Glycobiology, Vol 9, 897-906, Copyright © 1999 by Oxford University Press
C Kannicht, L Lucka, R Nuck, W Reutter and M Gohlke
Rat C-CAM is a ubiquitous, transmembrane and carcinoembryonic antigen
related cell adhesion molecule. The human counterpart is known as biliary
glycoprotein (BGP) or CD66a. It is involved in different cellular functions
ranging from intercellular adhesion, microbial receptor activity, signaling
and tumor suppression. In the present study N-glycosylation of C-CAM
immunopurified from rat liver was analyzed in detail. The primary sequence
of rat C-CAM contains 15 potential N-glycosylation sites. The N-glycans
were enzymatically released from glycopeptides, fluorescently labeled with
2- aminobenzamide, and separated by two-dimensional HPLC. Oligosaccharide
structures were characterized by enzymatic sequencing and MALDI-TOF-MS.
Mainly bi- and triantennary complex structures were identified. The
presence of type I and type II chains in the antennae of these glycans
results in heterogeneous glycosylation of C-CAM. Sialylation of the sugars
was found to be unusual; bi- and triantennary glycans contained three and
four sialic acid residues, respectively, and this linkage seemed to be
restricted to the type I chain in the antennae. Approximately 20% of the
detected sugars contain these unusual numbers of sialic acids. C-CAM is the
first transmembrane protein found to be oversialylated.
ORIGINAL ARTICLES
N-Glycosylation of the carcinoembryonic antigen related cell adhesion molecule, C-CAM, from rat liver: detection of oversialylated bi- and triantennary structures
Institut fur Molekularbiologie und Biochemie der Freien Universitat Berlin, Fachbereich Humanmedizin, Berlin-Dahlem, Germany.
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