielsen, J. H. (1991). Growth hormone action in rat insulinoma cells expressing truncated growth hormone receptors. The Journal of Biological Chemistry, 266(26), 17441-5.

Vancouver

Møldrup A, Allevato G, Dyrberg T, Billestrup N, Nielsen JH. Growth hormone action in rat insulinoma cells expressing truncated growth hormone receptors. The Journal of Biological Chemistry. 1991 sep 15;266(26):17441-5.

Author

Møldrup, Annette ; Allevato, G ; Dyrberg, Thomas ; Billestrup, N ; Nielsen, Jens Høiriis. / Growth hormone action in rat insulinoma cells expressing truncated growth hormone receptors. I: The Journal of Biological Chemistry. 1991 ; Bind 266, Nr. 26. s. 17441-5.

Bibtex

@article{2224eec7f5ae4210932c2c36a99d2d4c,
title = "Growth hormone action in rat insulinoma cells expressing truncated growth hormone receptors",
abstract = "Transfection of the insulin-producing rat islet tumor cell line RIN-5AH with a full length cDNA of the rat hepatic growth hormone (GH) receptor (GH-R1-638) augments the GH-responsive insulin synthesis in these cells. Using this functional system we analyzed the effect of COOH-terminal truncation of the GH receptor. Two mutated cDNAs encoding truncated GH receptors, GH-R1-294 and GH-R1-454, respectively, were generated by site-directed mutagenesis and transfected into the RIN cells. Both receptor mutants were expressed on the cell surface and displayed normal GH binding affinity. Whereas GH-R1-638 had a molecular mass of about 110 kDa, GH-R1-294 and GH-R1-454 showed molecular masses of 49 and 80 kDa, respectively. Cells expressing GH-R1-454 internalized GH to a similar extent as cells transfected with the full length receptor and the parent cell line, but GH-R1-294-expressing cells showed a markedly reduced capability of GH internalization. In contrast to cells transfected with GH-R1-638, none of the cell lines expressing truncated GH receptors exhibited any increase of the GH-stimulated insulin production. We conclude that domains within the COOH-terminal half of the cytoplasmic part of the GH receptor are required for transduction of the signal for GH-stimulated insulin synthesis, whereas cytoplasmic domains proximal to the transmembrane region are involved in receptor-mediated GH internalization.",
keywords = "Animals, Cytoplasm, Growth Hormone, Insulinoma, Kinetics, Mutagenesis, Site-Directed, Precipitin Tests, Rats, Receptors, Somatotropin, Transfection, Tumor Cells, Cultured",
author = "Annette M{\o}ldrup and G Allevato and Thomas Dyrberg and N Billestrup and Nielsen, {Jens H{\o}iriis}",
year = "1991",
month = "9",
day = "15",
language = "English",
volume = "266",
pages = "17441--5",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "26",

}

RIS

TY - JOUR

T1 - Growth hormone action in rat insulinoma cells expressing truncated growth hormone receptors

AU - Møldrup, Annette

AU - Allevato, G

AU - Dyrberg, Thomas

AU - Billestrup, N

AU - Nielsen, Jens Høiriis

PY - 1991/9/15

Y1 - 1991/9/15

N2 - Transfection of the insulin-producing rat islet tumor cell line RIN-5AH with a full length cDNA of the rat hepatic growth hormone (GH) receptor (GH-R1-638) augments the GH-responsive insulin synthesis in these cells. Using this functional system we analyzed the effect of COOH-terminal truncation of the GH receptor. Two mutated cDNAs encoding truncated GH receptors, GH-R1-294 and GH-R1-454, respectively, were generated by site-directed mutagenesis and transfected into the RIN cells. Both receptor mutants were expressed on the cell surface and displayed normal GH binding affinity. Whereas GH-R1-638 had a molecular mass of about 110 kDa, GH-R1-294 and GH-R1-454 showed molecular masses of 49 and 80 kDa, respectively. Cells expressing GH-R1-454 internalized GH to a similar extent as cells transfected with the full length receptor and the parent cell line, but GH-R1-294-expressing cells showed a markedly reduced capability of GH internalization. In contrast to cells transfected with GH-R1-638, none of the cell lines expressing truncated GH receptors exhibited any increase of the GH-stimulated insulin production. We conclude that domains within the COOH-terminal half of the cytoplasmic part of the GH receptor are required for transduction of the signal for GH-stimulated insulin synthesis, whereas cytoplasmic domains proximal to the transmembrane region are involved in receptor-mediated GH internalization.

AB - Transfection of the insulin-producing rat islet tumor cell line RIN-5AH with a full length cDNA of the rat hepatic growth hormone (GH) receptor (GH-R1-638) augments the GH-responsive insulin synthesis in these cells. Using this functional system we analyzed the effect of COOH-terminal truncation of the GH receptor. Two mutated cDNAs encoding truncated GH receptors, GH-R1-294 and GH-R1-454, respectively, were generated by site-directed mutagenesis and transfected into the RIN cells. Both receptor mutants were expressed on the cell surface and displayed normal GH binding affinity. Whereas GH-R1-638 had a molecular mass of about 110 kDa, GH-R1-294 and GH-R1-454 showed molecular masses of 49 and 80 kDa, respectively. Cells expressing GH-R1-454 internalized GH to a similar extent as cells transfected with the full length receptor and the parent cell line, but GH-R1-294-expressing cells showed a markedly reduced capability of GH internalization. In contrast to cells transfected with GH-R1-638, none of the cell lines expressing truncated GH receptors exhibited any increase of the GH-stimulated insulin production. We conclude that domains within the COOH-terminal half of the cytoplasmic part of the GH receptor are required for transduction of the signal for GH-stimulated insulin synthesis, whereas cytoplasmic domains proximal to the transmembrane region are involved in receptor-mediated GH internalization.

KW - Animals

KW - Cytoplasm

KW - Growth Hormone

KW - Insulinoma

KW - Kinetics

KW - Mutagenesis, Site-Directed

KW - Precipitin Tests

KW - Rats

KW - Receptors, Somatotropin

KW - Transfection

KW - Tumor Cells, Cultured

M3 - Journal article

VL - 266

SP - 17441

EP - 17445

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 26

ER -

ID: 47973746