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Furin initiates gelsolin familial amyloidosis in the Golgi through a defect in Ca2+ stabilization

Academic Article
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Overview

related to degree

  • Pelletier, Mary Elizabeth Huff, Ph.D. in Chemistry, Scripps Research 1998 - 2003

authors

  • Chen, C. D.
  • Pelletier, Mary Elizabeth Huff
  • Matteson, J.
  • Page, L.
  • Phillips, R.
  • Kelly, Jeffery
  • Balch, William E.

publication date

  • November 2001

journal

  • EMBO Journal  Journal

abstract

  • Hereditary familial amyloidosis of Finnish type (FAF) leading to amyloid in the peripheral and central nervous systems stems from deposition of a 71 residue fragment generated from the D187N/Y variants of plasma gelsolin by two sequential endoproteolytic events. We identify the protease accomplishing the first cleavage as furin, a proprotein convertase. Endoproteolysis of plasma gelsolin occurs in the trans-Golgi network due to the inability of the FAF variants to bind and be stabilized by Ca(2+). Secretion and processing of the FAF variants by furin can be uncoupled by blocking the convergence of the exocytic pathway transporting plasma gelsolin and the endocytic recycling of furin. We propose that coincidence of membrane trafficking pathways contributes to the development of proteolysis-initiated amyloid disease.

subject areas

  • Amyloidosis, Familial
  • Animals
  • Calcium
  • Calorimetry
  • Cell Line
  • Cell Membrane
  • Cricetinae
  • Dose-Response Relationship, Drug
  • Endocytosis
  • Furin
  • Gelsolin
  • Genetic Variation
  • Golgi Apparatus
  • Protein Binding
  • Protein Structure, Tertiary
  • Subtilisins
  • Thermodynamics
  • Time Factors
  • Transfection
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Research

keywords

  • amyloid
  • calcium
  • familial amyloidosis of Finnish type
  • furin
  • gelsolin
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Identity

PubMed Central ID

  • PMC125307

International Standard Serial Number (ISSN)

  • 0261-4189

Digital Object Identifier (DOI)

  • 10.1093/emboj/20.22.6277

PubMed ID

  • 11707399
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Additional Document Info

start page

  • 6277

end page

  • 6287

volume

  • 20

issue

  • 22

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