Joseph Zaia, PhD

Professor, Boston University Chobanian & Avedisian School of Medicine

Biography

The manner in which a cell responds to many growth factor stimuli depends on interactions between glycosaminoglycans (GAGs), growth factors, and growth factor receptors. Extracellular matrix GAGs binds growth factors, creating morphogens gradients essential to tissue patterning. Because these events depend on the fine structure of the GAG chains present, regulation of GAG biosynthesis is a key factor for understanding normal and disease related cellular growth
The key to exploiting an understanding of GAG structure-function relationships for human disease therapy is to winnow oligosaccharide-protein binding patterns from heterogeneous biological preparations. Toward this end, we have developed mass spectral methods for GAGs that enable comparison of structures as a function of biological variables.

The long term research aims are (1) to develop a fundamental understanding of the manner in which glycosaminoglycan expression is varied according to the cellular growth environment related to human disease and (2) to identify HS chain structures useful as therapeutic targets.

New bioinformatics methods are essential to realizing these goals. The data produced using our methods are information rich and not amenable to manual interpretation. Further, the methods needed are distinct from those used in genomics and proteomics. We are developing bioinformatics methods appropriate for interpretation of structural data on glycosaminoglycans and other carbohydrates to identify targets for disease therapy.

Publications

  • Published 9/3/2025

    Halvorsen SC, Gkousioudi A, Nicks R, Alvarez VE, Bigio IJ, Zaia J, Stein TD, Zhang Y. Cerebrovascular remodeling in aging and neurodegenerative disease progression. Front Bioeng Biotechnol. 2025; 13:1597917. PMID: 40969224.

    Read at: PubMed

  • Published 7/9/2025

    Wu S, Lu J, Tursumamat N, Liu Q, Liu S, Bian Y, Klein J, Han Z, Zaia J, Lin C, Zhu J, Wei J. Unveiling the Accurate Site-Specific N- and O-Glycosylation of Hyperglycosylated Erythropoietin Drugs by an Integrated Approach. Anal Chem. 2025 Jul 22; 97(28):15410-15419. PMID: 40631521.

    Read at: PubMed

  • Published 7/1/2025

    Nalehua MR, Zaia J. Software Design and Analytical Challenges for Confident Glycopeptide Identification With Data-Independent Acquisition. Mass Spectrom Rev. 2025 Jul 01. PMID: 40590152.

    Read at: PubMed

  • Published 5/6/2025

    Mernie E, Zaia J. Recent analytical advances in the detection and characterization of 3-O-sulfated heparan sulfate. Anal Bioanal Chem. 2025 Jul; 417(16):3551-3562. PMID: 40328973.

    Read at: PubMed

  • Published 4/20/2025

    Mernie E, Cavallero GJ, Xia C, Lin C, Zaia J. Untangling Heparan Sulfate 3-O-Sulfation Using a Novel Offline Cationic-Peptide Affinity Enrichment, Followed by HILIC-cIM-MS. Anal Chem. 2025 Apr 29; 97(16):8700-8708. PMID: 40254935.

    Read at: PubMed

View All 241 Publications:   View Full Profile in BUMC

Other Positions

  • Member, Bioinformatics Graduate Program
    Boston University
  • Member, BU-BMC Cancer Center
    Boston University
  • Member, Genome Science Institute
    Boston University
  • Center Faculty Member, Mass Spectrometry
    Boston University Chobanian & Avedisian School of Medicine
  • Graduate Faculty (Primary Mentor of Grad Students)
    Boston University Chobanian & Avedisian School of Medicine, Graduate Medical Sciences

Websites

Education

  • Massachusetts Institute of Technology, PhD
  • Bates College, BS

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