Identification of the salmon somatolactin receptor, a new member of the cytokine receptor family

Haruhisa Fukada, Yuichi Ozaki, Andrew L. Pierce, Shinji Adachi, Kohei Yamauchi, Akihiko Hara, Penny Swanson, Walton W. Dickhoff

Research output: Contribution to journalArticle

64 Citations (Scopus)

Abstract

Somatolactin (SL) is a pituitary hormone of the GH/prolactin (PRL) family that so far has been found only in fish. Compared with GH and PRL, the primary structure of SL is highly conserved among divergent fish species, suggesting it has an important function and a discriminating receptor that constrains structural change. However, SL functions are poorly understood, and receptors for SL have not yet been identified. During cloning of GH receptor cDNA from salmon, we found a variant with relatively high (38-58%) sequence identity to vertebrate GH receptors and low (28-33%) identity to PRL receptors; however, the recombinant protein encoding the extracellular domain showed only weak binding of GH. Ligand binding of the recombinant extracellular domain for this receptor confirmed that the cDNA encoded a specific receptor for SL. The SL receptor (SLR) has common features of a GH receptor including FGEFS motif, six cysteine residues in the extracellular domain, a single transmembrane region, and Box 1 and 2 regions in the intracellular domain. These structural characteristics place the SLR in the cytokine receptor type I homodimeric group, which includes receptors for GH, PRL, erythropoietin, thrombopoietin, granulocyte-colony stimulating factor, and leptin. Transcripts for SLR were found in 11 tissues with highest levels in liver and fat, supporting the notion that a major function of SL is regulation of lipid metabolism. Cloning SLR cDNA opens the way for discovery of new SL functions and target tissues in fish, and perhaps novel members of this receptor family in other vertebrates.

Original languageEnglish
Pages (from-to)2354-2361
Number of pages8
JournalEndocrinology
Volume146
Issue number5
DOIs
Publication statusPublished - 2005 May
Externally publishedYes

Fingerprint

Cytokine Receptors
Salmon
Prolactin Receptors
Fishes
Complementary DNA
Prolactin
Vertebrates
Organism Cloning
Thrombopoietin
Pituitary Hormones
Granulocyte Colony-Stimulating Factor
Erythropoietin
Leptin
Lipid Metabolism
Recombinant Proteins
Cysteine
Fats
Ligands
Liver

ASJC Scopus subject areas

  • Endocrinology
  • Endocrinology, Diabetes and Metabolism

Cite this

Fukada, H., Ozaki, Y., Pierce, A. L., Adachi, S., Yamauchi, K., Hara, A., ... Dickhoff, W. W. (2005). Identification of the salmon somatolactin receptor, a new member of the cytokine receptor family. Endocrinology, 146(5), 2354-2361. https://doi.org/10.1210/en.2004-1578

Identification of the salmon somatolactin receptor, a new member of the cytokine receptor family. / Fukada, Haruhisa; Ozaki, Yuichi; Pierce, Andrew L.; Adachi, Shinji; Yamauchi, Kohei; Hara, Akihiko; Swanson, Penny; Dickhoff, Walton W.

In: Endocrinology, Vol. 146, No. 5, 05.2005, p. 2354-2361.

Research output: Contribution to journalArticle

Fukada, H, Ozaki, Y, Pierce, AL, Adachi, S, Yamauchi, K, Hara, A, Swanson, P & Dickhoff, WW 2005, 'Identification of the salmon somatolactin receptor, a new member of the cytokine receptor family', Endocrinology, vol. 146, no. 5, pp. 2354-2361. https://doi.org/10.1210/en.2004-1578
Fukada H, Ozaki Y, Pierce AL, Adachi S, Yamauchi K, Hara A et al. Identification of the salmon somatolactin receptor, a new member of the cytokine receptor family. Endocrinology. 2005 May;146(5):2354-2361. https://doi.org/10.1210/en.2004-1578
Fukada, Haruhisa ; Ozaki, Yuichi ; Pierce, Andrew L. ; Adachi, Shinji ; Yamauchi, Kohei ; Hara, Akihiko ; Swanson, Penny ; Dickhoff, Walton W. / Identification of the salmon somatolactin receptor, a new member of the cytokine receptor family. In: Endocrinology. 2005 ; Vol. 146, No. 5. pp. 2354-2361.
@article{0c3aadfdaa2e477ebe71b96dde5f2853,
title = "Identification of the salmon somatolactin receptor, a new member of the cytokine receptor family",
abstract = "Somatolactin (SL) is a pituitary hormone of the GH/prolactin (PRL) family that so far has been found only in fish. Compared with GH and PRL, the primary structure of SL is highly conserved among divergent fish species, suggesting it has an important function and a discriminating receptor that constrains structural change. However, SL functions are poorly understood, and receptors for SL have not yet been identified. During cloning of GH receptor cDNA from salmon, we found a variant with relatively high (38-58{\%}) sequence identity to vertebrate GH receptors and low (28-33{\%}) identity to PRL receptors; however, the recombinant protein encoding the extracellular domain showed only weak binding of GH. Ligand binding of the recombinant extracellular domain for this receptor confirmed that the cDNA encoded a specific receptor for SL. The SL receptor (SLR) has common features of a GH receptor including FGEFS motif, six cysteine residues in the extracellular domain, a single transmembrane region, and Box 1 and 2 regions in the intracellular domain. These structural characteristics place the SLR in the cytokine receptor type I homodimeric group, which includes receptors for GH, PRL, erythropoietin, thrombopoietin, granulocyte-colony stimulating factor, and leptin. Transcripts for SLR were found in 11 tissues with highest levels in liver and fat, supporting the notion that a major function of SL is regulation of lipid metabolism. Cloning SLR cDNA opens the way for discovery of new SL functions and target tissues in fish, and perhaps novel members of this receptor family in other vertebrates.",
author = "Haruhisa Fukada and Yuichi Ozaki and Pierce, {Andrew L.} and Shinji Adachi and Kohei Yamauchi and Akihiko Hara and Penny Swanson and Dickhoff, {Walton W.}",
year = "2005",
month = "5",
doi = "10.1210/en.2004-1578",
language = "English",
volume = "146",
pages = "2354--2361",
journal = "Endocrinology",
issn = "0013-7227",
publisher = "The Endocrine Society",
number = "5",

}

TY - JOUR

T1 - Identification of the salmon somatolactin receptor, a new member of the cytokine receptor family

AU - Fukada, Haruhisa

AU - Ozaki, Yuichi

AU - Pierce, Andrew L.

AU - Adachi, Shinji

AU - Yamauchi, Kohei

AU - Hara, Akihiko

AU - Swanson, Penny

AU - Dickhoff, Walton W.

PY - 2005/5

Y1 - 2005/5

N2 - Somatolactin (SL) is a pituitary hormone of the GH/prolactin (PRL) family that so far has been found only in fish. Compared with GH and PRL, the primary structure of SL is highly conserved among divergent fish species, suggesting it has an important function and a discriminating receptor that constrains structural change. However, SL functions are poorly understood, and receptors for SL have not yet been identified. During cloning of GH receptor cDNA from salmon, we found a variant with relatively high (38-58%) sequence identity to vertebrate GH receptors and low (28-33%) identity to PRL receptors; however, the recombinant protein encoding the extracellular domain showed only weak binding of GH. Ligand binding of the recombinant extracellular domain for this receptor confirmed that the cDNA encoded a specific receptor for SL. The SL receptor (SLR) has common features of a GH receptor including FGEFS motif, six cysteine residues in the extracellular domain, a single transmembrane region, and Box 1 and 2 regions in the intracellular domain. These structural characteristics place the SLR in the cytokine receptor type I homodimeric group, which includes receptors for GH, PRL, erythropoietin, thrombopoietin, granulocyte-colony stimulating factor, and leptin. Transcripts for SLR were found in 11 tissues with highest levels in liver and fat, supporting the notion that a major function of SL is regulation of lipid metabolism. Cloning SLR cDNA opens the way for discovery of new SL functions and target tissues in fish, and perhaps novel members of this receptor family in other vertebrates.

AB - Somatolactin (SL) is a pituitary hormone of the GH/prolactin (PRL) family that so far has been found only in fish. Compared with GH and PRL, the primary structure of SL is highly conserved among divergent fish species, suggesting it has an important function and a discriminating receptor that constrains structural change. However, SL functions are poorly understood, and receptors for SL have not yet been identified. During cloning of GH receptor cDNA from salmon, we found a variant with relatively high (38-58%) sequence identity to vertebrate GH receptors and low (28-33%) identity to PRL receptors; however, the recombinant protein encoding the extracellular domain showed only weak binding of GH. Ligand binding of the recombinant extracellular domain for this receptor confirmed that the cDNA encoded a specific receptor for SL. The SL receptor (SLR) has common features of a GH receptor including FGEFS motif, six cysteine residues in the extracellular domain, a single transmembrane region, and Box 1 and 2 regions in the intracellular domain. These structural characteristics place the SLR in the cytokine receptor type I homodimeric group, which includes receptors for GH, PRL, erythropoietin, thrombopoietin, granulocyte-colony stimulating factor, and leptin. Transcripts for SLR were found in 11 tissues with highest levels in liver and fat, supporting the notion that a major function of SL is regulation of lipid metabolism. Cloning SLR cDNA opens the way for discovery of new SL functions and target tissues in fish, and perhaps novel members of this receptor family in other vertebrates.

UR - http://www.scopus.com/inward/record.url?scp=17744392015&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=17744392015&partnerID=8YFLogxK

U2 - 10.1210/en.2004-1578

DO - 10.1210/en.2004-1578

M3 - Article

VL - 146

SP - 2354

EP - 2361

JO - Endocrinology

JF - Endocrinology

SN - 0013-7227

IS - 5

ER -