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Papers In Press, published online ahead of print October 22, 2002
Pediatrics and Biochemistry, Case Western Reserve University, Cleveland, OH 44106
Corresponding Author: txg2{at}po.cwru.edu
The influence of peptide sequence and environment on the initiation and elongation of mucin O-glycosylation is not well understood. The in vivo glycosylation pattern of the porcine submaxillary gland mucin (PSM) tandem repeat containing 31 O-glycosylation sites (Gerken et. al. J. Biol. Chem. 277, 7736 (2002)), reveals a weak inverse correlation with hydroxyaminoacid density (and by inference the density of glycosylation) with the extent of GalNAc glycosylation and core-1 substitution. We now report the time course of in vitro glycosylation of the apo-PSM tandem repeat by recombinant ppGalNAc transferases T1 and T2 that confirm these findings. Found are a wide range of glycosylation rates, with several residues showing apparent plateaus in glycosylation. An adjustable kinetic model which reduces the first order rate constants proportional to neighboring glycosylation status, plus or minus three residues of the site of glycosylation, was found to reasonably reproduce the experimental rate data for both transferases, including apparent plateaus in glycosylation. The unique, transferase specific, positional weighting constants reveal information on each transferase's peptide/glycopeptide recognition site. Both transferases displayed high sensitivities to neighboring Ser/Thr glycosylation while ppGalNAc T2 displayed additional high sensitivities to the presence of nonglycosylated Ser/Thr residues. This is the first demonstration of the ability to model mucin O-glycosylation kinetics, confirming that under the appropriate conditions, neighboring glycosylation status can be a significant factor modulating the first step of mucin O-glycan biosynthesis.
J. Biol. Chem, 10.1074/jbc.M205851200
Submitted on June 12, 2002
Revised on October 3, 2002
Accepted on October 22, 2002
Mucin core O-glycosylation is modulated by neighboring residue glycosylation status: Kinetic modeling of the site specific glycosylation of the apo-porcine submaxillary mucin tandem repeat by UDP-GalNAc:Polypeptide N-acetylgalactosaminyltransferases T1 and T2
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