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Methods Enzymol. 2010;480:401-16. doi: 10.1016/S0076-6879(10)80018-7.

O-fucosylation of thrombospondin type 1 repeats.

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Department of Biochemistry and Cell Biology, Institute for Cell and Developmental Biology, Stony Brook University, Stony Brook, New York, USA.


Thrombospondin type 1 repeats (TSRs) are small cysteine-rich motifs with three conserved disulfide bonds originally described as modules in the thrombospondins. Since then, TSRs have been found as tandem repeats in a wide variety of secreted and cell-surface proteins of diverse function. TSRs in many contexts are known to bind a variety of receptors and have antiangiogenic capabilities. They can be modified with O-linked fucose on serine/threonine found in the consensus, CX(2-3)(S/T)CX(2)G. Here we review what is known about O-fucosylation of TSRs and describe in detail mass spectral methods to map sites of O-fucosylation on proteins containing TSRs. These methods include techniques to identify glycosylated peptides and the relative amounts of elongated products by electrospray ionization mass spectrometry of glycopeptides.

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