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Amyloidosis

  • Book
  • © 1986

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Editors:
  1. George G. Glenner

    1. University of California, San Diego La Jolla, USA

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  2. Elliott F. Osserman

    1. Columbia University, New York, USA

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  3. Earl P. Benditt

    1. University of Washington, Seattle, USA

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  4. Evan Calkins

    1. State University of New York at Buffalo, Buffalo, USA

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  5. Alan S. Cohen

    1. Boston University School of Medicine, Boston, USA

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  6. Dorothea Zucker-Franklin

    1. New York University School of Medicine, New York, USA

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Table of contents (103 chapters)

  1. Front Matter

    Pages i-xvii
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  2. SAA, AA, and AP Proteins

    1. Front Matter

      Pages 1-1
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    2. Protein AA and Associated Proteins in Type-AA Amyloid Substance

      • Nils Eriksen, Earl P. Benditt
      Pages 3-10

    3. Heterogeneity of Human Amyloid Protein AA and SAA

      • B. Skogen, K. Sletten, T. Lea, J. B. Natvig
      Pages 11-18

    4. Vascular AA Amyloidosis is Characterized by Special Protein AA Subspecies

      • Per Westermark, Gunilla T. Nilsson
      Pages 19-26

    5. The Physico-Chemical, Antigenic, and Functional Heterogeneity of Human Serum Amyloid A

      • M. E. Martin, C. J. Rosenthal, A. Huq
      Pages 27-38

    6. Reaggregation of Bovine Amyloid a Fibril Components to β-Pleated Sheet Fibrillar Structures

      • A. C. J. van Andel, P. R. Hol, J. H. van der Maas, E. T. G. Lutz, H. Krabbendam, E. Gruys
      Pages 39-48

    7. Analysis of X-Ray Scattering by Human AA Fibrils Using Secondary Structure Predictions of Human SAA1

      • W. G. Turnell, R. Sarra, I. D. Glover, J. O. Baum, D. Caspi, M. L. Baltz et al.
      Pages 49-55

    8. Characterization of Two Distinct Serum Amyloid A Gene Products Defined by Their Complementary DNAs

      • J. D. Sipe, P. Woo, G. Goldberger, A. S. Cohen, A. S. Whitehead
      Pages 57-60

    9. Human Serum Amyloid Genes — Molecular Characterization

      • George H. Sack Jr., John J. Lease
      Pages 61-68

    10. Kinetics of Human Serum Amyloid A

      • C. J. Rosenthal, N. Solomon, M. E. Martin
      Pages 69-77

    11. Ultrastructural Identification of AA-Type Amyloid Fibrils Using Polyclonal and Monoclonal Antibodies

      • Reinhold P. Linke, Dieter Huhn
      Pages 79-85

    12. Human Serum Amyloid P-Component (SAP) as an Acute Phase Reactant in the Female

      • Shunsuke Migita, Shigeru Hashimototo, Haruo Hisazumi, Mine Harada, Hiroaki Okabe
      Pages 87-97

  3. Experimental Models

    1. Front Matter

      Pages 99-99
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    2. Pathogenetic Mechanisms and Precursor Product Relationships in Murine Amyloidosis

      • M. L. Baltz, D. Caspi, I. F. Rowe, C. R. K. Hind, D. J. Evans, M. B. Pepys
      Pages 101-108

    3. A Possible Effect of Oral Tolerance in Casein Induced Murine Amyloidosis?

      • Ronald I. Carr, Judith Katilus, D. Petty
      Pages 109-113

    4. Isolation and Characterization of Amyloid Enhancing Factor (AEF)

      • M. L. Baltz, D. Caspi, C. R. K. Hind, A. Feinstein, M. B. Pepys
      Pages 115-121

    5. Enhancement of Amyloid Degradation by Ascorbic Acid: In Vivo Evidence in a Murine Model

      • M. Ravid, B. Chen, I. Kedar
      Pages 123-127

    6. Effect of Colchicine on the Acute Phase Serum Amyloid a Protein Response and Splenic Amyloid Deposition During Experimental Murine Inflammation

      • Sydney R. Brandwein, J. D. Sipe, Martha Skinner, Alan S. Cohen
      Pages 129-137

    7. Serum Amyloid A Protein (SAA) from Mink, Horse, and Man: A Comparative Study

      • G. Marhaug, A. Husebekk, G. Husby, K. Sletten, A. L. Børresen, B. Lium et al.
      Pages 139-147
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Keywords

About this book

From a process that from the days of Vir chow and Rokitansky, primarily stimulated the relatively narrow interest of pathologists, amyloidosis has risen full-blown as one of the most important of disease complexes. Its presence dominat:es the lesions of Alzheimer's disease, a disease affecting an estimated 2. 5 million people in the U. S. A. and thereby closely rivaling stroke as the third most common cause of death. If, as it has been de­ scribed, Alzheimer's disease is the "Disease of the Century," then amy­ loidosis is the Disease Complex of the Ages. It affects in one or more of its manifestations every organ of the body, and is at least as old as the afflicted Egyptian mummies of the pyramids. With an increasing percentage of older individuals amyloid of the senior population becomes increasingly more frequent. The subjects covered in this Symposium range through almost every clinical medical specialty. From an average of one paper in each of the past three Symposiums, the explosive interest in cerebral amyloidosis has led to the presentation of 12 papers on this subject in the present volume. The genetically predisposed familial amyloidotic processes, such as the polyneuropathies and familial Mediterranean fever have also stimulated ex­ tensive and intriguing investigations which have revealed the striking effect of a single amino acid substitution in transforming a normal protein into. a lethal "amyloidogenic" one.

Editors and Affiliations

  • University of California, San Diego La Jolla, USA

    George G. Glenner

  • Columbia University, New York, USA

    Elliott F. Osserman

  • University of Washington, Seattle, USA

    Earl P. Benditt

  • State University of New York at Buffalo, Buffalo, USA

    Evan Calkins

  • Boston University School of Medicine, Boston, USA

    Alan S. Cohen

  • New York University School of Medicine, New York, USA

    Dorothea Zucker-Franklin

Bibliographic Information

  • Book Title: Amyloidosis

  • Editors: George G. Glenner, Elliott F. Osserman, Earl P. Benditt, Evan Calkins, Alan S. Cohen, Dorothea Zucker-Franklin

  • DOI: https://doi.org/10.1007/978-1-4613-2199-6

  • Publisher: Springer New York, NY

  • eBook Packages: Springer Book Archive

  • Copyright Information: Plenum Press, New York 1986

  • Softcover ISBN: 978-1-4612-9292-0Published: 22 October 2011

  • eBook ISBN: 978-1-4613-2199-6Published: 06 December 2012

  • Edition Number: 1

  • Number of Pages: XVIII, 858

  • Topics: Psychiatry

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