RRC ID 34908
Author Goto Y, Niwa Y, Suzuki T, Uematsu S, Dohmae N, Simizu S.
Title N-glycosylation is required for secretion and enzymatic activity of human hyaluronidase1.
Journal FEBS Open Bio
Abstract Hyaluronidase1 (HYAL1) is a hydrolytic enzyme that degrades hyaluronic acid (HA) and has three predicted N-glycosylation sites at Asn(99), Asn(216), and Asn(350). In this report, we show the functional significance of N-glycosylation on HYAL1 functions. Using mass spectrometry, we demonstrated that HYAL1 was N-glycosylated at the three asparagine residues. N-glycosylation of HYAL1 is important for secretion of HYAL1, as demonstrated by site-directed mutation. Moreover, a defect of N-glycosylation attenuated the enzymatic activity of HYAL1. Thus, HYAL1 is N-glycosylated at the three asparagine residues, and its secretion and enzymatic activity are regulated by N-glycosylation.
Volume 4
Pages 554-9
Published 2014-1-1
DOI 10.1016/j.fob.2014.06.001
PII S2211-5463(14)00056-4
PMID 25009769
PMC PMC4087149
IF 2.231
Times Cited 22
DNA material pCI-HYAL1 (RDB13307) pCI-HYAL1-N99Q (RDB13308) pCI-HYAL1-N216Q (RDB13309) pCI-HYAL1-N350Q (RDB13310).