Journal
FEBS OPEN BIO
Volume 4, Issue -, Pages 554-559Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.fob.2014.06.001
Keywords
Hyaluronidase1; N-glycosylation; Enzymatic activity; Secretion
Categories
Funding
- [23310163]
- [24310167]
- [254256]
- Grants-in-Aid for Scientific Research [13J04256] Funding Source: KAKEN
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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. (C) 2014 The Authors. Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies. This is an open access article under the CC BY-NC-ND license.
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