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February 8, 2026Molecules0 citationsOpen Access

Fatty Acid Amide Hydrolase Signaling and Ovarian Disorders: From Molecular Mechanism to Clinical Significance

QLQinghe LinZZZhenghong ZhangDWDefan Wang

Key Points

  • To examine the role of FAAH in female reproductive physiology and its implications in ovarian disorders.
  • Reviewed literature connecting FAAH to ovarian processes.
  • Discussed biochemical properties and distribution of FAAH in ovarian tissues.
  • Analyzed evidence of FAAH involvement in disorders like PCOS and infertility.
  • FAAH regulates anandamide levels, impacting follicular development and hormone synthesis.
  • Altered FAAH activity is linked to conditions such as PCOS and infertility.
  • FAAH presents as a potential target for therapies in reproductive medicine.

Abstract

Fatty acid amide hydrolase (FAAH) is a central component of the endocannabinoid system (ECS), where it primarily regulates intracellular levels of anandamide (AEA) through enzymatic hydrolysis. Although FAAH has been extensively studied in neural and immune contexts, its involvement in female reproductive physiology is receiving increasing attention. Accumulating evidence indicates that FAAH participates in several important ovarian processes, including follicular development, steroid hormone synthesis, ovulation, and luteal function. In this review, we outline the biochemical properties of FAAH and its spatial distribution in ovarian tissues, with a particular focus on how FAAH-mediated AEA metabolism contributes to intraovarian signaling. Furthermore, we highlight the potential implications of altered FAAH activity in ovarian disorders such as polycystic ovary syndrome (PCOS), premature ovarian insufficiency (POI), and infertility. By integrating molecular observations with clinical findings, this work provides updated perspectives on FAAH as both a physiological regulator and a potential therapeutic target in reproductive medicine.

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Cite This Study

Lin et al. (2026) studied this question.

synapsesocial.com/papers/698828990fc35cd7a88482b5https://doi.org/10.3390/molecules31030556
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