Expression of the developmental I antigen by a cloned human cDNA encoding a member of a beta-1,6-N-acetylglucosaminyltransferase gene family

The blood group i/I antigens were the first identified alloantigens that display a dramatic change during human development. The i and I antigens are determined by linear and branched poly-N-acetyllactosaminoglycans, respectively. In human erythrocytes during embryonic development, the fetal (i) ant...

Full description

Saved in:
Bibliographic Details
Published in:Genes & development 1993-03, Vol.7 (3), p.468-478
Main Authors: Bierhuizen, M F, Mattei, M G, Fukuda, M
Format: Article
Language:English
Subjects:
Adult
Animals
Carbohydrate Sequence
CHO Cells
Chromosome Banding
Chromosome Mapping
Chromosomes, Human, Pair 9
Cloning, Molecular - methods
Cricetinae
DNA - genetics
DNA - metabolism
Embryonic and Fetal Development - physiology
Erythrocytes - enzymology
Glycopeptides - biosynthesis
Glycopeptides - isolation & purification
Humans
I Blood-Group System - genetics
Isoantigens - genetics
Molecular Sequence Data
Multigene Family
N-Acetylglucosaminyltransferases - genetics
N-Acetylglucosaminyltransferases - metabolism
Sequence Homology, Nucleic Acid
Transfection
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The blood group i/I antigens were the first identified alloantigens that display a dramatic change during human development. The i and I antigens are determined by linear and branched poly-N-acetyllactosaminoglycans, respectively. In human erythrocytes during embryonic development, the fetal (i) antigen is replaced by the adult (I) antigen as a result of the appearance of a beta-1,6-N-acetylglucosaminyltransferase, the I-branching enzyme. Here, we report the cDNA cloning and expression of this branching enzyme that converts linear into branched poly-N-acetyllactosaminoglycans, thus introducing the I antigen in transfected cells. The cDNA sequence predicts a protein with type II membrane topology as has been found for all other mammalian glycosyltransferases cloned to date. The Chinese hamster ovary cells that stably express the isolated cDNA acquire I-branched structures as evidenced by the structural analysis of glycopeptides from these cells. Comparison of the amino acid sequence with those of other glycosyltransferases revealed that this I-branching enzyme and another beta-1,6-N-acetylglucosaminyltransferase that forms a branch in O-glycans are strongly homologous in the center of their putative catalytic domains. Moreover, the genes encoding these two beta-1,6-N-acetylglucosaminyltransferases were found to be located at the same locus on chromosome 9, band q21. These results indicate that the I-branching enzyme represents a member of a beta-1,6-N-acetylglucosaminyltransferase gene family of which expression is controlled by developmental programs.
ISSN:0890-9369
1549-5477
DOI:10.1101/gad.7.3.468