Research summary
Current published research focuses on the individual components rather than the finished blend.
GHRH means growth-hormone-releasing hormone. Its analogues and ipamorelin act through distinct receptor pathways in the component literature. Ipamorelin is a five-residue peptide. The original pharmacology study distinguished its receptor response from the GHRH pathway using antagonist comparisons in experimental models. PMID 9849822
The analytical CJC-1295 paper examined an amidated 29-residue peptide in one preparation. The plasma-degradation paper examined defined GHRH sequences and D-amino-acid substitutions. Neither is a trial of this finished blend. Different component mechanisms provide a research rationale, but do not demonstrate synergy or establish the identity of a separately supplied mixture. PMID 21204297 · PMID 2565342
CJC-1295 without DAC study
Identification of CJC-1295, a growth-hormone-releasing peptide, in an unknown pharmaceutical preparation.
Drug testing and analysis 2010
Molecular and analytical characterisation
Mass spectrometry identified an amidated 29-residue peptide in a preparation marketed as CJC-1295. The proposed sequence arose from analysis of that particular sample. The finding demonstrates how molecular identity can be examined; it does not establish the complete sequence of every material sold under the same name.
View on PubMed: Identification of CJC-1295, a growth-hormone-releasing peptide, in an unknown pharmaceutical preparation.Ipamorelin study
Ipamorelin, the first selective growth hormone secretagogue.
European journal of endocrinology 1998
Cell, rat and swine pharmacology
Ipamorelin stimulated growth-hormone release in rat pituitary cells and animal experiments. In swine comparisons, GHRP-2 and GHRP-6 raised ACTH and cortisol, while ipamorelin did not produce significant increases above the GHRH comparison. This is the basis for its relative selectivity under those conditions, rather than a guarantee of an identical hormonal profile in every model.
View on PubMed: Ipamorelin, the first selective growth hormone secretagogue.CJC-1295 without DAC study
Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma.
The Journal of clinical investigation 1989
Cellular and animal mechanistic research
D-amino-acid substitution at position 1 or 2 protected defined GHRH preparations against cleavage by DPP-IV in plasma experiments. Native and shortened GHRH fragments were readily cleaved near the N-terminus, with additional trypsin-like degradation contributing less. This explains the interest in position-2 modifications without establishing the rest of a catalogue analogue’s sequence.
View on PubMed: Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma.Models studied
- Ipamorelin component pharmacology
- CJC-1295 component identity
Key findings
GHRH-side stability
N-terminal D-amino-acid substitutions can protect GHRH preparations from DPP-IV cleavage; that mechanism does not identify all residues of a separately sold analogue.
Ipamorelin-side endocrine selectivity
Relative endocrine selectivity arose from defined animal comparisons, with GH release distinguished from ACTH and cortisol responses.
References
Identification of CJC-1295, a growth-hormone-releasing peptide, in an unknown pharmaceutical preparation.
Drug testing and analysis 2010
PMID 21204297
View on PubMed: Identification of CJC-1295, a growth-hormone-releasing peptide, in an unknown pharmaceutical preparation.Ipamorelin, the first selective growth hormone secretagogue.
European journal of endocrinology 1998
PMID 9849822
View on PubMed: Ipamorelin, the first selective growth hormone secretagogue.Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma.
The Journal of clinical investigation 1989
PMID 2565342
View on PubMed: Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma.
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