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Possible Derivation of Cutaneous Amyloid from Degenerating Collagen Fibers: Ultrastructural, Immunohistological Studies Employing Anticollagen Antibodies

  • M. Ishii
  • K. Fukai
  • M. Chanoki
  • H. Kobayashi
  • T. Hamada
  • Y. Muragaki
  • A. Ooshima
Chapter

Abstract

It has been suggested for some years that the cutaneous fibroblasts are the most probable sythesizer in the primary cutaneous amyloidoses(1, 2,3,4,5). However, nowadays, increasing number of investigators have suggested that amyloid in the primary cutaneous amyloidoses originates from necrotizing keratinocytes(6,7,8,9,10). Black & Wilson Jones (6) first reported this possibility from the light microscopic observation. This view has been supported by the reports of ‘colloid-amyloid body’ as the possible precursor amyloid (7) and positive reaction of amyloid with antikeratin antibodies using immunofluorescence microscopy and immunoelectron microscopy (8,9). Investigations employed several monoclonal anti-keratin antibodies were performed by Eto et al. (10) and they observed only one of them reacts with cutaneous amyloid in the primary cutaneous amyloidoses. However, several unsolved questions for this theory might be pointed out. In the monoclonal experiments, several antibodies which reacted with whole epidermis could not: react with amyloid masses and it is unclear how the significant ‘colloid-amyloid body’ were stained with these monoclonal antibodies which were positive for colloid bodies whereas negative for amyloid. It is also difficult to explain why many colloid bodies which are frequently observed in the cutaneous disorders,for example, lichen planus or discoid lupus erythematosus do rot change into amyloid masses. In addition, we and Noren et al. (11,12) have reported that in some cases of primary cutaneous amyloidoses, anti-keratin investigation is negative for amyloid deposition.

Keywords

Discoid Lupus Erythematosus Collagen Antibody Conventional Electron Microscopy Antikeratin Antibody Lichen Amyloidosus 
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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References

  1. 1.
    K. Hashimoto, B.G. Gross, and W. Lever, Lichen amyloidosus: Histo-chemical and electron microscopic studies. J. Invest. Dermatol. 45: 204 (1965).Google Scholar
  2. 2.
    O.E. Rodermund and G. Klingmüller, Zur submikroskopischen Struktur des Amyloid. Arch. klin. experiment. Dermatol. 236: 147 (1970).Google Scholar
  3. 3.
    L. Shapiro, A.K. Kurban and H.A. Azar, Lichen amyloidosus.: A histo-chemical and electron microscopic study. Arch Pathol. 90: 499 (1970).Google Scholar
  4. 4.
    K. Hashimoto and L.E. King, Secondary localized cutaneous amyloidosis associated with actinic keratosis. J. Invest. Dermatol. 61: 293 (1973).CrossRefGoogle Scholar
  5. 5.
    U. Runne and C.E. Orfanos, Amyloid production by dermal fibroblasts: Electron microscopic studies on the origin of amyloid in various dermatoses and skin tumors. Br. J. Dermatol. 97: 155 (1977).CrossRefGoogle Scholar
  6. 6.
    M.M. Black and E. Wilson Jones, Macular amyloidosis. A study of 21 cases with special references to the rele of the epidermis in its histogenesis. Br. J. Dermatol. 84: 199 (1970).CrossRefGoogle Scholar
  7. 7.
    K. Hashimoto and M. Kumakiri, Colloid-amyloid bodies in PUVA-treated human psoriatic patients. J. Invest. Dermatol. 72: 70 (1979).CrossRefGoogle Scholar
  8. 8.
    S Masu, M. Hosokawa and M. Seiji, Immunofluorescence studies on the cutaneous amyloidosis with anti-keratin antibody. Tohoku J. Exp. Med. 132: 121 (1980).CrossRefGoogle Scholar
  9. 9.
    H. Kobayashi and K. Hashimoto, Amyloidogenesison organ-limited cutaneous amyloidosis: an antigenic identity between epidermal keratin and skin amyloid. J. Invest. Dermatol. 80: 66 (1983)CrossRefGoogle Scholar
  10. 10.
    H. Eto, K. Hashimoto, H. Kobayashi, and T.T. Sun, Differential staining of cytoid bodies and skin-limited amyloids with monoclonal anti-keratin antibodies. Am. J. Pathol. 116: 473 (1984).Google Scholar
  11. 11.
    M. Ishii, Y. Asai and T. Hamada, Evaluation of cutaneous amyloid employing anti-keratin antibodies and the immunoperoxidasetechnique (PAP method) Acta Dermatovener. 64: 281 (1984).Google Scholar
  12. 12.
    P. Noren, P. Westermark, G.G. Cornwell III and W. Murdoch, Immunofluores-cence and histochemical studies of localized cutaneous amyloidosis. Br. J. Dermatol. 108: 277 (1983).CrossRefGoogle Scholar
  13. 13.
    M. Ishii, Y. Terao, Y. Asai and T. Hamada, Macular amyloidosis with patchy filamentous degeneration of collagen islands. J. Cutan. Pathol. 8: 421 (1981).CrossRefGoogle Scholar
  14. 14.
    K. Sakakibara, A. Ooshima, S. Igarashi and J. Sakakibara, Immunolocaliza-tion of type III collagen and procollagen in cirrhoric human liver using monoclonal antibodies. Virchows Arch Pathol Anat. 409: 37 (1986).CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • M. Ishii
    • 1
  • K. Fukai
    • 1
  • M. Chanoki
    • 1
  • H. Kobayashi
    • 1
  • T. Hamada
    • 1
  • Y. Muragaki
    • 1
    • 2
  • A. Ooshima
    • 1
    • 2
  1. 1.Department of DermatologyOsaka City University Medical SchoolJapan
  2. 2.Department of PathologyWakayama Medical CollegeWakayamaJapan

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