344153 RESULTS
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
CONFERENCE COVERAGE 1999-10-24 Conference Coverage Sukanto Sinha, departing from his abstract (122.1), described the purification and partial characterization of a novel 501 amino acid long aspartyl protease. The data were entirely consistent with the β-secretase activities reported by
CONFERENCE COVERAGE 1999-10-24 Conference Coverage Just when it appeared as though the mechanisms of the proteolytic processing of APP were finally becoming apparent, Andreas Weidemann presented an elegant study demonstrating the existence of a different processing event (122.2). Using
CONFERENCE COVERAGE 1999-10-24 Conference Coverage Using difluoroketone peptidomimetics previously shown to reversibly inhibit γ-secretase activity in CHO cells, Michael Wolfe reported that increasing the bulkiness of the P1 substituent of these compounds increased their potency, thus,
CONFERENCE COVERAGE 1999-10-24 Conference Coverage In testing the hypothesis that unscheduled cell death may alter APP processing, Andrea Le Blanc (122.4) provided compelling evidence that caspase 6 can directly cleave APP and cause an increase in Aβ levels in serum deprived human prim
CONFERENCE COVERAGE 1999-10-24 Conference Coverage Recent studies have demonstrated that wild-type APP can protect against p53 mediated apoptosis, whereas FAD mutant APP (FADAPP) cannot. N3 rat neuroblastoma cells which are deficient in APP were transfected with wtAPP or FADAPP and the
CONFERENCE COVERAGE 1999-10-24 Conference Coverage Yamin (122.9) presented evidence that the zinc metalloproteinase EC 3.4.24.15 (E24.15) plays a role in neuronal mediated degradation of Aβ. In fact transfection of neuroblastoma cells with antisense E24.15 allows the accumulation of Aβ
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