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Glycobiology Advance Access published online on April 20, 2005
Glycobiology, doi:10.1093/glycob/cwi064
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© The Author 2005. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oupjournals.org
Received February 4, 2005
Revised April 13, 2005
Accepted April 14, 2005

Article

Compositional profiling of heparin/heparan sulfate using mass spectrometry: Assay for specificity of a novel extracellular human endosulfatase

Ola M. Saad 1, Heiner Ebel 2, Kenji Uchimura 3, Steven D. Rosen 3, Carolyn R. Bertozzi 4, and Julie A. Leary 1*

1 Department of Chemistry, University of California, Berkeley, California 94720, USA; Present address: Department of Chemistry and Division of Molecular and Cellular Biology, Genome Center, University of California Davis, One Shields Road, Davis, California 95616
2 Department of Chemistry, University of California, Berkeley, California 94720, USA
3 Department of Anatomy, and UCSF Comprehensive Cancer Center, University of California, San Francisco, California 94143, USA
4 Department of Chemistry, University of California, Berkeley, California 94720, USA; Department of Molecular and Cell Biology, and Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA

* To whom correspondence should be addressed.
Julie A. Leary, E-mail: jaleary{at}ucdavis.edu


  Abstract

An important class of carbohydrates studied within the field of glycobiology, heparin and heparan sulfate (HS) have been implicated in a diverse array of biological functions. Changes in their sulfation pattern and domain organization have been associated with different pathological situations such as viral infectivity, tumor growth and metastasis. To obtain structural information about these biomolecules, and the modifications they may undergo during different stages of cell growth and development, a mass spectrometry based method was developed and used to obtain unambiguous structural information on the glycosaminoglycans that comprise heparin/HS. The method was applied to assay for the heparin substrate specificity of a newly discovered human extracellular endosulfatase, HSulf-2, which has been implicated in tumorigenesis. This new protocol incorporates twelve known heparin disaccharides, including three sets of isomers. A unique response factor (R) is determined for each dissacharide, while a multiplexed and data processing method is incorporated for faster data acquisition and quantification purposes. Proof of principle was performed using various heparin/HS samples isolated from bovine and porcine tissues.

Keywords: glycosaminoglycans / heparan sulfate / heparin / mass spectrometry / sulfatase assay.
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