Characteristics of aquaporin expression surrounding senile plaques and cerebral amyloid angiopathy in Alzheimer disease.

Progression of clinical deterioration and pathological changes in patients with Alzheimer disease evaluated at biopsy and autopsy.

OBJECTIVES To quantify the progression of senile plaques, neurofibrillary tangles, cerebral amyloid angiopathy, and microglial activation in the cortex and white matter of patients with Alzheimer disease evaluated at both biopsy and subsequent autopsy and correlate these changes with the progression of neurologic impairment. SETTING Academic referral center for patient with Alzheimer disease....

Differences between the pathogenesis of senile plaques and congophilic angiopathy in Alzheimer disease.

The Pathology of Alzheimer Disease Elicits an In Vivo Immunological Response

The mechanism(s) responsible for the loss of neurons that characterizes Alzheimer disease is incompletely understood. Nonetheless, there is considerable evidence suggestive of immune abnormalities coupled to alterations in blood-brain barrier permeability that likely play a key role in both the etiology and progression of the disease. To examine these issues further, this study was designed to ...

Potential Therapeutic Strategies to Prevent the Progression of Alzheimer to Disease States

Senile plaques are mainly composed of different species of fibrillar β-amyloid (Aβ), a product of the cleavage of the β-amyloid precursor protein (APP), and they are surrounded by dystrophic neurites, reactive astrocytes and microglia. Aβ fibrillar deposits also occur in diffuse plaques, subpial deposits and in the wall of the cerebral and meningeal blood vessels in the form of amyloid angiopat...

Amyloid plaque core protein in Alzheimer disease and Down syndrome.

We have purified and characterized the cerebral amyloid protein that forms the plaque core in Alzheimer disease and in aged individuals with Down syndrome. The protein consists of multimeric aggregates of a polypeptide of about 40 residues (4 kDa). The amino acid composition, molecular mass, and NH2-terminal sequence of this amyloid protein are almost identical to those described for the amyloi...