{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T23:44:26Z","timestamp":1790120666043,"version":"4.0.1"},"reference-count":32,"publisher":"Wiley","issue":"9","license":[{"start":{"date-parts":[[2009,4,2]],"date-time":"2009-04-02T00:00:00Z","timestamp":1238630400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000050","name":"National Heart, Lung, and Blood Institute","doi-asserted-by":"crossref","award":["R01 HL078944-01"],"award-info":[{"award-number":["R01 HL078944-01"]}],"id":[{"id":"10.13039\/100000050","id-type":"DOI","asserted-by":"crossref"}]},{"name":"University of Nebraska"}],"content-domain":{"domain":["analyticalsciencejournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Proteomics"],"published-print":{"date-parts":[[2009,5]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Human protein C (hPC) is glycosylated at three Asn\u2010X\u2010Ser\/Thr and one atypical Asn\u2010X\u2010Cys sequons. We have characterized the micro\u2010 and macro\u2010heterogeneity of plasma\u2010derived hPC and compared the glycosylation features with recombinant protein C (tg\u2010PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels. The N\u2010glycans of hPC are complex di\u2010 and tri\u2010sialylated structures, and we measured 78% site occupancy at Asn\u2010329 (the Asn\u2010X\u2010Cys sequon). The N\u2010glycans of tg\u2010PC are complex sialylated structures, but less branched and partially sialylated. The porcine mammary epithelial cells glycosylate the Asn\u2010X\u2010Cys sequon with a similar efficiency as human hepatocytes even at these high expression levels, and site occupancy at this sequon was not affected by expression level. A distinct bias for particular structures was present at each of the four glycosylation sites for both hPC and tg\u2010PC. Interestingly, glycans with GalNAc in the antennae were predominant at the Asn\u2010329 site. The N\u2010glycan structures found for tg\u2010PC are very similar to those reported for a recombinant Factor IX produced in transgenic pig milk, and similar to the endogenous milk protein lactoferrin, which may indicate that N\u2010glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.<\/jats:p>","DOI":"10.1002\/pmic.200800775","type":"journal-article","created":{"date-parts":[[2009,4,2]],"date-time":"2009-04-02T05:25:55Z","timestamp":1238649955000},"page":"2555-2567","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":42,"title":["N\u2010glycosylation microheterogeneity and site occupancy of an Asn\u2010X\u2010Cys sequon in plasma\u2010derived and recombinant protein C"],"prefix":"10.1002","volume":"9","author":[{"given":"Geun\u2010Cheol","family":"Gil","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William H.","family":"Velander","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kevin E.","family":"Van Cott","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,4,28]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI109521"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.3029867"},{"key":"e_1_2_1_4_2","doi-asserted-by":"crossref","first-page":"19710","DOI":"10.1016\/S0021-9258(18)41833-9","article-title":"Post\u2010translational processing events in the secretion pathway of human protein C, a complex vitamin K\u2010dependent antithrombotic factor","volume":"267","author":"McClure D. 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