Section 1
The Growth Hormone Axis
Tesamorelin
SUBQ SKU available · GHRH analog · 44-aa peptide
What it is: A synthetic analog of Growth Hormone-Releasing Hormone (GHRH), a 44-amino-acid peptide that signals the pituitary to release growth hormone.
Mechanism: Binds to GHRH receptors on pituitary somatotrophs, stimulating endogenous GH secretion in a pulsatile pattern that mimics natural physiology.
Research focus: Visceral adipose tissue reduction, body composition, cognition in aging populations.
Key findings: A 2010 NEJM study (Falutz et al.) demonstrated significant reduction in visceral adipose tissue in HIV-associated lipodystrophy with daily subcutaneous administration over 26 weeks. Subsequent NIH-funded research (Stanley et al., 2014) examined cognitive and cardiometabolic markers in the same population.
How researchers approach it: Daily subcutaneous, evening administration to align with natural GH pulse, multi-week study windows. The compound is FDA-approved as Egrifta for a specific clinical indication.
Considerations: GHRH-class compounds increase IGF-1; long-term IGF-1 elevation is a research consideration in any GH-axis investigation.
Citations
- Falutz J, et al. NEJM 2010;363:1108-1117. "Effects of tesamorelin on visceral fat and abdominal contour in HIV-associated lipodystrophy."
- Stanley TL, et al. J Clin Endocrinol Metab 2014;99(6):2073-2081. "Effect of tesamorelin on visceral adiposity and cardiometabolic risk."
Sermorelin
GHRH 1-29 fragment · short-acting
What it is: A 29-amino-acid fragment of GHRH (the biologically active portion).
Mechanism: Same GHRH-receptor agonism as Tesamorelin, but with a shorter half-life (~10-20 minutes), producing a single pulse of GH release rather than sustained stimulation.
Research focus: Pediatric growth hormone deficiency (its original FDA indication, marketed as Geref), age-related GH decline, sleep architecture.
Key findings: Vittone et al. (1997, Metabolism) examined GH and IGF-1 response in older adults; Khorram et al. (1997) studied immune and body composition markers in an aging cohort.
How researchers approach it: Subcutaneous administration, often pre-sleep to coincide with the body's natural nocturnal GH pulse.
Considerations: Shorter-acting than Tesamorelin; combined with a GHRP for synergistic study design is common in the literature.
Citations
- Vittone J, et al. Metabolism 1997;46(1):89-96.
- Khorram O, et al. J Clin Endocrinol Metab 1997;82(5):1472-1479.
Ipamorelin
SUBQ SKU available · Selective GHRP · pentapeptide
What it is: A pentapeptide growth hormone secretagogue (GHRP-class).
Mechanism: Selective agonist of the ghrelin receptor (GHS-R1a) on pituitary somatotrophs. Unlike older GHRPs (GHRP-2, GHRP-6), it does not significantly affect cortisol or prolactin in published research.
Research focus: Selective GH release without off-target endocrine activation; postoperative ileus in clinical trials.
Key findings: Raun et al. (1998, Eur J Endocrinol) characterized its receptor selectivity profile. Multiple Phase II clinical trials have investigated postoperative gastrointestinal recovery.
How researchers approach it: Subcutaneous, often paired with a GHRH (Sermorelin or Tesamorelin) in research designs that aim to model both arms of natural GH regulation.
Considerations: Receptor selectivity is the defining property — research interest centers on whether this selectivity translates to a different long-term profile than older GHRPs.
Citations
- Raun K, et al. Eur J Endocrinol 1998;139(5):552-561. "Ipamorelin, the first selective growth hormone secretagogue."
IGF-1 LR3
SUBQ SKU available · Long R3 IGF-1 analog
What it is: Long R3 IGF-1 — a recombinant analog of Insulin-Like Growth Factor 1, the primary downstream mediator of growth hormone action. The "Long R3" modification extends half-life and reduces binding to IGF-binding proteins.
Mechanism: Direct activation of IGF-1 receptors on tissue, bypassing the GH → liver → IGF-1 cascade.
Research focus: Skeletal muscle hypertrophy, satellite cell activation, neuronal survival research.
Key findings: Bell et al. (1995) characterized the binding-protein evasion of LR3 vs native IGF-1. Coleman et al. (1995, J Biol Chem) examined skeletal muscle effects in transgenic IGF-1 models.
How researchers approach it: Subcutaneous, typically peri-workout in studies investigating muscle protein synthesis kinetics.
Considerations: IGF-1 is a potent mitogen — long-term IGF-1 elevation is an active area of research scrutiny. Hypoglycemia risk is documented in higher-dose research designs.
Citations
- Bell GI, et al. Nucleic Acids Res 1986;14:7873-7882.
- Coleman ME, et al. J Biol Chem 1995;270:12109-12116.