Amyloid deposits inside myocardial fibers in transthyretin-Met30 familial amyloidotic polyneuropathy. A histological and biochemical study

Cardiology. 1994;85(3-4):145-53. doi: 10.1159/000176669.

Abstract

A case of severe cardiac involvement is reported in a patient affected with familial amyloidotic polyneuropathy due to the Portuguese type I variant (Val-->Met30) of the transthyretin (prealbumin) molecule. Echocardiographic and hemodynamic studies suggested the presence of a progressive infiltrative cardiomyopathy that was later confirmed by endomyocardial biopsy. Amyloid deposits were found in both intra- and extra-myofiber location and thought to be related to primary involvement of the heart. Norepinephrine content of myocardial bioptic specimens was about threefold lower than normal, indicating that autonomic denervation may contribute to the maintenance and progression of cardiomyopathy. A sample obtained from the sural nerve showed a loss of myelinated fibers along with accumulation of amyloid masses in the endoneurial space. This histopathologic pattern correlated with a sharp decrease in the activity of the enzyme subserving electrochemical conduction through the axonal membrane, Na+, K(+)-ATPase.

Publication types

  • Case Reports

MeSH terms

  • Amyloid / metabolism*
  • Amyloid Neuropathies / complications
  • Amyloid Neuropathies / genetics
  • Amyloid Neuropathies / metabolism*
  • Amyloid Neuropathies / pathology
  • Amyloidosis / genetics
  • Amyloidosis / metabolism
  • Amyloidosis / pathology
  • Cardiomyopathies / complications
  • Cardiomyopathies / metabolism
  • Cardiomyopathies / pathology
  • Humans
  • Male
  • Middle Aged
  • Myocardium / metabolism*
  • Myocardium / pathology
  • Norepinephrine / analysis
  • Prealbumin / metabolism*
  • Sodium-Potassium-Exchanging ATPase / analysis
  • Sural Nerve / enzymology
  • Sural Nerve / pathology

Substances

  • Amyloid
  • Prealbumin
  • amyloid prealbumin
  • Sodium-Potassium-Exchanging ATPase
  • Norepinephrine