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J Biol Chem, Vol. 274, Issue 35, 25085-25092, August 27, 1999
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From the Three mammalian hyaluronan synthase genes,
HAS1, HAS2, and HAS3, have recently
been cloned. In this study, we characterized and compared the enzymatic
properties of these three HAS proteins. Expression of any of these
genes in COS-1 cells or rat 3Y1 fibroblasts yielded de novo
formation of a hyaluronan coat. The pericellular coats formed by HAS1
transfectants were significantly smaller than those formed by HAS2 or
HAS3 transfectants. Kinetic studies of these enzymes in the membrane
fractions isolated from HAS transfectants demonstrated that HAS
proteins are distinct from each other in enzyme stability, elongation
rate of HA, and apparent Km values for the two
substrates UDP-GlcNAc and UDP-GlcUA. Analysis of the size distributions
of hyaluronan generated in vitro by the recombinant
proteins demonstrated that HAS3 synthesized hyaluronan with a molecular
mass of 1 × 105 to 1 × 106 Da,
shorter than those synthesized by HAS1 and HAS2 which have molecular
masses of 2 × 105 to ~2 × 106 Da.
Furthermore, comparisons of hyaluronan secreted into the culture media
by stable HAS transfectants showed that HAS1 and HAS3 generated
hyaluronan with broad size distributions (molecular masses of 2 × 105 to ~2 × 106 Da), whereas HAS2
generated hyaluronan with a broad but extremely large size (average
molecular mass of >2 × 106 Da). The occurrence of
three HAS isoforms with such distinct enzymatic characteristics may
provide the cells with flexibility in the control of hyaluronan
biosynthesis and functions.
Institute for Molecular Science of Medicine, Department of Biological Chemistry,
School of Medicine, University of California,
Davis, California 95616, and the ** Department of Biochemistry and
Molecular Biology, Mayo Clinic Scottsdale,
Scottsdale, Arizona 85259
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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