✦ LIBER ✦

Amyloid fibril formation by the CAD domain of caspase-activated DNase

✍ Scribed by Koichi Uegaki; Tsutomu Nakamura; Hitoshi Yamamoto; Atsuko Kobayashi; Takayuki Odahara; Kazuaki Harata; Yoshihisa Hagihara; Norikazu Ueyama; Toshio Yamazaki; Noboru Yumoto

Publisher: Wiley (John Wiley & Sons)
Year: 2005
Tongue: English
Weight: 290 KB
Volume: 79
Category: Article
ISSN: 0006-3525
DOI: 10.1002/bip.20327

No coin nor oath required. For personal study only.

✦ Synopsis

Abstract

Caspase‐activated DNase (CAD) is a key protein in the process of apoptosis that degrades DNA through the action of caspases. Its N‐terminal region, the CAD domain (CAD‐CD), is highly conserved among CAD family proteins and is responsible for the interaction with its inhibitor. We report here that CAD‐CD spontaneously aggregates to form amyloid fibrils, without a lag time, under the conditions of low pH (below 4) and the presence of anions. Interestingly, the secondary structure of CAD‐CD in the fibril state comprised not only β‐sheet but also α‐helix, as found in CD, FTIR, and x‐ray fiber diffraction experiments. Aromatic side chains have a defined orientation and are in the hydrophobic environment occurring with the CAD‐CD fibrillogenesis. These findings provide new insights into the architecture of amyloid fibrils. © 2005 Wiley Periodicals, Inc. Biopolymers 79: 39–47, 2005

This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at [email protected]

📜 SIMILAR VOLUMES

Elevated vulnerability to oxidative stre

Elevated vulnerability to oxidative stress-induced cell death and activation of caspase-3 by the Swedish amyloid precursor protein mutation

✍ Anne Eckert; Barbara Steiner; Celio Marques; Steffen Leutz; Helmut Romig; Christ 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 398 KB

## Abstract The Swedish double mutation (KM670/671NL) of amyloid precursor protein (APPsw) is associated with early‐onset familial Alzheimer's disease (FAD) and results in from three‐ to sixfold increased β‐amyloid production. The goal of the present study was to elucidate the effects of APPsw on m

ChemInform Abstract: Construction of Pep

ChemInform Abstract: Construction of Peptides that Undergo Structural Transition from α-Helix to β-Sheet and Amyloid Fibril Formation by the Introduction of N-Terminal Hydrophobic Amino Acids.

✍ Yuta Takahashi; Taro Yamashita; Akihiko Ueno; Hisakazu Mihara 📂 Article 📅 2000 🏛 John Wiley and Sons ⚖ 27 KB 👁 2 views

Linear analogues derived from the first

Linear analogues derived from the first EGF-like domain of human blood coagulation factor VII: enhanced inhibition of FVIIa/TF complex activity by backbone modification through aspartimide formation

✍ Mette Husbyn; Lars Ørning; Alan Cuthbertson; Peter M. Fischer 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 105 KB 👁 2 views

Coagulation factor VII bound to its cofactor tissue factor is the physiological initiator of blood coagulation. The interaction between factor VII and tissue factor involves all four of the structural modules found in factor VII, with the most significant contribution coming from the first EGF-like