Cortical tissue of patients with hereditary cerebral hemorrhage with amyloidosis (Dutch) contains various extracellular matrix deposits.

BACKGROUND

Hereditary cerebral hemorrhage with amyloidosis (Dutch) (HCHWA-D) and Alzheimer's disease (AD) have certain clinical and histopathologic features in common; both are characterized by cerebral amyloid beta deposits. Extracellular matrix (ECM) components have been demonstrated in plaques and in vascular amyloid of AD, suggesting a causative relation.

EXPERIMENTAL DESIGN

We studied the immunohistochemical expression of the ECM components collagen type I, III, and IV, heparan sulfate proteoglycan (HSPG), laminin, and fibronectin in cortical tissue of six HCHWA-D patients, two AD patients, and five controls.

RESULTS

The vasculature of control patients and the noncongophilic vessels in HCHWA-D and AD patients stained for all ECM components, with the exception of collagen type I in part of the capillaries. The media of normal larger vessels stained for collagen type I and III and fibronectin; a similar pattern was found in the vascular amyloid in HCHWA-D and AD patients. The plaques in HCHWA-D and AD reacted for HSPG and weakly for collagen III and IV and laminin. Furthermore, with the exception of anti-collagen type I, all anti-ECM Ab decorated coarse deposits clustered in the vicinity of thick-walled, amyloid-laden vessels in HCHWA-D patients; these deposits were not spatially related to amyloid beta-positive plaques.

CONCLUSIONS

This study demonstrates the presence of ECM components in the main pathologic features of HCHWA-D and as perivascular deposits. The observed distribution of matrix molecules is partly different from AD. The ECM may well be essential for the evolvement of the pathology of HCHWA-D.