The Sulfate Moieties of Glycosaminoglycans Are Critical for the Enhancement of β-Amyloid Protein Fibril Formation

A1thought the mechanisms of amyloidogenesis have not been entirely clarified, proteolysis of the parent proteins may be one of the important steps in the amyloid fibril formation. Recently, we reported that "dense fibrillar inclusions" (DFI), which had the characteristics of lysosomes and contained organized fibrillar profiles as well, were observed in the reticuloendothelial cells in close association with the foci of new amyloid deposits. We considered the findings as evidence for the involvement of lysosomal system in amyloid fibril formation (l). In the present study, we attempted to determine the identity of the contents of the DFI by the use of antisera against the amyloid protein (AA) and an immuno-electron microscopic technique.Amyloidosis was induced in CBA/J mice by daily injections of casein (l). AA was isolated from amyloid-laden spleens by gel filtration and antibody to it was produced in rabbits (2). For immunocytochemistry, the unlabeled antibody enzyme method (3) was employed.

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Protective effect by T-588 against β-amyloid protein-induced microglial cell death

The Japanese Journal of Pharmacology ◽

10.1016/s0021-5198(19)34226-x ◽

1999 ◽

Vol 79 ◽

pp. 51

Author(s):

Takashi Fujita ◽

Yuji Kimura ◽

Yoko Komeda ◽

Kazuhiro Takuma ◽

Toshio Matsuda ◽

...

Keyword(s):

Cell Death ◽

Protective Effect ◽

Microglial Cell ◽

Amyloid Protein ◽

Β Amyloid

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The role of Ca2+ channel modulation in the neuroprotective actions of estrogen in β-amyloid protein and 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) cytotoxic models

Neurochemistry International ◽

10.1016/j.neuint.2003.12.013 ◽

2004 ◽

Vol 45 (1) ◽

pp. 31-38 ◽

Cited By ~ 23

Author(s):

F Ba

Keyword(s):

Amyloid Protein ◽

Channel Modulation ◽

Β Amyloid ◽

Neuroprotective Actions

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Inhibitors of Fibril Formation and Cytotoxicity of β-Amyloid Peptide Composed of KLVFF Recognition Element and Flexible Hydrophilic Disrupting Element

Biochemical and Biophysical Research Communications ◽

10.1006/bbrc.2001.6191 ◽

2002 ◽

Vol 290 (1) ◽

pp. 121-124 ◽

Cited By ~ 43

Author(s):

Ken-ichi Watanabe ◽

Kazuhiko Nakamura ◽

Shingo Akikusa ◽

Tomoko Okada ◽

Masato Kodaka ◽

...

Keyword(s):

Fibril Formation ◽

Amyloid Peptide ◽

Recognition Element ◽

Β Amyloid ◽

Β Amyloid Peptide

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Comparative studies on peptides representing the so-called tachykinin-like region of the Alzheimer Aβ peptide [Aβ(25–35)]

Biochemical Journal ◽

10.1042/bj3360419 ◽

1998 ◽

Vol 336 (2) ◽

pp. 419-427 ◽

Cited By ~ 18

Author(s):

Omar M. A. EL-AGNAF ◽

G. Brent IRVINE ◽

Geraldine FITZPATRICK ◽

W. Kenneth GLASS ◽

David J. S. GUTHRIE

Keyword(s):

Electron Microscopy ◽

Ligand Binding ◽

Comparative Studies ◽

Aβ Peptide ◽

Amyloid Protein ◽

Binding Studies ◽

Nk1 Receptors ◽

Ligand Displacement ◽

Β Amyloid

In an attempt to answer the question of whether or not the so-called tachykinin-like region of the Alzheimer β-amyloid protein [Aβ(25–35)] can act as a tachykinin, the sequences Aβ(25–35), Aβ(25–35)amide and their norleucine-35 and phenylalanine-31 analogues were synthesized. These peptides were examined with ligand binding studies, electron microscopy, CD and NMR. In all cases some differences were found between the Aβ(25–35) analogue and the corresponding Phe31 peptide. In addition, in ligand displacement studies on tachykinin NK1 receptors, only the Phe31 analogue showed activity comparable to that of genuine tachykinins. We conclude that peptides based on Aβ(25–35) but with a Phe residue at position 31 do display properties typical of a tachykinin, but that peptides with Ile at this position do not.

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