Download Alzheimer’s Disease: Lessons from Cell Biology by E. Grote, F. Bonzelius, G. Herman (auth.), K. S. Kosik M.D., PDF

By E. Grote, F. Bonzelius, G. Herman (auth.), K. S. Kosik M.D., D. J. Selkoe M.D., Y. Christen Ph.D. (eds.)

ISBN-10: 3642794254

ISBN-13: 9783642794254

Like the unflinching gaze of Captain Ahab strolling the deck of the Pequod, Alzheimer researchers have had their attractions mounted firmly at the affliction for a few years. Now, as this quantity amply demonstrates, comprehensive researchers from different fields, who've proposal deeply approximately mobile organic difficulties are making use of their insights to Alzheimer's affliction. The contri­ butions the following characterize the textual content types of the court cases from the 10th "Colloque medecine et recherche" of the Fondation IPSEN dedicated to learn on Alzheimer's disorder. The symposium, entitled "Alzheimer's sickness: classes from mobilephone Biology" used to be held in Paris on April 25, 1994. As is clear from the numerous backgrounds of the participants, the medical pursuit of Alzheimer's affliction has all started to meld with extra uncomplicated disciplines, rather phone biology. whereas at the one hand, new parts of specialization are regularly rising, the bounds of older disciplines are increas­ ingly blurred. probably for many of the years because the first descriptions of the illness in 1907, the technological know-how of Alzheimer's affliction used to be descriptive, and lay within the province of pathologists. this period of time, within which very much used to be discovered in regards to the topography of senile plaques and neurofibrillary tangles, culminated with an ultrastructural description of those hallmark constructions. the fashionable period of Alzheimer's illness study opened with the iden­ tification of the part proteins in plaques and tangles.

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Extra resources for Alzheimer’s Disease: Lessons from Cell Biology

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J Bioi Chern 269: 15427-15430 Duncan J, Kornfeld S (1988) Intracellular movement of two mannose 6-phosphate receptors: return to the Golgi apparatus. J Cell Bioi 106: 617-628 Farnsworth CL, Feig LA (1991) Dominant inhibitory mutations in the Mg++ -binding site of RasH prevent its activation by GTP. Mol Cell Bioi 11: 4822-4829 Feig LA, Cooper GM (1988) Inhibition of NIH 3T3 cell proliferation by mutated Res proteins with preferential affinity for GDP. Mol Cell Bioi 8: 3235-3243 Ferro-Novick S, Novick P (1993) The role of GTP-binding proteins in transport along the exocytic pathway.

R. Pfeffer TARGET rig. 1.. Prenylated rab proteins occur in the cytosol as a complex with GOI (center, right). GOI presents the complexes to specific organelles; this may be catalyzed by a GO I· displacement factor (GOF) in conjunction with a nucleotide exchanger (GEF). Rab proteins, with GTP bound, are recruited into nascent transport vesicles and may catalyze association of V·SNARES (on the vesicle) with T-SNARES (on the target membrane) to accomplish transport vesicle delivery. After fusion, a GTPase-activating protein (GAP) increases the GTPase rate of the rab protein, converting it into its GOP conformation.

1987; Le Bivic et al. 1990; Matter et al. 1990). Our recent work has demonstrated directly that endosomes and the TGN do indeed decode the same sorting signals. For example, inactivation of the LDL receptor's distal basolateral sorting signal converts it into a transcytotic protein which is as efficient at basolateral to apical transport as is the polymeric immunoglobulin receptor (Matter et al. 1993). Thus, partial inactivation of a signal which decreases the efficiency of basolateral sorting in the TGN leads to a corresponding decrease in basolateral sorting efficiency in endosomes.

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