PMID- 29501606
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20201123
IS  - 1879-2642 (Electronic)
IS  - 0005-2736 (Linking)
VI  - 1860
IP  - 9
DP  - 2018 Sep
TI  - Amyloid growth and membrane damage: Current themes and emerging perspectives from 
      theory and experiments on Abeta and hIAPP.
PG  - 1625-1638
LID - S0005-2736(18)30063-4 [pii]
LID - 10.1016/j.bbamem.2018.02.022 [doi]
AB  - Alzheimer's Disease (AD) and Type 2 diabetes mellitus (T2DM) are two incurable 
      diseases both hallmarked by an abnormal deposition of the amyloidogenic peptides 
      Abeta and Islet Amyloid Polypeptide (IAPP) in affected tissues. Epidemiological data 
      demonstrate that patients suffering from diabetes are at high risk of developing 
      AD, thus making the search for factors common to the two pathologies of special 
      interest for the design of new therapies. Accumulating evidence suggests that the 
      toxic properties of both Abeta or IAPP are ascribable to their ability to damage the 
      cell membrane. However, the molecular details describing Abeta or IAPP interaction 
      with membranes are poorly understood. This review focuses on biophysical and in 
      silico studies addressing these topics. Effects of calcium, cholesterol and 
      membrane lipid composition in driving aberrant Abeta or IAPP interaction with the 
      membrane will be specifically considered. The cross correlation of all these 
      factors appears to be a key issue not only to shed light in the countless and 
      often controversial reports relative to this area but also to gain valuable 
      insights into the central events leading to membrane damage caused by 
      amyloidogenic peptides. This article is part of a Special Issue entitled: Protein 
      Aggregation and Misfolding at the Cell Membrane Interface edited by Ayyalusamy 
      Ramamoorthy.
CI  - Copyright (c) 2018 Elsevier B.V. All rights reserved.
FAU - Sciacca, Michele F M
AU  - Sciacca MFM
AD  - Istituto CNR di Biostrutture e Bioimmagini- Sede Secondaria di Catania, Via Paolo 
      Gaifami 18, 95126 Catania, Italy.
FAU - Tempra, Carmelo
AU  - Tempra C
AD  - Universita degli Studi di Catania, Dipartimento di Scienze Chimiche, Viale Andrea 
      Doria 6, 95125 Catania, Italy.
FAU - Scollo, Federica
AU  - Scollo F
AD  - Universita degli Studi di Catania, Dipartimento di Scienze Chimiche, Viale Andrea 
      Doria 6, 95125 Catania, Italy.
FAU - Milardi, Danilo
AU  - Milardi D
AD  - Istituto CNR di Biostrutture e Bioimmagini- Sede Secondaria di Catania, Via Paolo 
      Gaifami 18, 95126 Catania, Italy.
FAU - La Rosa, Carmelo
AU  - La Rosa C
AD  - Universita degli Studi di Catania, Dipartimento di Scienze Chimiche, Viale Andrea 
      Doria 6, 95125 Catania, Italy. Electronic address: clarosa@unict.it.
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20180301
PL  - Netherlands
TA  - Biochim Biophys Acta Biomembr
JT  - Biochimica et biophysica acta. Biomembranes
JID - 101731713
SB  - IM
OTO - NOTNLM
OT  - Abeta
OT  - Alzheimer
OT  - Amylin
OT  - Amyloid
OT  - Model membrane
OT  - Type II diabetes mellitus
EDAT- 2018/03/05 06:00
MHDA- 2018/03/05 06:01
CRDT- 2018/03/05 06:00
PHST- 2017/12/22 00:00 [received]
PHST- 2018/02/21 00:00 [revised]
PHST- 2018/02/21 00:00 [accepted]
PHST- 2018/03/05 06:00 [pubmed]
PHST- 2018/03/05 06:01 [medline]
PHST- 2018/03/05 06:00 [entrez]
AID - S0005-2736(18)30063-4 [pii]
AID - 10.1016/j.bbamem.2018.02.022 [doi]
PST - ppublish
SO  - Biochim Biophys Acta Biomembr. 2018 Sep;1860(9):1625-1638. doi: 
      10.1016/j.bbamem.2018.02.022. Epub 2018 Mar 1.