The University of Tokyo · Medicine
Professor Yutaka Osuga's research lab focuses on the immunological and molecular mechanisms underlying endometriosis, a chronic gynecological disorder affecting reproductive-age women. The lab investigates immune cell dysfunction—particularly in T cells, B cells, and natural killer cells—within the context of endometriotic lesion development and immune escape. Additionally, the lab explores hormonal signaling pathways, including gonadotropin receptor function and their role in endometriosis pathogenesis, using molecular and cellular biology approaches. The research aims to uncover novel therapeutic targets by elucidating the interplay between immune regulation, endometrial function, and hormone signaling.
Figures are computed from collected data and may differ slightly.
Endometriosis is a disease characterized by the presence of endometriotic tissue outside the uterine cavity. Although its pathogenesis remains to be elucidated, immune status is suggested to play an important role in the initiation and the progression of the disease. In particular, immune cells in lymphoid lineage that comprised T and B lymphocytes and natural killer cells play essential roles in determining either accept or reject survival, implantation, and proliferation of endometrial and end
Endometriosis is a disease that causes the health of women of reproductive age to deteriorate. The implantation theory is the most widely accepted pathogenesis of the disease, although many points remain poorly understood concerning this theory. According to this theory, regurgitated endometrial debris has to go through various sequential events for the disease to develop. Recent studies have elucidated several aspects of these events. A remarkably reduced gene expression of GnRH II and an incre
Gonadotropin receptors are unique members of the seven-transmembrane (TM), G protein-coupled receptor family with a large extracellular (EC) sequence forming the high-affinity ligand binding domain. In a patient with Leydig cell hypoplasia, we identified a mutant LH receptor that is truncated at TM5. This protein retains limited ligand binding ability but cannot mediate cAMP responses. To study interactions between receptor fragments defective in either ligand binding or signal transduction, we
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