Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1987 Sep;84(18):6462-6.
doi: 10.1073/pnas.84.18.6462.

A monoclonal antibody against a family of nuclear pore proteins (nucleoporins): O-linked N-acetylglucosamine is part of the immunodeterminant

M K Park, M D'Onofrio, M C Willingham, J A Hanover

A monoclonal antibody against a family of nuclear pore proteins (nucleoporins): O-linked N-acetylglucosamine is part of the immunodeterminant

M K Park et al. Proc Natl Acad Sci U S A. 1987 Sep.

Abstract

Using nuclear envelopes from Chinese hamster ovary (CHO) cells as an antigen, a mouse monoclonal antibody (IgM; designated mAb CHON211) that specifically binds to components of the nuclear pore complex (nucleoporins) was isolated. Immunofluorescence localization of the antigen recognized by mAb CHON211 revealed a punctate pattern restricted to the nuclear envelope; this pattern changed dramatically during the cell cycle. When examined by electron microscopy, the antigen was largely restricted to the nucleoplasmic and cytoplasmic faces of the nuclear pore complex. Immunoblots showed that mAb CHON211 bound to a series of polypeptides enriched in the nuclear envelope fraction with apparent molecular masses ranging from 110 to 35 kDa. Using galactosyltransferase and the lectin wheat germ agglutinin as probes, we have previously shown that proteins bearing O-linked N-acetylglucosamine (GlcNAc) are restricted to the cytoplasmic and nucleoplasmic faces of the nuclear pore complex. The nuclear membrane proteins recognized by mAb CHON211 had properties very similar to those identified by galactosyltransferase and wheat germ agglutinin labeling. Removal of O-linked GlcNAc residues with beta-hexosaminidase greatly reduced the binding of mAb CHON211, strongly suggesting that O-linked GlcNAc moieties are part of the immunodeterminant. This monoclonal antibody defines a new family of antigens that are restricted to the nuclear pore and bear a common modification: O-linked GlcNAc. mAb CHON211 will be useful for defining the role of the nucleoporins in nucleo-cytoplasmic exchange.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Science. 1966 Dec 30;154(3757):1662-5 - PubMed
    1. Biochem Biophys Res Commun. 1972 Sep 26;48(6):1504-10 - PubMed
    1. J Biol Chem. 1973 May 10;248(9):3137-45 - PubMed
    1. J Cell Biol. 1976 Sep;70(3):581-91 - PubMed
    1. Biochim Biophys Acta. 1976 Sep 7;443(3):428-36 - PubMed

LinkOut - more resources