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 Lettjournal_title
FEBS lettersauthors
Zhou YB,Liu F,Zhu ZD,Zhu H,Zhang X,Wang ZQ,Liu JH,Han ZGdoi
10.1016/j.febslet.2004.09.039keywords:
subject
Has Abstractpub_date
2004-10-22 00:00:00pages
401-7issue
3eissn
0014-5793issn
1873-3468pii
S001457930401155Xjournal_volume
576pub_type
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