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Transportation selection mechanism between nucleus and cytoplasm in the nuclear pore complex Approach from morphology

Research Project

Project/Area Number 14570012
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field General anatomy (including Histology/Embryology)
Research InstitutionNational University Corporation Tottori University

Principal Investigator

NAGURO Tomonori  National University Corporation Tottori University, Faculty of Medicine, Ass.Prof, 医学部, 助教授 (50032230)

Project Period (FY) 2002 – 2004
Project Status Completed (Fiscal Year 2004)
Budget Amount *help
¥2,900,000 (Direct Cost: ¥2,900,000)
Fiscal Year 2004: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 2003: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 2002: ¥1,600,000 (Direct Cost: ¥1,600,000)
Keywordsnuclear membrane / nuclear pore complex / fine structure / SEM / nuclear pore / three-dimensional structure
Research Abstract

All eight kinds of surfaces of nuclear membranes (four true surfaces of the outer and inner nuclear membranes, four fracture faces of the outer and inner nuclear membranes) in the rat pancreatic acinar cell were exposed by adjusting the density and the kind of fixatives and/or by controlling the density of antifreeze solution at the freeze cracking process. The exposed surfaces were ion-coated with osmium and they were investigated with high-resolution scanning electron microscope(SEM).
As the proteins consisting nuclear pore complex(NPC) were tend to disappear at the maceration treatment process with 0.1% osmium solution, the observation of the nuclear pore without proteins of NPC about 45-65 nm in diameter could be possible both from the cytoplasm side and nucleus side. The membrane surrounding the nuclear pores rose slightly like the bank, and it seemed to form a ring of about 90 nm in diameter on the true surface of inner nuclear membrane.
SEM observation from the cytoplasm side reve … More aled that eight particles consisting the cytoplasmic part of NPC were not spherical but ovoid in shape. Since these particles disappeared rather easily at the maceration treatment process, it became possible to observe the true surface of outer nuclear membrane without the particles. The surface was smooth and flat appearance, and so it seemed to remain intact. This result indicates that the particles are situated on the true surface of outer nuclear membrane having little connection with the membrane.
The size of transporting material ("central plug" or "cargo" or "cargo and transport factors") was about 25-30 nm in diameter. The central part of NPC surrounding the transporting materiel formed a central ring of about 10-35 nm in inner diameter, 45-65 nm in outer diameter. It was composed of sixteen particles. The ring like structure of about 45-65 nm in inner diameter and about 90-100 nm in outer diameter situated in the perinuclear space was also composed of sixteen particles. The both composition protein particles in the perinuclear space and in the center of nuclear pore seemed to form a ring connecting tightly to each other across the membrane probably in the form of dimmer units. Less

Report

(4 results)
  • 2004 Annual Research Report   Final Research Report Summary
  • 2003 Annual Research Report
  • 2002 Annual Research Report
  • Research Products

    (2 results)

All 2004

All Journal Article (2 results)

  • [Journal Article] Nuclear pore complex as seen with high-resolution scanning electron Microscopy2004

    • Author(s)
      Naguro T, Inaga S, Nakane H, Kameie T
    • Journal Title

      Anatomical Science International 79:(Suppl)

      Pages: 416-416

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] Nuclear pore complex as seen with high-resolution scanning electron microscopy2004

    • Author(s)
      T.Naguro
    • Journal Title

      Anatomical Science International 79(Suppl)

      Pages: 416-416

    • Related Report
      2004 Annual Research Report

URL: 

Published: 2002-04-01   Modified: 2016-04-21  

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