Stage-specific embryonic antigen (SSEA) glycosphingolipids (GSLs) found in the central nervous system are impficated in regulating cell-cell recognition, targeting and migration of cells during development. Through the action of fucosyltransferase enzymes, SSEA-1 (Lewis~ glycolipids arebiosynthesized in the brain by fucosylation of lipid substrates with the neolacto series glycolipid core structure [Galp 1-4GIcNAcp 1-3Galp 1-4GIcp I- I'Cer] (originally termed paragloboside) or its higher analogs. In order to optimize methodology for high sensitivity structural determinations of SSEA-1 type glycofipids from fetal calf brain, potential precursors and SSEA-1 glycolipids of previously established structure were first isolated from bovine erythrocytes and beige mutant mouse kidney, purified by colurnn chromatography and characterized by MALDI-TOF MS, LSIM[S, and M[S/M[S, among other techniques. Peracetylated derivatives were detected at the low ferntomole level by MALDI-TOF MS and the subnanomole level by LSIMS. MALDI-TOF MS produced mainly [M+Na]' and [M+K]' species. On the basis of the direct and tandem mass spectral analyses of peracetylated and permethylated derivatives, the carbohydrate sequences in the selected bovine erythrocyte and mouse kidney GSL fractions were found to be consistent with those of glycolipids previously reported from larger-scale studies of these sources. Their heterogeneous ceramide moieties were characterized by CID M[S/M[S of abundant Zo-type ions in the LS1 mass spectra of the permethylated GSLs. MALDI-PSD-TOF mass spectral analyses of low and subpicomole amounts of derivatized GSL fractions from fetal calf brain provided carbohydrate sequence information that indicates the presence of mono- and difucosylated SSEA-I neolacto series glycolipids and their nonfucosylated analogs.

National Institute of Health (NIH)
National Center for Research Resources (NCRR)
Biotechnology Resource Grants (P41)
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Boston University
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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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