345779 RESULTS
CONFERENCE COVERAGE 1999-11-03 Conference Coverage Hashimoto, Masliah and colleagues (27.14) reported that cytochrome C stimulates α-synuclein aggregration in vitro and that cytochrome C can be observed in Lewy bodies, in postmortem brain tissue. Whether cytochrome C actually plays a r
CONFERENCE COVERAGE 1999-11-01 Conference Coverage Research on presenilins presented at this year's meeting centered around two major questions: 1) What is the role of presenilins in Aβ production and APP processing, and 2) what are the other biological actions of presenilins? A m
CONFERENCE COVERAGE 1999-10-26 Conference Coverage In the relatively short time allotted, Dale Schenk (519.5) managed to describe most of the data from his group’s recent Nature paper (Nature 1999;400:173-177), and a little more. Schenk demonstrated that Aβ immunization of young (six-w
CONFERENCE COVERAGE 1999-10-26 Conference Coverage Chronic mucosal administration of certain proteins is known to decrease organ-specific autoimmune processes in several autoimmune models, including those affecting the CNS. In AD, local inflammatory responses frequently occur in the vi
CONFERENCE COVERAGE 1999-10-25 Conference Coverage Using exquisite human primary cortical cultures containing neurons, astrocytes, and microglia, Nadeau (319.1) demonstrated that addition of VLDLs or HDLs increased media levels of both Aβ40 and Aβ42. Moreover, addition of ApoE3, Apo4 o
CONFERENCE COVERAGE 1999-10-25 Conference Coverage Using primary hippocampal neurons transfected with APP by means of the Semliki-forest-virus expression system Christine Bergmann (319.2) demonstrated that lovastatin (which inhibits de novo cholesterol synthesis) and methyl-b-cyclodext
CONFERENCE COVERAGE 1999-10-25 Conference Coverage Until very recently, Aβ accumulation and aggregation were thought to be exclusively extracellular phenomena. However, a number of abstracts presented at this meeting (see 120.10 and 720.10) suggest that this notion must be revisited. G
CONFERENCE COVERAGE 1999-10-25 Conference Coverage Kawarabayashi (319.10) presented compelling data for a time-dependent accumulation of Aβ in the detergent-insoluble glycolipid enriched membrane domains (DIGs) of Tg2576 mouse brain. He also showed that Aβ accumulated in DIGs from huma
CONFERENCE COVERAGE 1999-10-25 Conference Coverage In an exhaustive study, Iwata (240.1) presented evidence that the trans Golgi network was the major site of Aβ42 production in both neural and non-neural cells. Cos-1 and N2a cells were transfected with C100 bearing retention signals f
CONFERENCE COVERAGE 1999-10-25 Conference Coverage The mechanisms of regulated α-secretase cleavage were thoroughly examined in two excellent companion posters from Virginia Lee’s lab (240.2, 240.3). The authors demonstrated that TNFalpha converting enzyme (TACE) knockout mice show red
CONFERENCE COVERAGE 1999-10-25 Conference Coverage At times the scene around this poster (240.11) was more like a football scrimmage or a rugby scrum than the normally genteel atmosphere associated with a scientific event. By the time I made my way to within sight of the poster, the pr
CONFERENCE COVERAGE 1999-10-25 Conference Coverage Janet Johnston (240.16) presented a detailed study of the effect of proteasome and prolendopeptidase (PEP) inhibitors on Aβ production by SH SY 5Y human neuroblastoma cells stably transfected with SPA4CT (C99). Both the proteasome and
CONFERENCE COVERAGE 1999-10-24 Conference Coverage Treatment of human cerebovascular smooth muscle (HCSM) cells with Aβ1-42 or AβQ22 (a mutant associated with hereditary cerebral hemorrhage with amyloidosis-Dutch type) leads to the formation of amyloid fibrils on the surface of HCSM ce
CONFERENCE COVERAGE 1999-10-24 Conference Coverage Papassotiropoulos (1201) began his presentation by reviewing the evidence for a role of cathepsin D, an aspartyl protease, in AD. Previous work has implicated catD as a secretase in the cleavage of APP. It is found in plaques and exhib
CONFERENCE COVERAGE 1999-10-24 Conference Coverage One of the limitations in studying the pathogenic role of amyloid plaque deposition is the fact that conventional methods allow microscopic analysis only of postmortem tissue, which can provide only a single snapshot of a process that
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