Differential subcompartmentation of terminal glycosylation in the Golgi apparatus of intestinal absorptive and goblet cells

Two terminal glycosyltransferases, a sialyltransferase and the blood group A alpha 1,3 N-acetylgalactosaminyltransferase, were found to exhibit differential subcompartmentation in the Golgi apparatus of intestinal goblet and absorptive cells. As expected from their role in terminal glycosylation, th...

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Bibliographic Details
Published in:The Journal of biological chemistry Vol. 261; no. 30; p. 14307
Main Authors: Roth, J, Taatjes, D J, Weinstein, J, Paulson, J C, Greenwell, P, Watkins, W M
Format: Journal Article
Language:English
Published: United States 25.10.1986
Subjects:
ABO Blood-Group System
Animals
Cell Compartmentation
Galactosyltransferases - analysis
Glycosylation
Golgi Apparatus - enzymology
Golgi Apparatus - ultrastructure
Histocytochemistry
Immunologic Techniques
Intestines - ultrastructure
Microscopy, Electron
N-Acetylgalactosaminyltransferases
Rats
Sialic Acids - analysis
Sialyltransferases - analysis
ISSN:0021-9258
Online Access:Get more information
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Summary:Two terminal glycosyltransferases, a sialyltransferase and the blood group A alpha 1,3 N-acetylgalactosaminyltransferase, were found to exhibit differential subcompartmentation in the Golgi apparatus of intestinal goblet and absorptive cells. As expected from their role in terminal glycosylation, the two glycosyltransferases and their products, sialic acid residues and blood group A substance, were localized in the trans cisternae of the Golgi apparatus of goblet cells. In contrast, however, they were found throughout the Golgi apparatus stack of adjacent absorptive cells, with the exception of the fenestrated first cis cisterna. The results are in contrast to the general view that enzymes in the glycosylation pathway are arranged in a cis to trans gradient across the Golgi apparatus and that such polarized distributions may instead be cell type-specific.
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ISSN:0021-9258
DOI:10.1016/s0021-9258(18)67019-x