N-glycosylation is required for secretion and enzymatic activity of human hyaluronidase1

Yuki Goto, Yuki Niwa, Takehiro Suzuki, Shiho Uematsu, Naoshi Dohmae, Siro Simizu

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

Hyaluronidase1 (HYAL1) is a hydrolytic enzyme that degrades hyaluronic acid (HA) and has three predicted N-glycosylation sites at Asn99, Asn216, and Asn350. 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.

Original languageEnglish
Pages (from-to)554-559
Number of pages6
JournalFEBS Open Bio
Volume4
DOIs
Publication statusPublished - 2014

Keywords

  • Enzymatic activity
  • Hyaluronidase1
  • N-glycosylation
  • Secretion

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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