Evidence map›Paper›PMID 10859341›Full record

ArticleThe Journal of experimental medicine2000

The N-glycans determine the differential blood clearance and hepatic uptake of human immunoglobulin (Ig)A1 and IgA2 isotypes.

A Rifai, K Fadden, S L Morrison, K R Chintalacharuvu

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
7.2field-weighted citation impact, top 3% 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

59 citing papers in PubMed, 160 citations in OpenAlex.

  1. Review
  2. Structural promiscuity in the human circulatory IgA1 clonal repertoire.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Immunoglobulin A carries sulfated andFrontiers in molecular biosciences · 2025
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. History of IgA Nephropathy Mouse Models.Journal of clinical medicine · 2021
    Review
  19. Article
  20. Review
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

4 authors at 2 institutions in 1 country.

A RifaiDepartment of Pathology, Rhode Island Hospital, Brown University, Providence, Rhode Island 02903, USA.
K Fadden
S L Morrison
K R Chintalacharuvu
Brown University · USUniversity of California, Los Angeles · US

Funding

GLYCOSYLATION AND ANTIBODY FUNCTIONR37AI029470 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MORRISON, SHERIE L · 1996 to 2005
$1.6M
RECOMBINANT ANTIBODIES FOR INFANT PROTECTIONR01AI039187 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MORRISON, SHERIE L · 1995 to 2004
$1.5M
GLYCOSYLATION AND ANTIBODY FUNCTIONR01AI029470 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MORRISON, SHERIE L · 1991 to 1995
–
NIAID NIH HHS AI08994NIAID NIH HHS AI29470NIAID NIH HHS AI39187NIAID NIH HHS R01 AI039187NIAID NIH HHS R37 AI029470
6 · The paper itself

Abstract

Human immunoglobulin (Ig)A exists in blood as two isotypes, IgA1 and IgA2, with IgA2 present as three allotypes: IgA2m(1), IgA2m(2), and IgA2m(n). We now demonstrate that recombinant, chimeric IgA1 and IgA2 differ in their pharmacokinetic properties. The major pathway for the clearance of all IgA2 allotypes is the liver. Liver-mediated uptake is through the asialoglycoprotein receptor (ASGR), since clearance can be blocked by injection of excess galactose-Ficoll ligand and suppressed in ASGR-deficient mice. In contrast, only a small percentage of IgA1 is cleared through this pathway. The clearance of IgA1 lacking the hinge region with its associated O-linked carbohydrate was more rapid than that of wild-type IgA1. IgA1 and IgA2 that are not rapidly eliminated by the ASGR are both removed through an undefined ASGR-independent pathway with half-lives of 14 and 10 h, respectively. The rapid clearance of IgA2 but not IgA1 through the liver may in part explain why the serum levels of IgA1 are greater than those of IgA2. In addition, dysfunction of the ASGR or altered N-linked glycosylation, but not O-glycans, that affects recognition by this receptor may account for the elevated serum IgA seen in liver disease and IgA nephropathy.

Indexed as

AnimalsAntibodiesAsialoglycoprotein ReceptorGlycoproteinsGlycosylationHumansImmunoglobulin AImmunoglobulin AllotypesImmunoglobulin IsotypesLiverMetabolic Clearance RateMiceMice, Mutant StrainsMolecular WeightReceptors, Cell SurfaceRecombinant ProteinsAntibodiesAsialoglycoprotein ReceptorGlycoproteinsImmunoglobulin AImmunoglobulin AllotypesImmunoglobulin Isotypespolymeric IgAReceptors, Cell SurfaceRecombinant Proteins

Identifiers

PMID10859341
PMCPMC2193211
OpenAlexW2114571489

What OpenQuestion holds

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LicenceCC BY-NC-SA
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Registered trials

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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.