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J Biol Chem, Vol. 274, Issue 4, 2511-2517, January 22, 1999
From the Bristol-Myers Squibb Pharmaceutical Research Institute,
Princeton, New Jersey 08543 and the § Department of
Dermatology, University of Washington, Seattle, Washington 98105
Isoforms of CD44 are differentially modified by
the glycosaminoglycans (GAGs) chondroitin sulfate (CS), heparan sulfate
(HS), and keratan sulfate. GAG assembly occurs at serines followed by glycines (SG), but not all SG are utilized. Seven SG motifs are distributed in five CD44 exons, and in this paper we identify the HS
and CS assembly sites that are utilized in CD44. Not all the CD44 SG
sites are modified. The SGSG motif in CD44 exon V3 is the only HS
assembly site; this site is also modified with CS. HS and CS attachment
at that site was eliminated by mutation of the serines in the V3 motif
to alanine (AGAG). Exon E5 is the only other CD44 exon that supports
GAG assembly and is modified with CS. Using a number of recombinant
CD44 protein fragments we show herein that the eight amino acids
located downstream of the SGSG site in V3 are responsible for the
specific addition of HS to this site. If the eight amino acids located
downstream from the first SG site in CD44 exon E5 are exchanged with
those located downstream of the SGSG site in exon V3, the SG site in E5
becomes modified with HS and CS. Likewise if the eight amino acids
found downstream from the first SG in E5 are placed downstream from the
SGSG in V3, this site is modified with CS but not HS. We also show that
these sequences cannot direct the modification of CD44 with HS from a
distance. Constructs containing CD44 exon V3 in which the SGSG motif
was mutated to AGAG were not modified with HS even though they
contained other SG motifs. Thus, a number of sequence and structural
requirements that dictate GAG synthesis on CD44 have been identified.
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