N-linked glycosylation of VWF modulates its interaction with ADAMTS13

摘要: We examined the role of N-linked glycan structures VWF on its interaction with ADAMTS13. PNGase F digestion followed by lectin analysis demonstrated that more than 90% chains could be removed from molecule (PNG-VWF) without disruption multimeric structure or ability to bind collagen. PNG-VWF had an approximately 4-fold increased affinity for ADAMTS13 compared control VWF. was cleaved faster and also proteolysed in absence urea. Occupancy sites at N1515 N1574 their presentation ABO(H) blood group sugars were confirmed isolated tryptic fragment. Recombinant mutated prevent glycosylation these sites. Mutation did not alter binding increase rate proteolysis. susceptibility proteolysis allowed cleavage recombinant VWF-A2 domain These data demonstrate glycans have a modulatory effect At least part this is conformational, but steric hindrance may important.