Evidence map›Paper›PMID 19343721›Full record

ArticleProteomics2009

N-glycosylation microheterogeneity and site occupancy of an Asn-X-Cys sequon in plasma-derived and recombinant protein C.

Geun-Cheol Gil, William H Velander, Kevin E Van Cott

Open access · greenAbstract read
In one paragraph

Article in Proteomics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 1 synthesis or guideline pooled it, 46 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Towards understanding the extensive diversity of protein N-glycan structures in eukaryotes.Biological reviews of the Cambridge Philosophical Society · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. The atypical N-glycosylation motif, Asn-Cys-Cys, in human GPR109A is required for normal cell surface expression and intracellular signaling.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Geun-Cheol GilDepartment of Chemical and Biomolecular Engineering, University of Nebraska-Lincoln, Lincoln, NE 68588, USA.
William H Velander
Kevin E Van Cott
University of Nebraska–Lincoln · USReprogenetics · US

Funding

cGMP Recombinant FIX for IV &Oral Hemophilia B TherapyR01HL078944 · NHLBI · UNIVERSITY OF NEBRASKA LINCOLN · PI VELANDER, WILLIAM H · 2005 to 2009
$9.6M
NHLBI NIH HHS R01 HL078944
6 · The paper itself

Abstract

Human protein C (hPC) is glycosylated at three Asn-X-Ser/Thr and one atypical Asn-X-Cys sequons. We have characterized the micro- and macro-heterogeneity of plasma-derived hPC and compared the glycosylation features with recombinant protein C (tg-PC) produced in a transgenic pig bioreactor from two animals having approximately tenfold different expression levels. The N-glycans of hPC are complex di- and tri-sialylated structures, and we measured 78% site occupancy at Asn-329 (the Asn-X-Cys sequon). The N-glycans of tg-PC are complex sialylated structures, but less branched and partially sialylated. The porcine mammary epithelial cells glycosylate the Asn-X-Cys 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-PC. Interestingly, glycans with GalNAc in the antennae were predominant at the Asn-329 site. The N-glycan structures found for tg-PC 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-glycan processing in the porcine mammary epithelial cells is more uniform than in other tissues.

Indexed as

AnimalsAnimals, Genetically ModifiedAsparagineBioreactorsChromatography, High Pressure LiquidCysteineEpitheliumGlycopeptidesGlycosylationHumansMammary Glands, AnimalMass SpectrometryN-Acetylneuraminic AcidPlasmaProtein CRecombinant ProteinsAsparagineCysteineGlycopeptidesN-Acetylneuraminic AcidProtein CRecombinant Proteins

Identifiers

PMID19343721
PMCPMC2785108
OpenAlexW2113772656

What OpenQuestion holds

Textmetadata
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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.