ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2024
Characterization of the molecular mechanisms that govern anti-Müllerian hormone synthesis and activity.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- The role of anti-Müllerian hormone as a therapeutic agent to preserve the ovarian follicle pool during chemotherapy.Journal of assisted reproduction and genetics · 2026Review
- Enhancing anti-Müllerian hormone processing reduces preantral follicle survival but spares female reproduction in mice.Endocrinology · 2026Article
- Molecular Mechanism Analysis of the Activation of Human Olfactory Receptor OR9Q2 by 4-Methylphenol.Foods (Basel, Switzerland) · 2025Article
- Anti-Müllerian hormone binds heat shock protein glucose-regulated protein 78 in human follicular fluid.Journal of assisted reproduction and genetics · 2025Article
- Gene therapy with feline anti-Müllerian hormone analogs disrupts folliculogenesis and induces pregnancy loss in female domestic cats.Nature communications · 2025Article
- A divergent two-domain structure of the anti-Müllerian hormone prodomain.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural Basis of Non-Latent Signaling by the Anti-Müllerian Hormone Procomplex.bioRxiv : the preprint server for biology · 2024Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
The roles of anti-Müllerian hormone (AMH) continue to expand, from its discovery as a critical factor in sex determination, through its identification as a regulator of ovarian folliculogenesis, its use in fertility clinics as a measure of ovarian reserve, and its emerging role in hypothalamic-pituitary function. In light of these actions, AMH is considered an attractive therapeutic target to address diverse reproductive needs, including fertility preservation. Here, we set out to characterize the molecular mechanisms that govern AMH synthesis and activity. First, we enhanced the processing of the AMH precursor to >90% by introducing more efficient proprotein convertase cleavage sites (RKKR or ISSRKKRSVSS [SCUT]). Importantly, enhanced processing corresponded with a dramatic increase in secreted AMH activity. Next, based on species differences across the AMH type II receptor-binding interface, we generated a series of human AMH variants and assessed bioactivity. AMH
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