Affiliations: [a] Department of Biochemistry, Medicine and Surgery, Stroke Program of the Sanders Brown Center on Aging, University of Kentucky Medical Center, Lexington, KY 40536, USA | [b] Department of Veterans Affairs Medical Center, Cooper Drive Division, Lexington, KY 40506, USA
Correspondence:
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Corresponding author: Dr. Mark S. Kindy, Department of Biochemistry, University of Kentucky, 800 Rose Street, Lexington, KY 40536, USA, Tel.: +1 606 2334511 ext. 4606; Fax: +1 606 2814989; E-mail: mskindy@pop.uky.edu.
Abstract: Alzheimer's disease is characterized by the tissue deposition of β-amyloid peptide (Aβ) in the brain. Recent studies have shown apoproteins (apo) in amyloid plaques and associated with high-density lipoprotein (HDL) particles in the cerebrospinal fluid (CSF). Western blot analysis revealed that serum amyloid A (apoSAA) protein was present in control and AD patients at low levels compared to apoE and apoA-I, however, AD brains showed a significant increase over control values. Analysis of CSF-HDL from control and AD individuals showed that apoA-I, apoE and apoSAA were on the particle. Immuno-cytochemical analysis showed that SAA was detected in senile plaques in AD tissue, but was predominantly localized to neuritic plaques. ApoE staining of AD brain confirmed that most plaques contained the apoprotein, similar to Aβ immunoreactivity, whereas apoA-I expressed little staining of senile plaques. No significant differences were detected in the level of apoSAA when compared to APOE genotype in AD samples, suggesting that interactions with apoE were non-specific. These data imply that the specific interactions of SAA with Aβ in the neuritic plaques may play a role in AD.
