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Molecular Heterogeneity of Amyloid Fibril Proteins in Primary Amyloidosis

  • Tomotaka Shinoda
  • Fuyuki Kametani
  • Tatsuyuki Takenawa
  • Takashi Isobe
Chapter

Abstract

Current studies on the primary structure of amyloid fibril(AL) proteins, in primary and in myeloma associated amyloidosis, have revealed that they are derived from monoclonal immunoglobulin light(L) chains and/or their fragments which vary in size ranging from 6000 to 24000 daltons1,2. Although sequence data are limited, it is assumed that AL proteins consist of the variable (V) region of the L chains, the V region flanked by a portion of the constant (C) region, the intact L chain, or a combination of various intermediate molecular forms3. These data strongly suggest that the V domain plays more role than does the C domain in the formation of such pathological fibrils. If this is the case, question may be raised as to whether there is any association between the primary structure of the V region (i.e. subgroups) and amyloidogenicity, and whether or not there is any difference in this characteristic between two types of the L chains. However, because of the limited and rather incomplete sequence data, the questions have still been left to be answered, though several observations have recently been made to suggest that certain L chain subgroups are more amyloidogenic4,5.

Keywords

Amyloid Fibril Versus Region Primary Amyloidosis Putative Precursor Rare Amino Acid 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Tomotaka Shinoda
    • 1
    • 2
  • Fuyuki Kametani
    • 1
    • 2
  • Tatsuyuki Takenawa
    • 1
    • 2
  • Takashi Isobe
    • 1
    • 2
  1. 1.Department of ChemistryTokyo Metropolitan UniversitySetagaya-ku, Tokyo 158Japan
  2. 2.Department of MedicineKobe UniversityKobe 650Japan

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