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61.
The ability of particular cell surface glycoproteins to recycle and become
exposed to individual Golgi enzymes has been demonstrated. This study was
designed to determine whether endocytic trafficking includes significant
reentry into the overall oligosaccharide processing pathway. The Lec1
mutant of Chinese hamster ovary (CHO) cells lack N -
acetylglucosaminyltransferase I (GlcNAc-TI) activity resulting in surface
expression of incompletely processed Man5GlcNAc2 N -linked
oligosaccharides. An oligosaccharide tracer was created by exoglycosylation
of cell surface glycoproteins with purified porcine GlcNAc-TI and
UDP-[3H]GlcNAc. Upon reculturing, all cell surface glycoproteins that
acquired [3H]GlcNAc were acted upon by intracellular mannosidase II, the
next enzyme in the Golgi processing pathway of complex N -linked
oligosaccharides (t1/2= 3-4 h). That all radiolabeled cell surface
glycoproteins were included in this endocytic pathway indicates a common
intracellular compartment into which endocytosed cell surface glycoproteins
return. Significantly, no evidence was found for continued oligosaccharide
processing consistent with transit through the latter cisternae of the
Golgi apparatus. These data indicate that, although recycling plasma
membrane glycoproteins can be reexposed to individual Golgi-derived
enzymes, significant reentry into the overall contiguous processing pathway
is not evident.
相似文献
62.
In the current model for Glc3Man9GlcNAc2-P-P-Dol assembly, Man5GlcNAc2-
P-P-Dol, Man-P-Dol, and Glc-P-Dol are synthesized on the cytoplasmic face
of the ER and diffuse transversely to the lumenal leaflet where the
synthesis of the lipid-bound precursor oligosaccharide is completed. To
establish the topological sites of Glc-P-Dol synthesis and the
lipid-mediated glucosyltransfer reactions involved in
Glc3Man9GlcNAc2-P-P-Dol synthesis in ER vesicles from pig brain, the
trypsin-sensitivity of Glc-P-Dol synthase activity and the Glc-P-
Dol:Glc0-2Man9GlcNAc2-P-P-Dol glucosyltransferases (GlcTases) was examined
in sealed microsomal vesicles. Since ER vesicles from brain do not contain
glucose 6-phosphate (Glc 6-P) phosphatase activity, the latency of the
lumenally oriented, processing glucosidase I/II activities was used to
assess the intactness of the vesicle preparations. Comparative enzymatic
studies with sealed ER vesicles from brain and kidney, a tissue that
contains Glc 6-P phosphatase, demonstrate the reliability of using the
processing glucosidase activities as latency markers for topological
studies with microsomal vesicles from non-gluconeogenic tissues lacking Glc
6-P phosphatase. The results obtained from the trypsin-sensitivity assays
with sealed microsomal vesicles from brain are consistent with a
topological model in which Glc-P-Dol is synthesized on the cytoplasmic face
of the ER, and subsequently utilized by the three Glc-P-Dol-mediated
GlcTases after "flip-flopping" to the lumenal monolayer.
相似文献
63.
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Junior Barrera Roberto M CesarJr Carlos HumesJr David C MartinsJr Diogo FC Patrão Paulo JS Silva Helena Brentani 《BMC bioinformatics》2007,8(1):169
Background
One goal of gene expression profiling is to identify signature genes that robustly distinguish different types or grades of tumors. Several tumor classifiers based on expression profiling have been proposed using microarray technique. Due to important differences in the probabilistic models of microarray and SAGE technologies, it is important to develop suitable techniques to select specific genes from SAGE measurements. 相似文献66.
L-glutamate, the major excitatory neurotransmitter in the human brain, activates a family of ligand-gated ion channels, the major subtypes of which are named AMPA, kainate, and NMDA receptors. In common with many signal transduction proteins, glutamate receptors are modulated by ions and small molecules, including Ca(2+), Mg(2+), Zn(2+), protons, polyamines, and steroids. Strikingly, the activation of kainate receptors by glutamate requires the presence of both Na(+) and Cl(-) in the extracellular solution, and in the absence of these ions, receptor activity is abolished. Here, we identify the site and mechanism of action of anions. Surprisingly, we find that Cl(-) ions are essential structural components of kainate receptors. Cl(-) ions bind in a cavity formed at the interface between subunits in a dimer pair. In the absence of Cl(-), dimer stability is reduced, the rate of desensitization increases, and the fraction of receptors competent for activation by glutamate drops precipitously. 相似文献
67.
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Daniel O’Connor Marta Valente Pinto Dylan Sheerin Adriana Tomic Ruth E Drury Samuel Channon‐Wells Ushma Galal Christina Dold Hannah Robinson Simon Kerridge Emma Plested Harri Hughes Lisa Stockdale Manish Sadarangani Matthew D Snape Christine S Rollier Michael Levin Andrew J Pollard 《Molecular systems biology》2020,16(11)
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70.