RRC ID |
34908
|
著者 |
Goto Y, Niwa Y, Suzuki T, Uematsu S, Dohmae N, Simizu S.
|
タイトル |
N-glycosylation is required for secretion and enzymatic activity of human hyaluronidase1.
|
ジャーナル |
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.
|
巻・号 |
4
|
ページ |
554-9
|
公開日 |
2014-1-1
|
DOI |
10.1016/j.fob.2014.06.001
|
PII |
S2211-5463(14)00056-4
|
PMID |
25009769
|
PMC |
PMC4087149
|
IF |
2.231
|
引用数 |
22
|
WOS 分野
|
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
リソース情報 |
遺伝子材料 |
pCI-HYAL1 (RDB13307)
pCI-HYAL1-N99Q (RDB13308)
pCI-HYAL1-N216Q (RDB13309)
pCI-HYAL1-N350Q (RDB13310). |