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Competition for FcRn-mediated transport gives rise to short half-life of human IgG3 and offers thera...

Competition for FcRn-mediated transport gives rise to short half-life of human IgG3 and offers thera...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3247843

Competition for FcRn-mediated transport gives rise to short half-life of human IgG3 and offers therapeutic potential

About this item

Full title

Competition for FcRn-mediated transport gives rise to short half-life of human IgG3 and offers therapeutic potential

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2011-12, Vol.2 (1), p.599, Article 599

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Human IgG3 displays the strongest effector functions of all IgG subclasses but has a short half-life for unresolved reasons. Here we show that IgG3 binds to IgG-salvage receptor (FcRn), but that FcRn-mediated transport and rescue of IgG3 is inhibited in the presence of IgG1 due to intracellular competition between IgG1 and IgG3. We reveal that this...

Alternative Titles

Full title

Competition for FcRn-mediated transport gives rise to short half-life of human IgG3 and offers therapeutic potential

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3247843

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3247843

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/ncomms1608

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