Title : 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
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. N-glycosylation, , glycoprotein, -, -
- 0. N-glycosylation, , hPAP21, -, -
- 0. glycoprotein, , glycoprotein, -, -
- 0. glycoprotein, , hPAP21, -, -
- 5. N-glycosylation, , hPAP21, -, -
- 6. N-glycosylation, , -, -, Asn171
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):