N-glycosylation is required for efficient secretion of a novel human secreted glycoprotein, hPAP21.

Abstract:

:The present study reported the isolation and characterization of a novel human secreted protein, named as hPAP21 (human protease-associated domain-containing protein, 21 kDa), encoded by the hypothetical gene chromosome 2 open reading frame 7 (C2orf7) that contains signal peptide in its N-terminus, without transmembrane domain, except for PA domain in its middle. Western blotting assay indicated that the c-Myc tagged hPAP21 could be secreted into culture medium in the transfected Chinese hamster ovary cells. However, the molecular weights, whatever intracellular (28 kDa) or extracellular (30 kDa) forms, are larger than that of the prediction. To define whether the glycosylation was important process for its secretion, endoglycosidase H (Endo H) and PNGase F (PNG F) were employed to evaluate the effect of glycosylation types on secretion of hPAP21. Interestingly, the extracellular forms were primarily sensitive to PNG F, not Endo H, implying that complex N-glycosylation could be required for the secretion of hPAP21. Furthermore, N-glycosylation of Asn171 was confirmed as potential crucial process for the secretory protein via site-directed mutagenesis assay. All data will be contributed to the understanding of molecular functions of hPAP21.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Zhou YB,Liu F,Zhu ZD,Zhu H,Zhang X,Wang ZQ,Liu JH,Han ZG

doi

10.1016/j.febslet.2004.09.039

keywords:

subject

Has Abstract

pub_date

2004-10-22 00:00:00

pages

401-7

issue

3

eissn

0014-5793

issn

1873-3468

pii

S001457930401155X

journal_volume

576

pub_type

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