Human menopausal gonadotropin (hMG), also called menotropins, is a gonadotropin preparation that carries both follicle-stimulating hormone (FSH) and luteinizing hormone (LH) activity. It was originally purified from the urine of postmenopausal women, whose pituitary output of both hormones is high, and it was one of the first sources of human gonadotropins available in quantity.
For laboratory work, hMG is useful precisely because it is a mixture. It lets researchers stimulate two receptors at once and study how FSH and LH signals cooperate in the ovary and testis. The sections below cover its history, the two receptors it acts on, the main experimental systems, and the limits that come with a biologically sourced, variable preparation.
At a glance
- Class: Glycoprotein hormone mixture with FSH and LH activity
- Origin: Purified from the urine of postmenopausal women and developed into a standardized preparation in the mid-twentieth century
- Structure: FSH and LH are each alpha/beta heterodimers sharing a common 92-residue alpha subunit; individual hormones are roughly 30–35 kDa; CAS 61489-71-2
- Main research areas: follicle culture, granulosa and theca cell steroidogenesis, FSH and LH receptor signaling, gonadotropin glycoform analysis
- Regulatory status: Menotropins are the active ingredient of FDA-approved prescription drug products; the material sold here is a research reagent; LH is listed by WADA under S2, prohibited in males
Structure and origin
Early gonadotropin research relied on whatever biological sources could be collected: animal and human pituitaries, pregnant mare serum, placenta and urine. Bruno Lunenfeld, one of the researchers involved, has described how gonadotropin extracted from postmenopausal urine was developed into a usable preparation and how purification improved over the following decades (Lunenfeld, 2004). Urine from postmenopausal women was attractive because, without ovarian feedback, the pituitary releases large amounts of both FSH and LH.
Chemically, hMG is not one molecule. FSH and LH share the same alpha subunit and differ in their hormone-specific beta subunits, which determine which receptor each binds. Both carry N-linked glycans whose branching and sialic acid content vary, and those glycans affect half-life and receptor activity. The ratio of FSH to LH activity, and the glycoform mix of each, depend on the source material and the purification process.
Mechanism: what the research shows
The two components act at two different receptors. FSH binds the FSH receptor (FSHR) on ovarian granulosa cells and testicular Sertoli cells. LH binds the LH/choriogonadotropin receptor (LHCGR) on theca, luteal and Leydig cells. Both are class A G protein-coupled receptors with large leucine-rich extracellular domains, and both signal mainly through Gs, cAMP and protein kinase A (Ascoli et al., 2002).
The structural basis of hormone recognition was clarified when Fan and Hendrickson solved the crystal structure of FSH bound to the hormone-binding portion of its receptor’s ectodomain. The hormone sat against the curved inner face of the leucine-rich repeats, with both the alpha and beta subunits making contact, which helps explain why the shared alpha subunit still contributes to binding while the beta subunit confers specificity (Fan & Hendrickson, 2005).
Key areas of study
Two cells, two gonadotropins
The classic reason to use combined FSH and LH activity is the two-cell model of ovarian estrogen synthesis. LH acting on theca cells drives androgen production, and FSH acting on neighboring granulosa cells induces aromatase, which converts those androgens to estrogens. Because neither hormone alone completes the pathway, follicle and co-culture systems that model it often use hMG or defined FSH plus LH. LHCGR biology underlying the theca side of the model is reviewed in detail by Ascoli and colleagues (Ascoli et al., 2002).
Follicle and oocyte culture
In-vitro growth of isolated rodent and other mammalian follicles, and oocyte maturation studies, use gonadotropin supplementation to support antral development and steroid output. hMG offers both activities in a single reagent, which simplifies early experimental designs, while defined recombinant hormones are used when each signal must be controlled separately.
LH-type signaling
Interest in the LH component has grown with evidence that LH and hCG, both LHCGR agonists, do not signal identically. In granulosa-lutein cells and transfected lines, LH favored ERK1/2 and AKT activation while hCG was the stronger activator of cAMP and progesterone production (Casarini et al., 2012). That finding matters for interpreting experiments with any preparation in which LH-type activity comes from more than one source.
Comparative and analytical work
Urinary-derived mixtures are compared with recombinant FSH and LH for glycoform profile, isoform charge distribution and receptor activity. These studies use isoelectric focusing, lectin binding, mass spectrometry and immunoassays, and they have shaped how gonadotropin potency is defined and measured.
What the evidence does not show
Because hMG is a biologically sourced mixture, its FSH:LH ratio and glycoform composition can differ from batch to batch and from one manufacturer to another. Activity is defined by bioassay rather than by mass, and findings obtained with one preparation may not reproduce with another. In cell and follicle culture, it can be hard to assign an effect to FSH or LH without defined recombinant hormones or receptor-selective tools. Data from rodent tissues do not always carry over to other species, given known species differences in gonadotropin-receptor pairing. hMG has a long clinical history, but none of that work describes the research material sold here.
Regulatory status
Menotropins are the active ingredient of FDA-approved prescription drug products in pharmaceutical form. Luteinizing hormone, one of its components, is listed by the World Anti-Doping Agency under S2 (peptide hormones), prohibited in males. The material offered by Rogue Compounds is a research reagent, not an approved drug product, and is not for human or veterinary use.
Handling and storage in the lab
Lyophilized hMG should be kept sealed and refrigerated at 2–8°C (36–46°F), protected from light. Keep the vial closed until use to limit exposure to moisture.
Sourcing and documentation
HMG is out of stock while its batch is tested by an independent, ISO 17025 accredited U.S. laboratory. Once it passes, the batch COA will be posted on the product page and in the COA Library, and each vial will carry a batch number and a QR code that opens the lab’s own report for that batch.
References
- Lunenfeld B. Historical perspectives in gonadotrophin therapy. Hum Reprod Update. 2004;10(6):453-467. PMID 15388674
- Fan QR, Hendrickson WA. Structure of human follicle-stimulating hormone in complex with its receptor. Nature. 2005;433(7023):269-277. PMID 15662415
- Ascoli M, Fanelli F, Segaloff DL. The lutropin/choriogonadotropin receptor, a 2002 perspective. Endocr Rev. 2002;23(2):141-174. PMID 11943741
- Casarini L, et al. LH and hCG action on the same receptor results in quantitatively and qualitatively different intracellular signalling. PLoS One. 2012;7(10):e46682. PMID 23071612
Research use only. Rogue Compounds products are sold strictly for laboratory research. They are not for human or veterinary use, and nothing in this article is medical advice. The studies cited here describe published research, not this product or any use of it.