Table I CSPGs identified in the present study with an intracellular distribution.
Protein nameaPeptide sequencebGlycan modificationcSample type
Intracellular granules CSPGs
    Bone marrow proteoglycan53ELEEEEEWGSGSEDASK69Embedded ImageUrine
    aCholecystokinin21QPVPPADPAGSGLQR35Embedded ImageCSF and Urine
    Chromogranin-A419KEEEGSANR427Embedded ImageCSF and Urine
    aCollagen and calcium-binding EGF domain-containing protein 1382DLGSGDDHPR391Embedded ImageUrine
    aDermcidin20YDPEAASAPGSGNPCHEASAAQK42Embedded ImageUrine
    aNeuropeptide W120APEPALEPESLDFSGAGQR138Embedded ImageCSF and Urine
    aSecretogranin-188DPADASEAHESSSR101Embedded ImageCSF and Urine
    aSecretogranin-1235SSQESGEETGSQENHPQESK254Embedded ImageCSF
    aSecretogranin-335ELSAERPLNEQIAEAEEDK53Embedded ImageUrine
  • a Indicate novel CSPGs identified in this study.

  • b Bold and underlined serine residues depict established attachment sites while bold depict probable attachment sites.

  • c The CS-hexasaccharide were identified either without or with sulfate (SO3) and/or phosphate (PO3) modifications and their positions on the hexasaccharide structure are indicated. The positioning and distinction of sulfate- (79.9663 Da) and phosphate (79.9568 Da) modifications were made by manually evaluating the MS2-spectra. When the expected modifications could not be identified a bracket including the whole hexasaccharide structure is presented as the expected modification could be, in theory, anywhere on the glycan.