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J Biol Chem, Vol. 273, Issue 19, 11902-11907, May 8, 1998

Identification and Expression in Mouse of Two Heparan Sulfate Glucosaminyl N-Deacetylase/N-Sulfotransferase Genes

Marion Kusche-Gullberg, Inger Eriksson^¶, Dagmar Sandbäck Pikas, and Lena Kjellén^¶

From the  Department of Medical Biochemistry and Microbiology, University of Uppsala, S 751 23 Uppsala, and the ^¶ Department of Veterinary Medical Chemistry, Swedish University of Agricultural Sciences, S750 07 Uppsala, Sweden

The biosynthesis of heparan sulfate/heparin is a complex process that requires the coordinate action of a number of different enzymes. In close connection with polymerization of the polysaccharide chain, the modification reactions are initiated by N-deacetylation followed by N-sulfation of N-acetylglucosamine units. These two reactions are carried out by a single protein. Proteins with such dual activities were first purified and cloned from rat liver and mouse mastocytoma. The mouse mastocytoma enzyme is encoded by an ~;14-kilobase (kb) mRNA, whereas the rat liver transcript contains ~;18 kb. In the present study, the primary structure of the enzyme encoded by the mouse 8-kb transcript is described. It is demonstrated that both the 4-and 8-kb transcripts have a wide tissue distribution and that they are encoded by separate genes. Characterization of the gene encoding the 4-kb transcript demonstrates that it spans a region of about 8 kb and that it contains at least 14 exons. The similarity of this gene and the previously characterized human gene for the 8-kb transcript is discussed.

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