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Updated: Sep 29, 2025

Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells
Published on: April 27, 2010
What Happens If a Human Galectin Enters the Endoplasmic Reticulum?
Tanja J Kutzner1, Alonso M Higuero2, Martina Süßmair3
1Faculty of Veterinary Medicine, Institute of Physiological Chemistry, Ludwig-Maximilians-University Munich, Munich, Germany.
Abstract:
Mammalian galectins have no signal peptide, and it is not known what would happen if a galectin is directed to take the classical export route. The corresponding engineering of galectin-specific cDNA will answer questions on the fate of a signal peptide-bearing protein variant after its entry into the endoplasmic reticulum (ER). Affinity chromatography and mass-spectrometric analysis of occupancy of potential N-glycosylation sites for the galectin, binding and functional assays with cells as well as subcellular fractionation by density gradient ultracentrifugation and immunocytochemical colocalization with ER/Golgi markers report on aspects of the consequences of letting a galectin enter new territory. Applying these methods will help to clarify why galectins are leaderless and thus produced by free ribosomes.
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