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Research library, mechanism

The growth hormone-releasing hormone (GHRH) receptor and its peptide analogues

Growth hormone-releasing hormone is a 44-residue peptide first isolated from a human pancreatic tumour in 1982. Its pituitary receptor was cloned in 1992. Sermorelin, tesamorelin and CJC-1295 are analogues built on the sequence of the native peptide.

Written by the Peptency editorial teamLast reviewed 7 studies checked in PubMed on 5 October 2026

Research-use information. This page summarises published literature and regulator records. It is not guidance for use, not medical advice, and not a statement that any material is suitable for use in people or animals.

How was GHRH identified?

Two 1982 papers isolated a growth hormone-releasing factor from a human pancreatic tumour and determined its amino acid sequence, a 44-residue peptide amidated at the C-terminus. The synthetic replicate had full biological activity.[6],[7]

What is known about the receptor?

A pituitary-specific G-protein-coupled receptor for GHRH was cloned and expressed in human kidney cells, which bound GHRH with high affinity and produced cyclic AMP. A later review covers the receptor's signal transduction, gene expression and physiological function.[5],[4]

How do the catalog analogues differ from the native sequence?

Sermorelin is the first 29 residues of the native sequence, amidated. Tesamorelin is the full 44-residue sequence with a trans-3-hexenoyl group on Tyr1, which slowed degradation in plasma in the non-clinical paper. CJC-1295 without DAC differs from sermorelin at four positions (2, 8, 15 and 27, computed from the listed sequences); the albumin-binding form of CJC-1295 is the subject of most clinical papers.[1],[3],[2]

Which compounds in the catalog belong to this group?

GHRH(1-29) fragment, amidatedSermorelin

C149H246N44O42S, 3357.9 g/mol

GHRH(1-44) analogue, hexenoylatedTesamorelin

C221H366N72O67S, 5136 g/mol

GHRH(1-29) analogue, amidatedCJC-1295 no DAC

C152H252N44O42, 3367.9 g/mol

Research materials: Sermorelin, Tesamorelin, CJC-1295 no DAC.

Which studies are cited on this page?

  1. [1] Ferdinandi ES, Brazeau P, High K, Procter B, Fennell S, Dubreuil P. Non-clinical pharmacology and safety evaluation of TH9507, a human growth hormone-releasing factor analogue. Basic Clin Pharmacol Toxicol. 2007;100:49-58.

    Non-clinical pharmacology and safety evaluation of TH9507 (tesamorelin), a growth hormone-releasing factor analogue carrying a trans-3-hexenoyl group, including plasma stability.

    Animal studyPMID 17214611DOI 10.1111/j.1742-7843.2007.00008.x

  2. [2] Teichman SL, Neale A, Lawrence B, Gagnon C, Castaigne JP, Frohman LA. Prolonged stimulation of growth hormone (GH) and insulin-like growth factor I secretion by CJC-1295, a long-acting analog of GH-releasing hormone, in healthy adults. J Clin Endocrinol Metab. 2006;91:799-805.

    Randomised, placebo-controlled trials in healthy adults reporting pharmacokinetics, GH and IGF-I pharmacodynamics and safety of CJC-1295 (the albumin-binding form).

    Human studyPMID 16352683DOI 10.1210/jc.2005-1536

  3. [3] Jetté L, Léger R, Thibaudeau K, Benquet C, Robitaille M, Pellerin I, et al.. Human growth hormone-releasing factor (hGRF)1-29-albumin bioconjugates activate the GRF receptor on the anterior pituitary in rats: identification of CJC-1295 as a long-lasting GRF analog. Endocrinology. 2005;146:3052-8.

    Albumin bioconjugates of GRF(1-29): stability against peptidase degradation and activity at the GRF receptor in vitro and in vivo.

    ChemistryPMID 15817669DOI 10.1210/en.2004-1286

  4. [4] Mayo KE, Miller TL, DeAlmeida V, Zheng J, Godfrey PA. The growth-hormone-releasing hormone receptor: signal transduction, gene expression, and physiological function in growth regulation. Ann N Y Acad Sci. 1996;805:184-203.

    Review of GHRH receptor signal transduction, gene expression and physiological function.

    ReviewPMID 8993403DOI 10.1111/j.1749-6632.1996.tb17483.x

  5. [5] Mayo KE. Molecular cloning and expression of a pituitary-specific receptor for growth hormone-releasing hormone. Mol Endocrinol. 1992;6:1734-44.

    Cloning and expression of the pituitary GHRH receptor, with ligand binding and cAMP production in transfected cells.

    Receptor biologyPMID 1333056DOI 10.1210/mend.6.10.1333056

  6. [6] Guillemin R, Brazeau P, Böhlen P, Esch F, Ling N, Wehrenberg WB. Growth hormone-releasing factor from a human pancreatic tumor that caused acromegaly. Science. 1982;218:585-7.

    Isolation and amino-acid sequence of a 44-residue growth hormone-releasing peptide from a human pancreatic tumour, with a synthetic replicate.

    ChemistryPMID 6812220DOI 10.1126/science.6812220

  7. [7] Rivier J, Spiess J, Thorner M, Vale W. Characterization of a growth hormone-releasing factor from a human pancreatic islet tumour. Nature. 1982;300:276-8.

    Isolation and characterisation of growth hormone-releasing factor from a human pancreatic islet tumour.

    ChemistryPMID 6292724DOI 10.1038/300276a0

Data dates: citations read from PubMed 2026-10-05.