# AMYLOID ANGIOPATHY, EARLY PLAQUES, AND AGING

> **NIH NIH R01** · NEW YORK UNIVERSITY · 1991 · $187,982

## Abstract

Amyloidosis comprises a heterogeneous group of diseases that vary
in clinical expression and the composition and distribution of
insoluble amyloid fibrils.  It is believed that all types of
amyloidosis involve overproduction of a soluble precursor, and that
deposition occurs in patients who are genetically or otherwise
defective in degrading these molecules.  We put forward a
tripartite division of the elements central to the issue of
pathogenesis: the inherent chemical amyliodogenic potential of the
precursor protein; the possibility of aberrant protein metabolism,
and the existence of disease microenviromental tissue factors that
may facilitate the conversion of precursor proteins into their
insoluble amyloid products.

Recently we have shown that the amyloid fibrils of sporadic
cerebral amyloid angiopathy and an autosomal dominant form of
familial amyloid angiopathy in patients of Dutch origin (also
designated Hereditary Cerebral Hemorrhage with Amyloidosis of Dutch
Type) are similar to Alzheimer Disease amyloid B-protein.  These
findings indicate that B-amyloid deposition disorders form a
spectrum of overlapping clinicopathological conditions which range
from patients with predominant vascular involvement to patients
having a combination of vascular and parenchyma involvement in
varying proportions, manifested clinically by stroke and dementia,
respectively.  We have also found that these disorders exhibit
varying neuritic plaque-like structures, or "preamyloidotic
lesions," suggesting that they represent an early stage of B-
protein deposition.  Similar amyloid deposits are often encountered
in a significant percent of neurologically asymptomatic aged
individuals; hence it is important to clarify their relationship.

We propose the following: 1) Biochemical and immunohistochemical
studies of early amyloid deposits in asymptomatic elders and
patients with cerebral amyloid angiopathy.  2) Identification of
the amyloid protein precursor in aged humans.  3) Study of cellular
origin and synthesis of the amyloid protein precursor in cells
grown in culture.

This study is relevant for understanding the basic etiopathogenetic
mechanisms associated with amyloid deposition in aging, amyloid
angiopathy, and Alzheimer's Disease; it may be useful for
diagnostic purposes at a pathological and clinical level.

## Key facts

- **NIH application ID:** 3120458
- **Project number:** 5R01AG008721-02
- **Recipient organization:** NEW YORK UNIVERSITY
- **SAM.gov UEI:** NX9PXMKW5KW8
- **Principal Investigator:** BLAS FRANGIONE
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1991
- **Award amount:** $187,982
- **Award type:** 5
- **Project period:** 1990-01-01 → 1994-12-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3120458

## Citation

> US National Institutes of Health, RePORTER application 3120458, AMYLOID ANGIOPATHY, EARLY PLAQUES, AND AGING (5R01AG008721-02). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3120458. Licensed CC0.

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