Joseph Zaia, PhD
Professor, Biochemistry & Cell Biology
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
Publications
- Published on 1/16/2025
Aoki-Kinoshita KF, Zaia J. Tools and databases for studying data in the glycosciences. Anal Bioanal Chem. 2025 Feb; 417(5):861-863. PMID: 39815128.
Read at: PubMed - Published on 1/1/2025
Chatterjee S, Zaia J, Sethi MK. Mass Spectrometry-Based Glycomics and Proteomics Profiling of On-Slide Digested Tissue from Complex Biological Samples. Methods Mol Biol. 2025; 2884:279-303. PMID: 39716010.
Read at: PubMed - Published on 7/22/2024
Klein J, Carvalho L, Zaia J. Expanding N-glycopeptide identifications by modeling fragmentation, elution, and glycome connectivity. Nat Commun. 2024 Jul 22; 15(1):6168. PMID: 39039063.
Read at: PubMed - Published on 7/11/2024
Xia C, Mernie E, Zaia J, Costello CE, Lin C. Accurate Collisional Cross Section Measurement by Multipass Cyclic Ion Mobility Spectrometry. Anal Chem. 2024 Jul 23; 96(29):11959-11968. PMID: 38990519.
Read at: PubMed - Published on 6/15/2024
Sethi MK, Maccioni R, Hogan JD, Kawamura T, Repunte-Canonigo V, Chen J, Zaia J, Sanna PP. Comprehensive Glycomic and Proteomic Analysis of Mouse Striatum and Lateral Hypothalamus Following Repeated Exposures to Cocaine or Methamphetamine. Mol Cell Proteomics. 2024 Aug; 23(8):100803. PMID: 38880242.
Read at: PubMed - Published on 4/26/2024
Chelini G, Mirzapourdelavar H, Durning P, Baidoe-Ansah D, Sethi MK, O'Donovan SM, Klengel T, Balasco L, Berciu C, Boyer-Boiteau A, McCullumsmith R, Ressler KJ, Zaia J, Bozzi Y, Dityatev A, Berretta S. Focal clusters of peri-synaptic matrix contribute to activity-dependent plasticity and memory in mice. Cell Rep. 2024 May 28; 43(5):114112. PMID: 38676925.
Read at: PubMed - Published on 2/15/2024
Nalehua MR, Zaia J. A critical evaluation of ultrasensitive single-cell proteomics strategies. Anal Bioanal Chem. 2024 Apr; 416(9):2359-2369. PMID: 38358530.
Read at: PubMed - Published on 1/25/2024
Hackett WE, Chang D, Carvalho L, Zaia J. RAMZIS: a bioinformatic toolkit for rigorous assessment of the alterations to glycoprotein composition that occur during biological processes. Bioinform Adv. 2024; 4(1):vbae012. PMID: 38384861.
Read at: PubMed - Published on 1/11/2024
Li R, Xia C, Wu S, Downs MJ, Tong H, Tursumamat N, Zaia J, Costello CE, Lin C, Wei J. Direct and Detailed Site-Specific Glycopeptide Characterization by Higher-Energy Electron-Activated Dissociation Tandem Mass Spectrometry. Anal Chem. 2024 Jan 23; 96(3):1251-1258. PMID: 38206681.
Read at: PubMed - Published on 12/21/2023
Zaarur N, Meriin AB, Singh M, Goel RK, Zaia J, Kandror KV. Akt may associate with insulin-responsive vesicles via interaction with sortilin. FEBS Lett. 2024 Feb; 598(4):390-399. PMID: 38105115.
Read at: PubMed
View 225 more publications: View full profile at BUMC