Glycodelin in reproduction
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MINIREVIEW
Glycodelin in reproduction Hiroshi Uchida • Tetsuo Maruyama • Sayaka Nishikawa-Uchida • Kaoru Miyazaki Hirotaka Masuda • Yasunori Yoshimura
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Received: 29 December 2012 / Accepted: 16 February 2013 / Published online: 14 March 2013 Ó Japan Society for Reproductive Medicine 2013
Abstract To achieve a successful pregnancy in humans, sperm is required for capacitation, followed by binding to and entry into an oocyte. Maternal endometrial epithelial cells (EECs) prepare the appropriate implantation environment through regulation of immune cells and endometrial cells. After acquiring endometrial receptivity, a successful pregnancy consists of complex and finely regulated steps involving apposition, adhesion, invasion, and penetration. Glycodelin is a secretory glycoprotein that affects cell proliferation, differentiation, adhesion, and motility. Glycodelin has four glycoforms (glycodelin-A, -S, -F. and -C); differences in glycosylation affect each characteristic function. Glycodelin has a unique temporospatial pattern of expression, primarily in the reproductive tract where glycodelin is mid-secretory phase-dominant. Recent studies have demonstrated that glycodelin protein has the potential to regulate various processes, including immunosuppression, fertilization, and implantation. This review details the orchestrated regulation of successful pregnancy by glycodelin as well as a discussion of the basic characteristics of glycodelin. Keywords Endometrial epithelial cell Fertilization Glycodelin Implantation Sperm
Basic characteristics of glycodelin After the initial identification of glycodelin in amniotic fluid [1], glycodelin was given various names by several investigators, such as placental a2-globulin [1], chorionic a2-microglobulin, a-uterine protein, placental protein (PP14), progestogen-dependent endometrial protein (PEP), pregnancy-associated endometrial a2-globulin (a2-PEG), and progesterone-associated endometrial protein (PAEP) [2]. Currently, the Human Genome Organization uses PAEP and glycodelin as the official symbol and preferred term amongst the list of recommended names, respectively. The glycodelin gene is located at 9q34.3 and the mRNA is comprised of 7 exons. Several splicing variants of glycodelin mRNA have been reported in the female and male reproductive organs and an endometrial cell line [3–5]; however, the differentiation of physiologic functions is still unknown. Although the full length of glycodelin mRNA encodes 180 amino acids and the predicted molecular mass of glycodelin protein is about 18–19 kDa, on SDS-PAGE and Western blotting, the glycodelin band is located at 50–60 kDa, because of glycosylation modification and homodimeric action.
Temporospatial expression of glycodelin
H. Uchida (&) T. Maruyama S. Nishikawa-Uchida K. Miyazaki H. Masuda Y. Yoshimura Department of Obstetrics and Gynecology, Keio University School of Medicine, 35 Shinanomachi, Shinjuku, Tokyo 160-8582, Japan e-mail: [email protected]
Glycodelin has a limited spatial pattern of express
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