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RESEARCH PRODUCT
Manifestation and ultrastructural typing of amyloid deposits in the heart
Hans-michael SchneiderStephan StörkelW. Thoenessubject
AdultMaleAmyloidPathologymedicine.medical_specialtyHistologyAdolescentAmyloidHeart diseasePlasma cell dyscrasiaAutopsyBasement MembranePathology and Forensic Medicinemental disordersmedicineHumansIsolated atrial amyloidosisHeart AtriaMolecular BiologyAgedbusiness.industryMyocardiumAmyloidosisCell DifferentiationAmyloidosisCell BiologyGeneral MedicineMiddle Agedmedicine.diseaseCoronary VesselsMicroscopy ElectronCardiac amyloidosisHeart failurecardiovascular systemFemaleAnatomyCardiomyopathiesbusinessdescription
Using light and electron microscopy, 65 cases of amyloid deposits in the heart were examined. Five different groups were distinguished: I. isolated atrial amyloidosis, II. senile cardiac amyloidosis, III. cardiac amyloid accompanying chronic infections and tumors, IV. cardiac amyloid accompanying plasma cell dyscrasia, V. idiopathic cardiac amyloidosis. Seen structurally, no principal differences in the precise localization of the amyloid deposits were found in any of the groups investigated. Amyloid is always deposited in the vicinity of cells with myocytic cell differentiation (i.e. the heart muscle cells, non-striated muscle cells of the vessels), whereby the relevant basement membranes serve as conductors. A systematic relationship between amyloid and the collagenous fibers of the interstitium or the tunica adventitia of the vessels could not be demonstrated, which shows the concept "pericollagen" to be inadequate for the morphological characterization of amyloid deposits in the heart. Whereas for group I a localized mechanism for the production of amyloid must be considered, in the case of groups II-V a vascular principle expression of a generalized amyloidosis seems to be the major factor. The question of the differing concentration of amyloid deposits in the heart suggests that localized factors (e.g. changes in the myocytic basement membranes) and quantitative changes of the amyloid-building proteins may also be important.
year | journal | country | edition | language |
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1983-01-01 | Virchows Archiv A Pathological Anatomy and Histopathology |