DETECTION OF CIRCULATING FORMS OF THE Β-Amyloid PRECURSOR PROTEIN (BAPP) IN HUMAN PLASMA

Selkoe, Dennis J.; Mammen, Andrew L.; Podlisny, Marcia B.; Palmert, Mark R.; Younkin, Steve; Schenk, D.

doi:10.1097/00005072-198905000-00236

Cited by 5 publications

(1 citation statement)

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“…Soluble APP derivatives have been detected in serum, brain homogenates, cerebrospinal fluid and tissue-culture medium [20][21][22][23][24] as a complex group of 105-135 kDa glycoproteins. The primary structure and biological properties of the soluble APP711 mRNA transcript are analogous to those of a cell-secreted proteinase inhibitor nexin II [25,26].…”

Section: Introductionmentioning

confidence: 99%

Epitope map of two polyclonal antibodies that recognize amyloid lesions in patients with Alzheimer's disease

Ghiso

Wısnıewskı

Vidal

et al. 1992

Biochemical Journal

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Two synthetic peptides with sequences identical with those of fragments of the extracellular domain of the Alzheimer's-disease amyloid precursor protein (APP) were used to raise antibodies. SP28 comprises positions 597-624 of the APP695 isoform, whereas SP41 extends towards the N-terminus (amino acids 584-624) and contains the entire SP28 peptide. Using e.l.i.s.a. and inhibition experiments we identified the two beta-turn-containing segments 602-607 and 617-624 as the epitopes recognized by anti-SP41 and anti-SP28 respectively. Both antibodies immunolabelled amyloid lesions in brains from Alzheimer's-disease patients and patients with related disorders, whereas they were unreactive in control brains. However, when probed on immunoblots, anti-SP28 failed to detect full-length APP from baculovirus-infected Sf9 cells, and anti-SP41 reacted weakly compared with other anti-APP antisera. The data suggest that these antibodies are directed to conformational epitopes not existent in the native molecules but present after alternative APP processing.

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