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Alterations in the Neuronal Cytoskeleton in Alzheimer Disease pp 33–44Cite as

Human Amyloidosis and In Vitro Formation of Alzheimer Amyloid Fibrils

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Part of the book series: Advances in Behavioral Biology ((ABBI,volume 34))

Abstract

Amyloidosis is a generic term that describes the chronic deposition in the extracellular and intracellular spaces of abnormal fibrillar proteins. These proteins share the properties of a β-pleated sheet secondary structure, insolubility, green birefringence after Congo red staining and the formation of fibrils with a typical electron microscopic appearance.1,2 The deposition of amyloid fibrils is the resultant of a diversity of pathological conditions, and the localization of these deposits is probably determined by tissue-related factors as well as by the type of protein involved (Table 1). Primary amyloidosis presents in 90% of the cases an M component that can be detected in serum, urine or cerebrospinal fluid.3,4 This observation and the presence of multiple myeloma in 20% of the cases, suggest that a plasma cell dysfunction plays an important role in its pathogenesis.5 The amyloid protein in primary amyloidosis has been shown to be the amino terminal fragment of immunoglobulin light chains with a variable molecular weight, ranging from 5–23 kDa.6,7 Some subgroups of light chains appear to have a highly amyloidogenic primary structure, as shown by preferential association of λVI with primary amyloidosis and the in vitro formation of amyloid fibrils from some, but not all, of the Bence Jones proteins studied.8–10 Secondary amyloidosis is related to acquired chronic inflammatory conditions such as rheumatoid arthritis, tuberculosis, leprosy, bronchiectasia, and osteomyelitis.

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Authors and Affiliations

  1. Department of Pathology, New York University Medical Center, 550 First Avenue, New York, N.Y., 10016, USA

    Eduardo M. Castaño

  2. Kaplan Cancer Center, New York University Medical Center, 550 First Avenue, New York, N.Y., 10016, USA

    Blas Frangione

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  1. Eduardo M. Castaño
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  2. Blas Frangione
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  1. Case Western Reserve University, Cleveland, Ohio, USA

    George Perry

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© 1987 Plenum Press, New York

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Castaño, E.M., Frangione, B. (1987). Human Amyloidosis and In Vitro Formation of Alzheimer Amyloid Fibrils. In: Perry, G. (eds) Alterations in the Neuronal Cytoskeleton in Alzheimer Disease. Advances in Behavioral Biology, vol 34. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1657-2_3

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