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Blood, Vol. 112, Issue 9, 3744-3752, November 1, 2008
E-selectin receptors on human leukocytes
Blood Nimrichter et al.
112: 3744
Supplemental materials for: Nimrichter et al
Files in this Data Supplement:
- Table S1. Relative abundance of monosialo poly-LacNAc glycosphingolipids in human leukocytes (PDF, 377 KB) -
Abundance is based on MALDI-TOF MS peaks. Poly-LacNAc GSLs with the general structure NeuAcα2-3(Fuc)0–1Galβ1-4GlcNAcβ1-3nGalβ1-4Glcβ1Cer are designated in an abbreviated form (n/m) where “n” is the number of LacNAc repeats and “m” the number of fucose residues.
- Figure S1. Relative abundance of LacNAc and poly-LacNAc sialoglycosphingolipids in human leukocytes (PDF, 126 KB) -
Monosialo GSLs were purified from human leukocytes and resolved by HPLC with detection by UV absorbance at 215 nm. Fractions were collected and subjected to MALDI-TOF MS for structural assignment. Structures are given as “n/m” of the general structure NeuAcα2-3Galβ1-4(Fucα1-3)0–1GlcNAcβ1-3nGalβ1-4GlcβCer, where n is the number of LacNAc repeats and m the number of fucoses. The peak areas corresponding to each structure, expressed as a percent of the summed LacNAc and poly-LacNAc peak areas is shown in black. For comparison, the summed signals of the corresponding masses from MALDI-TOF MS analysis of the mixture of monosialo GSLs, expressed as a percent of the summed LacNAc and poly-LacNAc signals, is shown in grey. Not all masses were assigned peaks in HPLC. Note the good quantitative correlation between the two methods.
- Figure S2. Total ion mapping of leukocyte monosialoglycosphingolipids (PDF, 14.2 MB) -
Primary data from total ion mapping nanospray ionization MSn performed on permethylated oligosaccharides released from the monosialoglycosphingolipid fraction purified from human leukocytes. For fucosylated species, MSn data are provided that allow assignment of the positions of the Fuc residues on the corresponding poly-LacNAc chain. Details of the method can be found in the text and in Aoki, et al. (Aoki, K., Perlman, M., Lim, J. M., Cantu, R., Wells, L., and Tiemeyer, M. (2007) J. Biol. Chem. 282, 9127-9142). Structures are abbreviated as “n/m” where n is the number of LacNAc repeats and m the number of fucoses in the general structure NeuAcα2¬3Galβ1-4(Fucα1-3)0–1GlcNAcβ1-3nGalβ1-4GlcβCer. Symbol nomenclature is that adopted by the Consortium for Functional Glycomics (http://glycomics.scripps.edu/CFGnomenclature.pdf).
- Figure S3. Total ion mapping of E-selectin binding glycosphingolipid (PDF, 4.75 MB) -
The following pages contain primary data from total ion mapping nanospray ionization MSn performed on the permethylated oligosaccharides released from the major E-selectin binding glycosphingolipid from human leukocytes. MSn data are provided that allow assignment of the positions of the Fuc residues on the poly-LacNAc chain. Details of the method can be found in the text and in Aoki, et al. (Aoki, K., Perlman, M., Lim, J. M., Cantu, R., Wells, L., and Tiemeyer, M. (2007) J. Biol. Chem. 282, 9127-9142). The “5/2” designation refers to general structure NeuAcα2-3Galβ1-4 (Fucα1-3)0–1GlcNAcβ1-3nGalβ1-4GlcβCer, in which there are 5 LacNAc repeats and 2 fucose residues. Symbol nomenclature is that adopted by the Consortium for Functional Glycomics (http://glycomics.scripps.edu/CFGnomenclature.pdf).
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