Skip to main content
. 2014 Oct 17;14(1):41–49. doi: 10.1074/mcp.M114.043703

Table I. CSPGs identified in the present study with an intracellular distribution.

Protein namea Peptide sequenceb Glycan modificationc Sample type
Intracellular granules CSPGs
    Bone marrow proteoglycan 53ELEEEEEWGSGSEDASK69 graphic file with name zjw0011549320006.jpg Urine
    aCholecystokinin 21QPVPPADPAGSGLQR35 graphic file with name zjw0011549320007.jpg CSF and Urine
    Chromogranin-A 419KEEEGSANR427 graphic file with name zjw0011549320008.jpg CSF and Urine
    aCollagen and calcium-binding EGF domain-containing protein 1 382DLGSGDDHPR391 graphic file with name zjw0011549320009.jpg Urine
    aDermcidin 20YDPEAASAPGSGNPCHEASAAQK42 graphic file with name zjw0011549320010.jpg Urine
    aNeuropeptide W 120APEPALEPESLDFSGAGQR138 graphic file with name zjw0011549320011.jpg CSF and Urine
    aSecretogranin-1 88DPADASEAHESSSR101 graphic file with name zjw0011549320012.jpg CSF and Urine
    aSecretogranin-1 235SSQESGEETGSQENHPQESK254 graphic file with name zjw0011549320013.jpg CSF
    aSecretogranin-3 35ELSAERPLNEQIAEAEEDK53 graphic file with name zjw0011549320014.jpg Urine

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.