Elsevier

Human Pathology

Volume 12, Issue 10, October 1981, Pages 917-922
Human Pathology

The relation of islet amyloid to the clinical type of diabetes*

https://doi.org/10.1016/S0046-8177(81)80197-9Get rights and content

Abstract

Islets were evaluated for the presence of amyloid deposits in 169 pancreases removed at autopsy. Islet amyloid occurred in 17 of 142 (12 per cent) of nondiabetics and in 16 of 27 (59 per cent) of diabetics. When diabetics were divided into categories according to clinical severity of disease, the insulin treated diabetics had the highest prevalence (89 per cent), the most diffuse distribution, and the most severe degree of islet amyloidosis. Amyloid was not found in any pancreases from subjects under 40 years of age. Above the age of 40, there was no correlation between aging and prevalence of islet amyloid. There was a significant association between severity of diabetes and prevalence of islet amyloid. The low prevalence of amyloid seen in nondiabetics and the fact that all adult onset, insulin treated diabetics had islet amyloid indicate that a reaction to endogenous insulin may be the basis for the deposition of islet amyloid.

References (20)

  • MelatoM. et al.

    Amyloidosis of the islets of Langerhans in relation to diabetes mellitus and aging

    Beitr. Path.

    (1977)
  • OpieE.L.

    The relation of diabetes mellitus to lesions of the pancreas. Hyaline degeneration of the islets of Langerhans

    J. Exper. Med.

    (1901)
  • WarrenS. et al.
  • BellE.T.

    Hyalinization of the islets of Langerhans in diabetes mellitus

    Diabetes

    (1952)
  • EhrlichJ. et al.

    Amyloidosis of the islets of Langerhans: a restudy of islet hyalin in diabetic and nondiabetic individuals

    Am. J. Pathol.

    (1961)
  • MaclarenN.K. et al.

    Antibody to cultured human insulinoma cells in insulin-dependent diabetes

    Lancet

    (1975)
  • RosenthalC.J. et al.

    VAriation with age and diseae of an amyloid A protein-related serum component

    J. Clin. Invest.

    (1975)
  • WestermarkP.

    On the nature of the amyloid in human islets of Langerhans

    Histochemistry

    (1974)
  • GlennerG.G. et al.

    ß-pleated sheet fibrils: a comparison of native amyloid with synthetic protein fibrils

    J. Histochem. Cytochem.

    (1974)
  • MlacM. et al.

    Amyloidosis of the pancreas: histochemical differentiation between insular and extrainsular deposits

    Basic Appl. Histochem.

    (1979)
There are more references available in the full text version of this article.

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*

This work was supported by grant CA 19410 from the National Cancer Institute through the National Pancreatic Cancer Project.

*

Medical Student, Dartmouth Medical School, Hanover, New Hampshire.

Professor of Pathology, Department of Pathology, Dartmouth Medical School. Attending Staff, Mary Hitchcock Afemorial Hospital, Hanover, New Hampshire.

Assistant Professor, Departments of Medicine and Community and Family Medicine, Dartmouth Medical School. Attending Staff, Mary Hitchcock Memorial Hospital, Hanover, New Hampshire.

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