Belgian researchers have identified a protein formulation that mimics the structure and rigidity of the natural lining in a women’s ovaries, a breakthrough for women with infertility or cancer patients who had radiation or chemotherapy treatments. Findings are published in the Journal of Assisted Reproduction and Genetics.
Currently, women with cancer can opt to undergo cryopreservation of ovarian tissue so they can plan on having a family after radiation or chemotherapy. However, these procedures are not recommended for women who have a risk of malignant cells in their ovarian tissue. Researchers in this study outlined how the development of an artificial ovary with isolated follicles could provide more options for a woman to conceive.
Researchers first removed and froze ovarian tissue from a woman before cancer treatment before isolating the follicles from the tissue and encapsulating them within a scaffold of fibrin grafted from the patient.
"The ideal is that these matrixes should mimic the structure and physical properties of the human ovary in such a way that it could ideally support the growth of follicles within which the egg cell resides," explained co-author Maria Costanza Chiti.
In this study, researchers focused on the small characteristics of human tissue to gain insight into how an artificial ovary could be formed. The team collected biopsies from three women of child bearing age and compared the thickness of the layers, stiffness of the tissue and other characteristics with four differing concentration of fibrin. In testing the fibrin matrix concentrations, the protein F50/T50 was shown to closely resemble the outer layer of a human ovary in terms of ultrastructure and rigidity.
"This was done to identify the fibrin formulation that best resembles the natural milieu of the human ovary in terms of architecture, porosity and rigidity," said Chiti. "These combinations may mimic the physiological environment of human follicles more closely, making them good candidates for the artificial ovary prototype. Such findings are essential to help us standardize fibrin matrix architecture.