Title : Rat platelets contain glycosylated and non-glycosylated forms of
platelet factor 4
Abstract :
- Identification and characterization by mass spectrometry
- Platelet factor 4 is a heparin-binding protein released from the alpha granules of activated platelets
- This study describes the purification and identification of two forms of rat platelet factor 4 , the previously characterized non-glycosylated form of 7 kDa and an additional glycosylated form of molecular mass 9 kDa
- The two proteins both neutralized the antithrombin-III-dependent inhibitory activity of heparin
- Although their amino acid com position was found to be the same, in the N-terminal sequence of the 9-kDa protein , the second threonine residue could not be detected and a difference of 976Da was determined by mass spectrometry
- After digestion with O-glycanase and sialidase , the two proteins showed the same molecular mass
- Overall consideration of these data led to identification of the higher-molecular-mass protein as a glycosylated form of rat platelet factor 4 with O-glycosylation at the second N-terminal amino acid, while the structure of the oligosaccharide core was established by mass spectrometry and sugar differentiation with lectins
- The two forms of platelet factor 4 are both present in platelets and secreted after platelet activation
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. glycosylated, , platelet factor 4, -, -
- 0. non-glycosylated, , platelet factor 4, -, -
- 7. O-glycosylation, , platelet factor 4, -, -
- 7. glycosylated, , platelet factor 4, -, -
Output(Part-Of) (sent_index,
protein,
site):
- 5. -, position
- 5. 9-kDa protein, sequence
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):