Download e-book for iPad: Glyco-and Cellbiology: Biosynthesis, Transport, and Function by T. A. Rapoport, D. Görlich, E. Hartmann, S. Prehn, K.-U.

By T. A. Rapoport, D. Görlich, E. Hartmann, S. Prehn, K.-U. Kalies (auth.), Professor Dr. Felix Wieland, Professor Dr. med. Werner Reutter (eds.)

Understanding the organic position of the various oligosaccharides of glycoproteins and glycolipids has been an immense problem in mobile biology. Glycosylation is a necessary step in the course of molecular acceptance and is taken with protein folding, sorting, concentrating on and intracellular translocation. additional, glycoproteins of the mobilephone membrane play a huge position in mobile adhesion, hormone functionality, antibody motion and sign mediation. present wisdom of the molecular and mobile mechanisms focused on those procedures is presented.

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Additional info for Glyco-and Cellbiology: Biosynthesis, Transport, and Function of Glycoconjugates

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This antibody was synthesized in the ER of micro-injected cells and transported to the Golgi apparatus, where it stopped, presumably because it was bound to Mann II. By so doing, however, it blocked transport through the Golgi apparatus of the VSV G protein, suggesting that large aggregates are incompatible with Golgi function. 40 cell line, transport is normal as shown by pulse-chase experiments following the transport of histocompatability antigens (HLA). ) Fig. 6. 40 HeLa cell lines. HLA was pulsed with 35S-methionine and chased for increasing times before immuneprecipitation and fractionation by SDS-PAGE.

J Bioi Chern 265:19928-19931 Burke B, Warren G (1984) Microinjection of mRNA coding for anti-Golgi antibody inhibits intracellular transport of a viral membrane protein. Cell 36:847-856 Burke J, Pettitt 1M, Schachter H, Sarkar M, Gleeson PA (1992) The transmembrane and flanking sequences of ~1,2-N-acetylglucosaminyltransferase I specify medial-Golgi localization. J Bioi Chern 267:24433-24440 Colley KJ, Lee EU, Paulson JC (1992) The signal anchor and stem regions of the b-galactoside a2,6-sialyltransferase may each act to localize the enzyme to the Golgi apparatus.

Since the latter abolished rapid internalization in BHK cells, this suggested that the structural requirements for the internalization signal are much more stringent than for basolateral sorting. Since it was conceivable that different requirements for basolateral sorting and rapid internalization of LAP were due to the use of different cell types and/or species, we analyzed also the internalization of LAP in MDCK cells (Prill et al. 1993). This analysis showed that only LAP mutants with an intact basolateral sorting signal were internalized.

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