Study Question: Do antral follicle dynamics change in women with obesity and regular ovulatory cycles after a 6-month hypocaloric dietary intervention?
Summary Answer: After a 6-month hypocaloric dietary intervention, women with obesity and regular ovulatory cycles displayed evidence of improved antral follicle dynamics defined by the emergence of more dominant follicles, larger ovulatory follicle diameter at selection, and increased luteal progesterone concentrations compared to pre-intervention.
What Is Known Already: Precise events in antral folliculogenesis must occur in order for natural and regular monthly ovulation. In healthy women of reproductive age, antral follicles are recruited for growth in a wave-like fashion, wherein a subset of follicles are selected for preferential growth, and typically, one dominant follicle culminates in ovulation.
Background: Polycystic ovary morphology (PCOM) on ultrasonography is considered as a cardinal feature of polycystic ovarian syndrome (PCOS). Its relevance as a diagnostic criterion for PCOS was reaffirmed in the most recent International Evidence-Based Guideline for the Assessment and Management of PCOS. However, there remains a lack of clarity regarding the best practices and specific ultrasonographic markers to define PCOM.
View Article and Find Full Text PDFObesity negatively impacts reproductive health, including ovarian function. Obesity has been posited to alter Anti-Müllerian hormone (AMH) production. Understanding biological factors that could impact AMH levels is necessary given the increasing use of AMH for predicting reproductive health outcomes in response to controlled ovarian stimulation, diagnosing ovulatory disorders, onset of menopause, and natural conception.
View Article and Find Full Text PDFContext: The mechanism of oligo-anovulation in polycystic ovary syndrome (PCOS) is unknown.
Objectives: To evaluate follicular and endocrine characteristics of anovulatory and sporadic ovulatory cycles in women with PCOS.
Design: Prospective, longitudinal study.
The α-helix is the most commonly found natural secondary structure in proteins and is intrinsic to many protein-protein interactions involved in important biological functions. Novel peptides designed to mimic helices found in nature employ a variety of methods to control their structure. These approaches are significant due to potential applications in developing new therapeutic agents and materials.
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