| 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
|
|
WOS Category
|
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
| Resource |
| DNA material |
pCI-HYAL1 (RDB13307)
pCI-HYAL1-N99Q (RDB13308)
pCI-HYAL1-N216Q (RDB13309)
pCI-HYAL1-N350Q (RDB13310). |
