In previous work, we showed that highly proliferative cells and cancer cells, but not cells with normal growth rate, have tubules rich in alpha-1,2 fucosylated epitopes that extend radially from the nucleus to the cell periphery and form an unusual uptake system. The importance of alpha-1,2 fucosylation in forming tubules was demonstrated by proving that down-regulating the two corresponding fucosyltransferases (FUT1 and FUT2) causes tubule fragmentation. Here, we present evidence that in the prostate cancer cell line DU145, the tubules arise in actively growing cells from vesicles in the medial and trans elements of a partially fragmented Golgi complex, while in not actively growing cells the tubules become completely independent from the Golgi complex. Formation and elongation of the tubules proved to depend on the actin cytoskeleton, since the alpha-1,2 fucosylated protein(s) segregate with the cytoskeleton proteins, and not in the membrane fraction, as do the Golgi markers and other fucosylated proteins, while depolymerization of the actin filaments causes tubule fragmentation and shifting of the alpha-1,2 fucosylated proteins into the membrane fraction.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1016/j.yexcr.2020.112324 | DOI Listing |
J Biosci Bioeng
September 2024
Department of Applied Biological Science, Faculty of Agriculture, Kagawa University, 2393 Ikenobe, Miki, Kagawa 761-0795, Japan. Electronic address:
J Biol Chem
August 2019
Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8P 5C2, Canada
An important aspect of the interaction between the opportunistic bacterial pathogen and its human host is its ability to harvest host glycans. The pneumococcus can degrade a variety of complex glycans, including - and -linked glycans, glycosaminoglycans, and carbohydrate antigens, an ability that is tightly linked to the virulence of Although is known to use a sophisticated enzyme machinery to attack the human glycome, how it copes with fucosylated glycans, which are primarily histo-blood group antigens, is largely unknown. Here, we identified two pneumococcal enzymes, GH29 and GH95, that target α-(1→3/4) and α-(1→2) fucosidic linkages, respectively.
View Article and Find Full Text PDFJ Am Chem Soc
July 2011
Division of Glycoscience, School of Biotechnology, Royal Institute of Technology (KTH), 106 91 Stockholm, Sweden.
The current drive for applications of biomass-derived compounds, for energy and advanced materials, has led to a resurgence of interest in the manipulation of plant polymers. The xyloglucans, a family of structurally complex plant polysaccharides, have attracted significant interest due to their intrinsic high affinity for cellulose, both in muro and in technical applications. Moreover, current cell wall models are limited by the lack of detailed structure-property relationships of xyloglucans, due to a lack of molecules with well-defined branching patterns.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!