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(Received for publication, April 17, 1996, and in revised form, July 18, 1996)
From the Burnham Institute,¶ La Jolla, California
92037
To identify the putative mammalian hyaluronan
synthase, we cloned a human cDNA that is related to the
Streptococcus hyaluronan synthase (HasA) and the
Xenopus developmental protein DG42 which has been shown to
have chitin synthase activity. The cDNA, for which we propose the
name Has2, encodes a novel protein with a predicted molecular mass of
63.6 kDa. Has2 shows 55% amino acid identity with Xenopus
DG42 and 52% identity with the mouse HAS protein, another putative
hyaluronan synthase recently reported by Itano and Kimata (Itano, N.,
and Kimata, K. (1996) J. Biol. Chem. 271, 9875-9878).
The deduced primary structure revealed the presence of several
hydrophobic stretches which can form multiple transmembrane domains. It
also demonstrated the complete conservation of amino acid residues that
are known to be critical for
N-acetylglucosaminyltransferase activity of yeast chitin
synthase. When the Has2 cDNA was transfected into human 293 and
Chinese hamster ovary cells, the production of hyaluronan in the
transfected cells increased up to 34- and 9-fold, respectively. Strong
expression of Has2 mRNA was observed in exponentially proliferating
human IMR-90 fibroblasts but not in growth-arrested IMR-90 cells. These
results suggest that the Has2 protein is a crucial component of the
human hyaluronan synthase system.
Volume 271, Number 38,
Issue of September 20, 1996
pp. 22945-22948
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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