Brain α-dystroglycan displays unique glycoepitopes and preferential binding to laminin-10/11

Erin L. McDearmon; Ariana C. Combs; Kiyotoshi Sekiguchi; Hironobu Fujiwara; James M. Ervasti

doi:10.1016/j.febslet.2006.05.010

Brain α-dystroglycan displays unique glycoepitopes and preferential binding to laminin-10/11

Erin L. McDearmon, Ariana C. Combs, Kiyotoshi Sekiguchi, Hironobu Fujiwara, James M. Ervasti

Biochemistry, Molecular Biology, and Biophysics (TMED)

Research output: Contribution to journal › Article › peer-review

19 Scopus citations

Abstract

α-Dystroglycan was quantitatively enriched from mammalian brain based on its uniform reactivity with Vicia villosa agglutinin and resolved into sub-populations possessing or lacking the sulfated glucuronic acid epitope recognized by monoclonal antibody HNK-1. We generated a new monoclonal antibody specific for a glycoepitope on brain α-dystroglycan but absent from α-dystroglycan expressed in all other tissues examined. Finally, we found that laminin-10/11 preferentially bound to brain α-dystroglycan compared to skeletal muscle α-dystroglycan. Our results suggest that tissue-specific glycosylation modifies the laminin binding specificity of α-dystroglycan.

Original language	English (US)
Pages (from-to)	3381-3385
Number of pages	5
Journal	FEBS Letters
Volume	580
Issue number	14
DOIs	https://doi.org/10.1016/j.febslet.2006.05.010
State	Published - Jun 12 2006

Bibliographical note

Funding Information:
We thank Dr. Hynda Kleinman for laminin-1 and Mr. Travis Suss for technical assistance. Supported by the UW Medical School under the HHMI Research Resources Program for Medical Schools, the MDA, and NIH Grant ARO1985 to J.M.E. and a Predoctoral Fellowship from the Northland Affiliate of the AHA to E.L.M.

Keywords

Laminin
Oligosaccharide structure
α-Dystroglycan

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abstract = "α-Dystroglycan was quantitatively enriched from mammalian brain based on its uniform reactivity with Vicia villosa agglutinin and resolved into sub-populations possessing or lacking the sulfated glucuronic acid epitope recognized by monoclonal antibody HNK-1. We generated a new monoclonal antibody specific for a glycoepitope on brain α-dystroglycan but absent from α-dystroglycan expressed in all other tissues examined. Finally, we found that laminin-10/11 preferentially bound to brain α-dystroglycan compared to skeletal muscle α-dystroglycan. Our results suggest that tissue-specific glycosylation modifies the laminin binding specificity of α-dystroglycan.",

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AU - McDearmon, Erin L.

AU - Combs, Ariana C.

AU - Sekiguchi, Kiyotoshi

AU - Fujiwara, Hironobu

AU - Ervasti, James M.

N1 - Funding Information: We thank Dr. Hynda Kleinman for laminin-1 and Mr. Travis Suss for technical assistance. Supported by the UW Medical School under the HHMI Research Resources Program for Medical Schools, the MDA, and NIH Grant ARO1985 to J.M.E. and a Predoctoral Fellowship from the Northland Affiliate of the AHA to E.L.M.

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AB - α-Dystroglycan was quantitatively enriched from mammalian brain based on its uniform reactivity with Vicia villosa agglutinin and resolved into sub-populations possessing or lacking the sulfated glucuronic acid epitope recognized by monoclonal antibody HNK-1. We generated a new monoclonal antibody specific for a glycoepitope on brain α-dystroglycan but absent from α-dystroglycan expressed in all other tissues examined. Finally, we found that laminin-10/11 preferentially bound to brain α-dystroglycan compared to skeletal muscle α-dystroglycan. Our results suggest that tissue-specific glycosylation modifies the laminin binding specificity of α-dystroglycan.

KW - Laminin

KW - Oligosaccharide structure

KW - α-Dystroglycan

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Brain α-dystroglycan displays unique glycoepitopes and preferential binding to laminin-10/11

Abstract

Bibliographical note

Keywords

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