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J. Biol. Chem., Vol. 279, Issue 3, 1861-1866, January 16, 2004

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Determining Heparan Sulfate Structure in the Vicinity of Specific Sulfotransferase Recognition Sites by Mass Spectrometry^*

Zhengliang L. Wu, Miroslaw Lech, David L. Beeler, and Robert D. Rosenberg¶

From the Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 and the Department of Medicine, Harvard Medical School, Beth Israel Deaconess Medical Center, Boston, Massachusetts 02215

Sulfated motifs on heparan sulfate (HS) are involved in various extracellular processes from cell signaling to enzymatic regulation, but the structures of these motifs are obscure. We have developed a strategy to determine the structure of sulfotransferase recognition sites which constitute these motifs. Stable isotope is first introduced into specific sites on HS with HS sulfotransferases and the modified HS is then digested into oligosaccharides of differing sizes. The overlapping oligosaccharides containing the introduced stable isotope are identified by changes in the m/z profiles by mass spectrometry, and their relationships are elucidated. In this way, the HS structures in the vicinity of the sulfotransferase recognition site are quickly determined and groups on precursor structures of HS that direct the action of HS sulfotransferases are pinpointed.

Received for publication, October 17, 2003 , and in revised form, November 4, 2003.

^* This work was supported in part by the National Institutes of Health Grants 1PO1 HL 66105 and 5RO1HL 59479. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed: Dept. of Biology, MIT, 31 Ames St., MIT Bldg. 68-488, Cambridge, MA 02142. Tel.: 617-253-8803; Fax: 617-258-6553; E-mail: rdrrosen{at}mit.edu.

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