Joseph Zaia, PhD

Professor, Biochemistry

Joseph Zaia
617.638.6762
670 Albany St Biosquare III

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.

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

Education

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

Classes Taught

  • GMSFC701
  • GMSOH751

Publications

  • Published on 6/20/2022

    Downs M, Zaia J, Sethi MK. Mass spectrometry methods for analysis of extracellular matrix components in neurological diseases. Mass Spectrom Rev. 2022 Jun 20; e21792. PMID: 35719114.

    Read at: PubMed
  • Published on 6/13/2022

    Lageveen-Kammeijer GSM, Rapp E, Chang D, Rudd PM, Kettner C, Zaia J. The minimum information required for a glycomics experiment (MIRAGE): reporting guidelines for capillary electrophoresis. Glycobiology. 2022 06 13; 32(7):580-587. PMID: 35348694.

    Read at: PubMed
  • Published on 4/19/2022

    Nalehua MR, Zaia J. Measuring change in glycoprotein structure. Curr Opin Struct Biol. 2022 Jun; 74:102371. PMID: 35452871.

    Read at: PubMed
  • Published on 3/30/2022

    Wu J, Chopra P, Boons GJ, Zaia J. Influence of saccharide modifications on heparin lyase III substrate specificities. Glycobiology. 2022 Mar 30; 32(3):208-217. PMID: 33822051.

    Read at: PubMed
  • Published on 2/23/2022

    Sethi MK, Downs M, Shao C, Hackett WE, Phillips JJ, Zaia J. In-Depth Matrisome and Glycoproteomic Analysis of Human Brain Glioblastoma Versus Control Tissue. Mol Cell Proteomics. 2022 Apr; 21(4):100216. PMID: 35202840.

    Read at: PubMed
  • Published on 2/2/2022

    Downs M, Sethi MK, Raghunathan R, Layne MD, Zaia J. Matrisome changes in Parkinson's disease. Anal Bioanal Chem. 2022 Apr; 414(9):3005-3015. PMID: 35112150.

    Read at: PubMed
  • Published on 1/28/2022

    Cavallero GJ, Zaia J. Resolving Heparan Sulfate Oligosaccharide Positional Isomers Using Hydrophilic Interaction Liquid Chromatography-Cyclic Ion Mobility Mass Spectrometry. Anal Chem. 2022 02 08; 94(5):2366-2374. PMID: 35090117.

    Read at: PubMed
  • Published on 1/1/2022

    Kawahara R, Chernykh A, Alagesan K, Bern M, Cao W, Chalkley RJ, Cheng K, Choo MS, Edwards N, Goldman R, Hoffmann M, Hu Y, Huang Y, Kim JY, Kletter D, Liquet B, Liu M, Mechref Y, Meng B, Neelamegham S, Nguyen-Khuong T, Nilsson J, Pap A, Park GW, Parker BL, Pegg CL, Penninger JM, Phung TK, Pioch M, Rapp E, Sakalli E, Sanda M, Schulz BL, Scott NE, Sofronov G, Stadlmann J, Vakhrushev SY, Woo CM, Wu HY, Yang P, Ying W, Zhang H, Zhang Y, Zhao J, Zaia J, Haslam SM, Palmisano G, Yoo JS, Larson G, Khoo KH, Medzihradszky KF, Kolarich D, Packer NH, Thaysen-Andersen M. Author Correction: Community evaluation of glycoproteomics informatics solutions reveals high-performance search strategies for serum glycopeptide analysis. Nat Methods. 2022 Jan; 19(1):130. PMID: 34893784.

    Read at: PubMed
  • Published on 11/1/2021

    Kawahara R, Chernykh A, Alagesan K, Bern M, Cao W, Chalkley RJ, Cheng K, Choo MS, Edwards N, Goldman R, Hoffmann M, Hu Y, Huang Y, Kim JY, Kletter D, Liquet B, Liu M, Mechref Y, Meng B, Neelamegham S, Nguyen-Khuong T, Nilsson J, Pap A, Park GW, Parker BL, Pegg CL, Penninger JM, Phung TK, Pioch M, Rapp E, Sakalli E, Sanda M, Schulz BL, Scott NE, Sofronov G, Stadlmann J, Vakhrushev SY, Woo CM, Wu HY, Yang P, Ying W, Zhang H, Zhang Y, Zhao J, Zaia J, Haslam SM, Palmisano G, Yoo JS, Larson G, Khoo KH, Medzihradszky KF, Kolarich D, Packer NH, Thaysen-Andersen M. Community evaluation of glycoproteomics informatics solutions reveals high-performance search strategies for serum glycopeptide analysis. Nat Methods. 2021 11; 18(11):1304-1316. PMID: 34725484.

    Read at: PubMed
  • Published on 10/12/2021

    Chang D, Klein JA, Nalehua MR, Hackett WE, Zaia J. Data-independent acquisition mass spectrometry for site-specific glycoproteomics characterization of SARS-CoV-2 spike protein. Anal Bioanal Chem. 2021 Dec; 413(29):7305-7318. PMID: 34635934.

    Read at: PubMed

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