Splenic amyloidosis: correlations between chemical types of amyloid protein and morphological features

• Published in: Modern pathology Vol. 3; no. 4; p. 419
• Main Authors: Ohyama, T, Shimokama, T, Yoshikawa, Y, Watanabe, T
• Format: Journal Article
• Language: English
• Published: United States 01-07-1990
• Subjects: Adult; Aged; Aged, 80 and over; Amyloid - analysis; Amyloidosis - metabolism; Amyloidosis - pathology; Female; Humans; Male; Middle Aged; Serum Amyloid A Protein - analysis; Splenic Diseases - metabolism; Splenic Diseases - pathology
• ISSN: 0893-3952

Sixty-one autopsy cases of splenic amyloidosis were reviewed to assess the relationship between the morphological patterns and chemical types of amyloid protein. On the basis of immunohistochemical reactions of amyloid protein, the cases were classified into 34 cases of AA and 27 of AL amyloidosis. Amyloid deposition in the spleen was divided into three major sites: the red pulp, the white pulp, and blood vessels. Red pulp involvement by amyloid was noted in 52% of the AL cases but in none of the AA cases. White pulp amyloid deposition was found in 70% of the AL and 35% of the AA cases. This difference was statistically significant (P less than 0.001). On the other hand, vascular deposition of amyloid was invariably noted in all cases with AA or AL amyloidosis, affecting the AA cases rather severely. These results strongly suggest that the widely held concept of deposition of amyloid as predominantly vascular in AL amyloidosis and parenchymal in AA amyloidosis requires revision. Our findings indicate that parenchymal, especially the red pulp, involvement is a consistent feature of AL amyloidosis, whereas vascular involvement is a finding common to both types of systemic amyloidosis.