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Title: Molecular polymorphism of the syndecans - Identification of a hypo-glycanated murine syndecan-1 splice variant
Authors: Romaris, M
Coomans, C
Ceulemans, H
Bruystens, AM
Vekemans, Sylvie
David, Guido # ×
Issue Date: Jun-1999
Publisher: Amer soc biochemistry molecular biology inc
Series Title: Journal of Biological Chemistry vol:274 issue:26 pages:18667-18674
Abstract: We have identified a cDNA that encodes a variant form of murine syndecan-1, The variant cDNA lacks the sequence corresponding to the first 132 nucleotides of the third exon of the syndecan-1 gene. The corresponding message is rare. The alternative splice respects the reading frame and deletes 44 amino acids from the protein, joining the S(45)GS(47)GT sequence to a variant immediate downstream context. This sequence context initiates with alanine instead of glycine as residue 50, reducing the number of SGXG sequence motifs in the protein from two to one. Expression of this variant syndecan-1 in Madin-Darby canine kidney or MOLT-4 cells yielded a recombinant proteoglycan with a reduced number and clustering of the heparan sulfate chains, Both the conversions of Ala(50) and of Lys(53) into glycine enhanced the heparan sulfate substitution of the variant protein. These findings support the concept that serine glycine dipeptide signals for glycosaminoglycan/heparan sulfate synthesis depend on sequence context (Zhang, L., David, G.., and Esko, J. D. (1995) J. Biol. Chem, 270, 27127-27135) and imply that alternative splicing mechanisms may in part control the molecular polymorphism of syndecan-1 and, therefore, the efficiency and versatility of this protein in its co-receptor functions.
ISSN: 0021-9258
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Department of Human Genetics - miscellaneous
Molecular Genetics Section (-)
× corresponding author
# (joint) last author

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