Joseph Zaia
Associate Professor
Department of Biochemistry
Associate Director, Mass Spectrometry Resource
Boston University School of Medicine
670 Albany Street, Rm. 509
Boston, MA 02118
Phone: 617-638-6762
Fax: 617-638-6761
For more information click here Joseph Zaia
Education
B.S., Bates College, Lewiston, ME
Ph.D., Massachusetts Institute of Technology, Cambridge, MA
Research Interest
Glycosaminoglycans (GAGs) are linear oligosaccharides attached to proteoglycan core proteins in virtually every animal species and tissue. A large number of proteins bind GAGs including those involved in blood clotting, many growth factors, and several extracellular matrix proteins. Mutation in GAG biosynthetic genes leads to severe malformations, indicating the critical roles these carbohydrates play in development. Much of proteoglycan biological activity is mediated though protein-binding interactions. The diverse nature of GAG structure renders them difficult to purify and hinders attempts to discover both structural determinants for the binding of proteins ligands and dissociation constants. To date the specific GAG sequences mediating protein binding have been described for only a few cases, primarily because of difficulties in obtaining pure samples. The broad goals of this research are to develop methodology to elucidate GAG structural determinants of protein binding using high resolution mass spectrometry. This work utilizes cutting edge mass spectrometric technology to detail functionally relevant GAG sub-structures.
Projects Include
Glycomics of glycosaminoglycan expression in the C. elegans model organism
Development of a model of glycosaminoglycan expression of mammalian organ and organ sub-structuress. Extension to tumor states in mammalian organs.
Assignment of biological function to specific glycosaminoglcycan domains based on binding to growth factors of cardiovascular interest and ability to mediate cell signaling.
Glycomics of chondroitin/dermatan sulfates in normal and diseased connective tissue (cartilage, bone, muscle, tendon, ligament, synovium)
Development of techniques for producing molecular information on glycosaminoglycan expression using histological tissue slides.
Representative Publications
Zaia, J. (2009) On-line separations combined with MS for analysis of glycosaminoglycans. Mass Spectrom Rev 28, 254-272.
Staples, G., Bowman, M., Costello, C. E., Hitchcock, A., Lau, J., Leymarie, N., Miller, C., Naimy, H., Shi, X., and Zaia, J. (2009) A Chip-based Amide-HILIC LC/MS Platform for Glycosaminoglycan Glycomics. Proteomics 9, 686-695.
Shi, X., and Zaia, J. (2009) Organ-specific heparan sulfate structural phenotypes. J Biol Chem in press 2/25/09, M809637200.
Zaia, J. (2008) Mass spectrometry and the emerging field of glycomics. Chem Biol 15, 881-92.
Hitchcock, A., Bowman, M., Staples, G., and Zaia, J. (2008) Improved Workup for Glycosaminoglycan Disaccharide Analysis using Capillary Electrophoresis with Laser-Induced Fluorescence Detection. Electrophoresis 29, 4538-4548.
Naimy, H., Leymarie, N., Bowman, M., and Zaia, J. (2008) Characterization of heparin oligosaccharides binding specifically to antithrombin III using mass spectrometry. Biochemistry 47, 3155-3161.
Hitchcock, A., Yates, K. E., Costello, C., and Zaia, J. (2008) Comparative Glycomics of Connective Tissue Glycosaminoglycans Proteomics 8, 1384-97.
Bowman, M., and Zaia, J. (2007) Novel tags for the stable isotopic labeling of carbohydrates and quantitative analysis by mass spectrometry. Anal Chem 76, 5777-5784.
Ziegler, A., and Zaia, J. (2006) Separation of heparin oligosaccharides by size-exclusion chromatography. J Chromatogr B Analyt Technol Biomed Life Sci 837, 76-86.
Miller, M. J. C., Costello, C. E., Malmström, A., and Zaia, J. (2006) A tandem
Hitchcock, A. M., Yates, K. E., Shortkroff, S., Costello, C. E., and Zaia, J. (2006) Optimized extraction of glycosaminoglycans from normal and osteoarthritic cartilage for glycomics profiling. Glycobiology 17, 25-35.
Hitchcock, A. M., Costello, C. E., and Zaia, J. (2006) Glycoform quantification of chondroitin/dermatan sulfate using an LC/MS/MS platform. Biochemistry 45, 2350-61.
