This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. C. elegans is one of the most thoroughly studied organisms for development, a process where carbohydrate recognition is important. Many databases exist for this organism. These include genomic, proteomic, expression, iRNA expression and anatomic databases. Databases such as the anatomic database are now being adopted to organize the anatomy of the organism as a hierarchy of tissue names and linking relationships within their tissue ontologies. Not only are whole organism data such as protein and RNA expression patterns now available, but such data is now being placed in the context of their expression throughout development in a tissue specific fashion. Currently, there is little information concerning the glycosylation and/or glycosylation patterns of specific proteins, glycolipids, or tissues, or throughout development. Since databases are now available that link protein and expression information to the stages of development and tissue location, the documentation of specific glycoprotein, glycolipid and tissue glycosylation patterns is now especially warranted. This project intends to document the glycosylation patterns found in glycoproteins using an LC-MS proteomics approach. The analysis of glycoproteins will provide tissue specific glycosylation information, as tissue specific protein expression databases exist for this organism. We will also continue to catalogue N-glycan, O-glycans and glycolipids in this organism with special attention to characteristic fragmentation patterns. The fragmentation patterns will be analysed for specific rules that apply in subsets of related compounds. These rules will aid in the structural assignment of compounds across species, as, C. elegans produces many glycans that are conserved in higher eukaryotes. C. elegans also contains novel glycoconjugates and, thus, rules that result from the study of these novel compounds may provide new insights for fragmentation mechanisms, patterns and ion chemistry in general. As data are accumulated it will be deposited into databases and software developed for their use.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR010888-10
Application #
7369318
Study Section
Special Emphasis Panel (ZRG1-BECM (03))
Project Start
2006-07-01
Project End
2007-06-30
Budget Start
2006-07-01
Budget End
2007-06-30
Support Year
10
Fiscal Year
2006
Total Cost
$7,730
Indirect Cost
Name
Boston University
Department
Biochemistry
Type
Schools of Medicine
DUNS #
604483045
City
Boston
State
MA
Country
United States
Zip Code
02118
Lu, Yanyan; Jiang, Yan; Prokaeva, Tatiana et al. (2017) Oxidative Post-Translational Modifications of an Amyloidogenic Immunoglobulin Light Chain Protein. Int J Mass Spectrom 416:71-79
Sethi, Manveen K; Zaia, Joseph (2017) Extracellular matrix proteomics in schizophrenia and Alzheimer's disease. Anal Bioanal Chem 409:379-394
Hu, Han; Khatri, Kshitij; Zaia, Joseph (2017) Algorithms and design strategies towards automated glycoproteomics analysis. Mass Spectrom Rev 36:475-498
Ji, Yuhuan; Bachschmid, Markus M; Costello, Catherine E et al. (2016) S- to N-Palmitoyl Transfer During Proteomic Sample Preparation. J Am Soc Mass Spectrom 27:677-85
Hu, Han; Khatri, Kshitij; Klein, Joshua et al. (2016) A review of methods for interpretation of glycopeptide tandem mass spectral data. Glycoconj J 33:285-96
Pu, Yi; Ridgeway, Mark E; Glaskin, Rebecca S et al. (2016) Separation and Identification of Isomeric Glycans by Selected Accumulation-Trapped Ion Mobility Spectrometry-Electron Activated Dissociation Tandem Mass Spectrometry. Anal Chem 88:3440-3
Wang, Yun Hwa Walter; Meyer, Rosana D; Bondzie, Philip A et al. (2016) IGPR-1 Is Required for Endothelial Cell-Cell Adhesion and Barrier Function. J Mol Biol 428:5019-5033
Srinivasan, Srimathi; Chitalia, Vipul; Meyer, Rosana D et al. (2015) Hypoxia-induced expression of phosducin-like 3 regulates expression of VEGFR-2 and promotes angiogenesis. Angiogenesis 18:449-62
Yu, Xiang; Sargaeva, Nadezda P; Thompson, Christopher J et al. (2015) In-Source Decay Characterization of Isoaspartate and ?-Peptides. Int J Mass Spectrom 390:101-109
Steinhorn, Benjamin S; Loscalzo, Joseph; Michel, Thomas (2015) Nitroglycerin and Nitric Oxide--A Rondo of Themes in Cardiovascular Therapeutics. N Engl J Med 373:277-80

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