Open AccessN ‐glycosylation is required for secretion and enzymatic activity of human hyaluronidase1
Author(s) -
Goto Yuki,
Niwa Yuki,
Suzuki Takehiro,
Uematsu Shiho,
Dohmae Naoshi,
Simizu Siro
Publication year - 2014
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1016/j.fob.2014.06.001
Subject(s) - glycosylation , secretion , enzyme , biochemistry , chemistry
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.