Multiple growth hormone-binding proteins are expressed on insulin-producing cells

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Standard

Multiple growth hormone-binding proteins are expressed on insulin-producing cells. / Møldrup, A; Billestrup, N; Thorn, N A; Lernmark, A; Nielsen, Jens Høiriis.

I: Molecular endocrinology (Baltimore, Md.), Bind 3, Nr. 8, 08.1989, s. 1173-82.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Møldrup, A, Billestrup, N, Thorn, NA, Lernmark, A & Nielsen, JH 1989, 'Multiple growth hormone-binding proteins are expressed on insulin-producing cells', Molecular endocrinology (Baltimore, Md.), bind 3, nr. 8, s. 1173-82.

APA

Møldrup, A., Billestrup, N., Thorn, N. A., Lernmark, A., & Nielsen, J. H. (1989). Multiple growth hormone-binding proteins are expressed on insulin-producing cells. Molecular endocrinology (Baltimore, Md.), 3(8), 1173-82.

Vancouver

Møldrup A, Billestrup N, Thorn NA, Lernmark A, Nielsen JH. Multiple growth hormone-binding proteins are expressed on insulin-producing cells. Molecular endocrinology (Baltimore, Md.). 1989 aug;3(8):1173-82.

Author

Møldrup, A ; Billestrup, N ; Thorn, N A ; Lernmark, A ; Nielsen, Jens Høiriis. / Multiple growth hormone-binding proteins are expressed on insulin-producing cells. I: Molecular endocrinology (Baltimore, Md.). 1989 ; Bind 3, Nr. 8. s. 1173-82.

Bibtex

@article{f85bd01a335f41efb9a544f0ec691f85,
title = "Multiple growth hormone-binding proteins are expressed on insulin-producing cells",
abstract = "The insulin-producing rat islet tumor cell line, RIN-5AH, expresses somatogen binding sites and responds to GH by increased proliferation and insulin production. Affinity cross-linking shows that RIN-5AH cells contain two major GH-binding subunits of Mr 100-130K (110K), which appear to exist as disulfide-linked multimers of Mr 270-350K (300K). In addition, a minor Mr 180K GH-binding protein is identified which does not appear to be associated with other proteins by disulfide bridges. A plasma membrane-enriched fraction accounts for 86{\%} of the RIN-cell GH-binding activity while cytosol and intracellular organelles are low in GH-binding activity. The plasma membrane-bound activity is soluble in Triton X-100 with intact hormone binding characteristics. The apparent KD in detergent solution is estimated to 18 ng/ml (8 x 10(-10) M). 125I-hGH-affinity cross-linking to intact and detergent-solubilized membranes as well as hGH-affinity purified protein reveals labeled proteins of Mr 180K and Mr 285-350K. In contrast to the cross-linked Mr 300K complexes of intact cells those of disintegrated cellular material are resistant to reduction with dithiothreitol, and it is speculated that this is due to intersubunit cross-linking of the disulfide-linked Mr 110K GH-binding subunits. The GH-binding proteins are purified approximately 100-fold by one cycle of hGH-affinity chromatography and five major proteins of Mr 180K, 94K, 86K, 64K, and 54K are identified by silver staining in the purified fraction. It is concluded that the RIN-5AH cells have multiple GH-binding proteins which may mediate signals for either proliferation and/or insulin production.",
keywords = "Affinity Labels, Animals, Cell Fractionation, Cell Line, Cell Membrane, Chromatography, Affinity, Cross-Linking Reagents, Islets of Langerhans, Octoxynol, Polyethylene Glycols, Rats, Receptors, Somatotropin, Succinimides",
author = "A M{\o}ldrup and N Billestrup and Thorn, {N A} and A Lernmark and Nielsen, {Jens H{\o}iriis}",
year = "1989",
month = "8",
language = "English",
volume = "3",
pages = "1173--82",
journal = "Molecular Endocrinology",
issn = "0888-8809",
publisher = "Oxford University Press",
number = "8",

}

RIS

TY - JOUR

T1 - Multiple growth hormone-binding proteins are expressed on insulin-producing cells

AU - Møldrup, A

AU - Billestrup, N

AU - Thorn, N A

AU - Lernmark, A

AU - Nielsen, Jens Høiriis

PY - 1989/8

Y1 - 1989/8

N2 - The insulin-producing rat islet tumor cell line, RIN-5AH, expresses somatogen binding sites and responds to GH by increased proliferation and insulin production. Affinity cross-linking shows that RIN-5AH cells contain two major GH-binding subunits of Mr 100-130K (110K), which appear to exist as disulfide-linked multimers of Mr 270-350K (300K). In addition, a minor Mr 180K GH-binding protein is identified which does not appear to be associated with other proteins by disulfide bridges. A plasma membrane-enriched fraction accounts for 86% of the RIN-cell GH-binding activity while cytosol and intracellular organelles are low in GH-binding activity. The plasma membrane-bound activity is soluble in Triton X-100 with intact hormone binding characteristics. The apparent KD in detergent solution is estimated to 18 ng/ml (8 x 10(-10) M). 125I-hGH-affinity cross-linking to intact and detergent-solubilized membranes as well as hGH-affinity purified protein reveals labeled proteins of Mr 180K and Mr 285-350K. In contrast to the cross-linked Mr 300K complexes of intact cells those of disintegrated cellular material are resistant to reduction with dithiothreitol, and it is speculated that this is due to intersubunit cross-linking of the disulfide-linked Mr 110K GH-binding subunits. The GH-binding proteins are purified approximately 100-fold by one cycle of hGH-affinity chromatography and five major proteins of Mr 180K, 94K, 86K, 64K, and 54K are identified by silver staining in the purified fraction. It is concluded that the RIN-5AH cells have multiple GH-binding proteins which may mediate signals for either proliferation and/or insulin production.

AB - The insulin-producing rat islet tumor cell line, RIN-5AH, expresses somatogen binding sites and responds to GH by increased proliferation and insulin production. Affinity cross-linking shows that RIN-5AH cells contain two major GH-binding subunits of Mr 100-130K (110K), which appear to exist as disulfide-linked multimers of Mr 270-350K (300K). In addition, a minor Mr 180K GH-binding protein is identified which does not appear to be associated with other proteins by disulfide bridges. A plasma membrane-enriched fraction accounts for 86% of the RIN-cell GH-binding activity while cytosol and intracellular organelles are low in GH-binding activity. The plasma membrane-bound activity is soluble in Triton X-100 with intact hormone binding characteristics. The apparent KD in detergent solution is estimated to 18 ng/ml (8 x 10(-10) M). 125I-hGH-affinity cross-linking to intact and detergent-solubilized membranes as well as hGH-affinity purified protein reveals labeled proteins of Mr 180K and Mr 285-350K. In contrast to the cross-linked Mr 300K complexes of intact cells those of disintegrated cellular material are resistant to reduction with dithiothreitol, and it is speculated that this is due to intersubunit cross-linking of the disulfide-linked Mr 110K GH-binding subunits. The GH-binding proteins are purified approximately 100-fold by one cycle of hGH-affinity chromatography and five major proteins of Mr 180K, 94K, 86K, 64K, and 54K are identified by silver staining in the purified fraction. It is concluded that the RIN-5AH cells have multiple GH-binding proteins which may mediate signals for either proliferation and/or insulin production.

KW - Affinity Labels

KW - Animals

KW - Cell Fractionation

KW - Cell Line

KW - Cell Membrane

KW - Chromatography, Affinity

KW - Cross-Linking Reagents

KW - Islets of Langerhans

KW - Octoxynol

KW - Polyethylene Glycols

KW - Rats

KW - Receptors, Somatotropin

KW - Succinimides

M3 - Journal article

C2 - 2674691

VL - 3

SP - 1173

EP - 1182

JO - Molecular Endocrinology

JF - Molecular Endocrinology

SN - 0888-8809

IS - 8

ER -

ID: 47974246