Journal of Gynecology and Obstetrics
Volume 1, Issue 1, July 2013, Pages: 1-6
Received: May 28, 2013;
Published: Jun. 30, 2013
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Takuma Hayashi, Dept, of Immunology and Infectious Disease, Shinshu University Graduate School of Medicine, Asahi, Matsumoto, Nagano, Japan
Takuma Hayashi, Promoting Business using Advanced Technology, Japan Science and Technology Agency (JST), Tokyo 102-8666, Japan
Takuma Hayashi, SIGMA-Aldrich Collaboration Laboratory
Akiko Horiuchi, Horiuch Ladies Clinic, Nagano 390-0821 Japan
Kenji Sano, Dept, of Laboratory Medicine, Shinshu University Hospital, Nagano 590-8621, Japan
Gal Gur, Sigma-Aldrich Israel Ltd., Rehovot 76100, Israel
Gal Gur, SIGMA-Aldrich Collaboration Laboratory
Hiroyuki Aburatani, The Cancer System Laboratory, Research Center for Advanced Science and Technology, the University of Tokyo, Tokyo 153-9804 Japan
Tomoyuki Ichimura, Department of Obstetrics and Gynecology, Osaka City University Graduate School of Medicine, Osaka 545-8585 Japan
Nobuo Yaegashi, Department of Obstetrics and Gynecology, Tohoku University Graduate School of Medicine, Miyagi 980-8574 Japan
Yae Kanai, Pathology Division, National Cancer Center Research Institute, Tokyo 104-0045, Japan
Dorit Zharhary, Sigma-Aldrich Israel Ltd., Rehovot 76100, Israel
Dorit Zharhary, SIGMA-Aldrich Collaboration Laboratory
Susumu Tonegawa, Picower Institution and Department of Biology, Massachusetts Institute of Technology, MA 02139-4307 USA
Ikuo Konishi, Department of Obstetrics and Gynecology, Kyoto University Graduate School of Medicine, Kyoto 606-8507, Japan
Protein degradation by the ubiquitin-proteasome system is central to cell homeostasis and survival. Defects in this process are associated with diseases such as cancer and neurodegenerative disorders. The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven a subunits, and the two central rings are each formed by seven subunits. Replacement of LMPY by LMP2/i increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. LMP2/i mediates the cell survival pathway. Embryo implantation involves the invasion of placental extravillous trophoblast cells (EVTs) into the uterus. Normal human placentas or placentas from hydatidiform mole patients were collected and the expression of LMP2/i in different cell types including trophoblastic column (TC), cytotrophoblast cells (CTB) and syncytiotrophoblasts (STBs) was examined under different pathological states by pathological analysis. LMP2/i expression in TC of partial hydatidiform mole and complete hydatidiform mole placentas was higher than that in TC of normal human placentas. The overexpression of LMP2/i in trophoblast cells of hydatidiform moles may contribute to its highly invasive phenotype. LMP2/i-deficient mice reportedly exhibit uterine neoplasms, with a disease prevalence of 36% by 12 months of age. Further experiments with human and mouse uterine tissues clarified the biological significance of LMP2/i in malignant myometrium transformation and the cell cycle, which implicated LMP2/i as an anti-tumorigenic candidate. In this mini review, we covered recent insights into the molecular and cellular pathways involved in LMP2/i-mediated biological functions, with a particular focus on embryo implantation and uterine mesenchymal tumorigenesis.
The Proteasome Subunit LMP2/b1i In the Female Genital System, Journal of Gynecology and Obstetrics.
Vol. 1, No. 1,
2013, pp. 1-6.
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