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The Proteasome Subunit LMP2/b1i In the Female Genital System

Received: 28 May 2013     Published: 30 June 2013
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Abstract

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.

Published in Journal of Gynecology and Obstetrics (Volume 1, Issue 1)
DOI 10.11648/j.jgo.20130101.11
Page(s) 1-6
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This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.

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Copyright © The Author(s), 2013. Published by Science Publishing Group

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Keywords

LMP2/b1i, Implantation, Trophoblast, Leiomyosarcoma, Leiomyoma

References
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Cite This Article
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    Takuma Hayashi, Takuma Hayashi, Takuma Hayashi, Akiko Horiuchi, Kenji Sano, et al. (2013). The Proteasome Subunit LMP2/b1i In the Female Genital System. Journal of Gynecology and Obstetrics, 1(1), 1-6. https://doi.org/10.11648/j.jgo.20130101.11

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    ACS Style

    Takuma Hayashi; Takuma Hayashi; Takuma Hayashi; Akiko Horiuchi; Kenji Sano, et al. The Proteasome Subunit LMP2/b1i In the Female Genital System. J. Gynecol. Obstet. 2013, 1(1), 1-6. doi: 10.11648/j.jgo.20130101.11

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    AMA Style

    Takuma Hayashi, Takuma Hayashi, Takuma Hayashi, Akiko Horiuchi, Kenji Sano, et al. The Proteasome Subunit LMP2/b1i In the Female Genital System. J Gynecol Obstet. 2013;1(1):1-6. doi: 10.11648/j.jgo.20130101.11

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  • @article{10.11648/j.jgo.20130101.11,
      author = {Takuma Hayashi and Takuma Hayashi and Takuma Hayashi and Akiko Horiuchi and Kenji Sano and Gal Gur and Gal Gur and Hiroyuki Aburatani and Tomoyuki Ichimura and Nobuo Yaegashi and Yae Kanai and Dorit Zharhary and Dorit Zharhary and Susumu Tonegawa and Ikuo Konishi},
      title = {The Proteasome Subunit LMP2/b1i In the Female Genital System},
      journal = {Journal of Gynecology and Obstetrics},
      volume = {1},
      number = {1},
      pages = {1-6},
      doi = {10.11648/j.jgo.20130101.11},
      url = {https://doi.org/10.11648/j.jgo.20130101.11},
      eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.jgo.20130101.11},
      abstract = {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.},
     year = {2013}
    }
    

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    AU  - Takuma Hayashi
    AU  - Takuma Hayashi
    AU  - Takuma Hayashi
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    AU  - Kenji Sano
    AU  - Gal Gur
    AU  - Gal Gur
    AU  - Hiroyuki Aburatani
    AU  - Tomoyuki Ichimura
    AU  - Nobuo Yaegashi
    AU  - Yae Kanai
    AU  - Dorit Zharhary
    AU  - Dorit Zharhary
    AU  - Susumu Tonegawa
    AU  - Ikuo Konishi
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    DO  - 10.11648/j.jgo.20130101.11
    T2  - Journal of Gynecology and Obstetrics
    JF  - Journal of Gynecology and Obstetrics
    JO  - Journal of Gynecology and Obstetrics
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    AB  - 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.
    VL  - 1
    IS  - 1
    ER  - 

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Author Information
  • Dept, of Immunology and Infectious Disease, Shinshu University Graduate School of Medicine, Asahi, Matsumoto, Nagano, Japan

  • Dept, of Immunology and Infectious Disease, Shinshu University Graduate School of Medicine, Asahi, Matsumoto, Nagano, Japan

  • Dept, of Immunology and Infectious Disease, Shinshu University Graduate School of Medicine, Asahi, Matsumoto, Nagano, Japan

  • Horiuch Ladies Clinic, Nagano 390-0821 Japan

  • Dept, of Laboratory Medicine, Shinshu University Hospital, Nagano 590-8621, Japan

  • Sigma-Aldrich Israel Ltd., Rehovot 76100, Israel

  • Sigma-Aldrich Israel Ltd., Rehovot 76100, Israel

  • The Cancer System Laboratory, Research Center for Advanced Science and Technology, the University of Tokyo, Tokyo 153-9804 Japan

  • Department of Obstetrics and Gynecology, Osaka City University Graduate School of Medicine, Osaka 545-8585 Japan

  • Department of Obstetrics and Gynecology, Tohoku University Graduate School of Medicine, Miyagi 980-8574 Japan

  • Pathology Division, National Cancer Center Research Institute, Tokyo 104-0045, Japan

  • Sigma-Aldrich Israel Ltd., Rehovot 76100, Israel

  • Sigma-Aldrich Israel Ltd., Rehovot 76100, Israel

  • Picower Institution and Department of Biology, Massachusetts Institute of Technology, MA 02139-4307 USA

  • Department of Obstetrics and Gynecology, Kyoto University Graduate School of Medicine, Kyoto 606-8507, Japan

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