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Molecular Endocrinology 11 (4): 415-423
Copyright © 1997 by The Endocrine Society

Molecular Analysis of Rat Pituitary and Hypothalamic Growth Hormone Secretagogue Receptors

Karen Kulju McKee, Oksana C. Palyha, Scott D. Feighner, Donna L. Hreniuk, Carina P. Tan, Michael S. Phillips, Roy G. Smith, Lex H. T. Van der Ploeg and Andrew D. Howard

Department of Biochemistry and Physiology (K.K.M., O.C.P., S.D.F., D.L.H., C.P.T., R.G.S., L.H.T.VdP., A.D.H.) Merck Research Laboratories Rahway, New Jersey 07065
Department of Human Genetics (M.S.P.) Merck Research Laboratories West Point, Pennsylvania 19486

GH release is thought to occur under the reciprocal regulation of two hypothalamic peptides, GH releasing hormone (GHRH) and somatostatin, via their engagement with specific cell surface receptors on the anterior pituitary somatotroph. In addition, GH-releasing peptides, such as GHRP-6 and the nonpeptide mimetics, L-692,429 and MK-0677, stimulate GH release through their activation of a distinct receptor, the GH secretagogue receptor (GHS-R). The recent cloning of the GHS-R from human and swine pituitary gland identifies yet a third G protein-coupled receptor (GPC-R) involved in the control of GH release and further supports the existence of an undiscovered hormone that may activate this receptor. Using the human GHS-R as a probe, we report the isolation of a rat pituitary GHS-R cDNA derived from an unspliced, precursor mRNA. The rat cDNA encodes a protein of 364 amino acids containing seven transmembrane domains (7-TM) with >90% sequence identity to both the human and swine GHS-Rs. A single intron of ~2 kb divides the open reading frame into two exons encoding TM 1–5 and TM 6–7, thus placing the GHS-R into the intron-containing class of GPC-Rs. The intron maps to the site of sequence divergence between the human and swine type 1a and 1b GHS-R mRNAs. In addition, determination of the nucleotide sequence for the human GHS-R gene confirmed the position of an intron in the human GHS-R gene at this position. A full-length contiguous cDNA from rat hypothalamus was isolated and shown to be identical in its nucleotide and deduced amino acid sequence to the rat pituitary GHS-R. The cloned rat GHS-R binds [35S]MK-0677 with high affinity [dissociation constant (KD) = 0.7 nM] and is functionally active when expressed in HEK-293 cells. Expression of the rat GHS-R was observed specifically in the pituitary and hypothalamus when compared with control tissues.




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Endocrinology, November 1, 1997; 138(11): 4552 - 4557.
[Abstract] [Full Text] [PDF]

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 Mol. Endocrinol.Home page
H. Zheng, A. Bailey, M.-H. Jiang, K. Honda, H. Y. Chen, M. E. Trumbauer, L. H.T. Van der Ploeg, J. M. Schaeffer, G. Leng, and R. G. Smith
Somatostatin Receptor Subtype 2 Knockout Mice Are Refractory to Growth Hormone-Negative Feedback on Arcuate Neurons
Mol. Endocrinol., October 1, 1997; 11(11): 1709 - 1717.
[Abstract] [Full Text]

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H. Hosoda, M. Kojima, H. Matsuo, and K. Kangawa
Purification and Characterization of Rat des-Gln14-Ghrelin, a Second Endogenous Ligand for the Growth Hormone Secretagogue Receptor
J. Biol. Chem., July 14, 2000; 275(29): 21995 - 22000.
[Abstract] [Full Text] [PDF]

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H. Kaiya, M. Kojima, H. Hosoda, A. Koda, K. Yamamoto, Y. Kitajima, M. Matsumoto, Y. Minamitake, S. Kikuyama, and K. Kangawa
Bullfrog Ghrelin Is Modified by n-Octanoic Acid at Its Third Threonine Residue
J. Biol. Chem., October 26, 2001; 276(44): 40441 - 40448.
[Abstract] [Full Text] [PDF]

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V. Bodart, M. Febbraio, A. Demers, N. McNicoll, P. Pohankova, A. Perreault, T. Sejlitz, E. Escher, R.L. Silverstein, D. Lamontagne, et al.
CD36 Mediates the Cardiovascular Action of Growth Hormone-Releasing Peptides in the Heart
Circ. Res., May 3, 2002; 90(8): 844 - 849.
[Abstract] [Full Text] [PDF]


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