Notch from Neurodevelopment to Neurodegeneration

by Israel, A.; De Strooper, B.; Checker, F.; Christen, Y.

• ISBN13: 9783540430735
• ISBN10: 3540430733
• Format: Hardcover
• Copyright: 2002-10-01
• Publisher: Springer Verlag

Summary

Can molecular mechanisms involved in neural development help us to understand, prevent and perhaps reverse the course of brain ageing and neurodegenerative disorders? Brain development and function require complex cellular and molecular processes controlled by a number of different signaling mechanisms. One such signaling mechanism, the Notch pathway, has been recognized as an important player in the regulation of cellfate decisions during early neural development. However, the action of this evolutionary conserved and widely used cell-cell interaction mechanism is not confined to the developing nervous system. In addition, recent studies have shown that elucidating the mechanism of Notch signaling and its role in the brain is important for our understanding of neurological disorders such as Alzheimer's disease and cerebral arteriopathy CADASIL.

Table of Contents

Regulated Intramembrane Proteolysis - New Lessons from Lipid Metabolism and the Unfolded Protein Response	1	(19)
R. B. Rawson
Notch Signaling in the Brain: More than Just a Developmental Story	19	(22)
N. Sestan
F. Rakic
Control of Notch Activity by the Ubiquitin-Proteasome Pathway	41	(18)
N. Gupta-Rossi
O. Le Bail
Ch. Brou
F. Logeat
E. Six
A. Israel
A Presenilin-Dependent S3-Like γ-Secretase Cleavage of the β-Amyloid Precursor Protein	59	(4)
H. Steiner
M. Sastre
G. Multhaup
D.B. Teplow
Ch. Haass
New Non-Peptidic Inhibitors of y-Secretase Abolish Aβ Production Without Modifying Notch Cleavage	63	(8)
A. Petit
F. Bihel
C. Alves da Costa
O. Pourquie
Y.-H. Suh
J.-L. Kraus
F. Checler
Presenilins, APP, and Notch: Proteolysis from Womb to Tomb	71	(18)
M.S. Wolfe
W.P. Esler
W.T. Kimberly
D.J. Selkoe
Missorting of the Dendritic Cell Adhesion Molecule Telencephalin in Presenilin-Deficient Neurons	89	(12)
C. Esselens
C. Boeve
V. Baert
G. Snellings
P. Cupers
K. Craessaerts
B. De Strooper
W. Annaert
βAPP Processing, its Biology and Alzheimer's Disease	101	(8)
L. D'Adamio
Further Analysis of the Nicastrin: Presenilin Complex	109	(10)
F. Chen
G. Yu
S. Arawaka
M. Nishimura
T. Kawarai
H. Yu
A. Tandon
A. Supala
Y.Q. Song
E. Rogaeva
P. Milman
Ch. Sato
Ch. Janus
J. Lee
L. Song
L. Zhang
P.E. Fraser
P.H. St George-Hyslop
PSI Interacts With and Facilitates β-Catenin Turnover	119	(12)
E.H. Koo
S. Soriano
D.E. Kang
δ-Catenin, Presenilin, and the Synaptic-Adherens Junction Complex	131	(12)
K.S. Kosik
M. Medina
T. Ochiishi
M.C. Martinez
Q. Lu
Vascular Smooth Muscle Cells Are the Primary Target of the Events Leading from Notch3 Mutations to CADASIL	143	(32)
A. Joutel
F. Andreux
A. Francois
V. Domenga
F. Chapon
C. Godfraind
E. Tournier-Lasserve
Subject Index	175