The immunoglobulin-superfamily molecule basigin is a binding protein for oligomannosidic carbohydrates: an anti-idiotypic approach.

Martin Heller; Maren von der Ohe; Ralf Kleene; M Hasan Mohajeri; Melitta Schachner

The immunoglobulin-superfamily molecule basigin is a binding protein for oligomannosidic carbohydrates: an anti-idiotypic approach.

Standard

The immunoglobulin-superfamily molecule basigin is a binding protein for oligomannosidic carbohydrates: an anti-idiotypic approach. / Heller, Martin; von der Ohe, Maren; Kleene, Ralf; Mohajeri, M Hasan; Schachner, Melitta.

In: J NEUROCHEM, Vol. 84, No. 3, 3, 2003, p. 557-565.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Heller, M, von der Ohe, M, Kleene, R, Mohajeri, MH & Schachner, M 2003, 'The immunoglobulin-superfamily molecule basigin is a binding protein for oligomannosidic carbohydrates: an anti-idiotypic approach.', J NEUROCHEM, vol. 84, no. 3, 3, pp. 557-565. <http://www.ncbi.nlm.nih.gov/pubmed/12558975?dopt=Citation>

APA

Heller, M., von der Ohe, M., Kleene, R., Mohajeri, M. H., & Schachner, M. (2003). The immunoglobulin-superfamily molecule basigin is a binding protein for oligomannosidic carbohydrates: an anti-idiotypic approach. J NEUROCHEM, 84(3), 557-565. [3]. http://www.ncbi.nlm.nih.gov/pubmed/12558975?dopt=Citation

Vancouver

Heller M, von der Ohe M, Kleene R, Mohajeri MH, Schachner M. The immunoglobulin-superfamily molecule basigin is a binding protein for oligomannosidic carbohydrates: an anti-idiotypic approach. J NEUROCHEM. 2003;84(3):557-565. 3.

Bibtex

@article{f0d4b5cffd4e4febaa9fa33ec8ef1451,

title = "The immunoglobulin-superfamily molecule basigin is a binding protein for oligomannosidic carbohydrates: an anti-idiotypic approach.",

abstract = "Recognition molecules that carry carbohydrate structures regulate cell interactions during development and play important roles in synaptic plasticity and regeneration in the adult. Glycans appear to be involved in these interactions. We have searched for binding proteins for oligomannosidic structures using the L3 antibody directed against high mannose-type glycans in an anti-idiotypic approach. A selected monoclonal anti-idiotype antibody was used for affinity chromatography and identified basigin as a binding protein from mouse brain detergent lysates. Basigin was found to bind to high mannose-carrying cell recognition molecules, such as myelin-associated glycoprotein, L1, the beta2-subunit of Na+/K+-ATPase and an oligomannosidic neoglycolipid. Furthermore, basigin was involved in outgrowth of astrocytic processes in vitro. A striking homology between the first immunoglobulin (Ig)-like domain of basigin and the fourth Ig-like domain of NCAM, previously shown to bind to oligomannosidic glycans, and the lectin domain of the mannose receptor confirms that basigin is an oligomannose binding lectin. To our knowledge this is the first report that anti-idiotypic antibodies can be used to identify binding partners for carbohydrates.",

keywords = "Animals, Cells, Cultured, Mice, Amino Acid Sequence, Molecular Sequence Data, Sequence Homology, Amino Acid, Brain Chemistry, Neural Cell Adhesion Molecule L1/metabolism, Antigens, CD147, Chromatography, Affinity, Antibody Specificity, Antibodies, Anti-Idiotypic/chemistry/*metabolism, Antibodies, Monoclonal/chemistry/metabolism, *Antigens, CD, *Antigens, Neoplasm, *Antigens, Surface, Astrocytes/cytology/metabolism, *Avian Proteins, *Blood Proteins, Carrier Proteins/genetics/immunology/*metabolism, Immunoglobulins/genetics/immunology/*metabolism, Membrane Glycoproteins/genetics/immunology/*metabolism, Myelin-Associated Glycoprotein/metabolism, Neural Cell Adhesion Molecules/genetics, Oligosaccharides/immunology/*metabolism, Polysaccharides/chemistry/metabolism, Protein Structure, Tertiary/physiology, Sodium-Potassium-Exchanging ATPase/metabolism, Animals, Cells, Cultured, Mice, Amino Acid Sequence, Molecular Sequence Data, Sequence Homology, Amino Acid, Brain Chemistry, Neural Cell Adhesion Molecule L1/metabolism, Antigens, CD147, Chromatography, Affinity, Antibody Specificity, Antibodies, Anti-Idiotypic/chemistry/*metabolism, Antibodies, Monoclonal/chemistry/metabolism, *Antigens, CD, *Antigens, Neoplasm, *Antigens, Surface, Astrocytes/cytology/metabolism, *Avian Proteins, *Blood Proteins, Carrier Proteins/genetics/immunology/*metabolism, Immunoglobulins/genetics/immunology/*metabolism, Membrane Glycoproteins/genetics/immunology/*metabolism, Myelin-Associated Glycoprotein/metabolism, Neural Cell Adhesion Molecules/genetics, Oligosaccharides/immunology/*metabolism, Polysaccharides/chemistry/metabolism, Protein Structure, Tertiary/physiology, Sodium-Potassium-Exchanging ATPase/metabolism",

author = "Martin Heller and {von der Ohe}, Maren and Ralf Kleene and Mohajeri, {M Hasan} and Melitta Schachner",

year = "2003",

language = "English",

volume = "84",

pages = "557--565",

journal = "J NEUROCHEM",

issn = "0022-3042",

publisher = "Wiley-Blackwell",

number = "3",

}

RIS

TY - JOUR

T1 - The immunoglobulin-superfamily molecule basigin is a binding protein for oligomannosidic carbohydrates: an anti-idiotypic approach.

AU - Heller, Martin

AU - von der Ohe, Maren

AU - Kleene, Ralf

AU - Mohajeri, M Hasan

AU - Schachner, Melitta

PY - 2003

Y1 - 2003

N2 - Recognition molecules that carry carbohydrate structures regulate cell interactions during development and play important roles in synaptic plasticity and regeneration in the adult. Glycans appear to be involved in these interactions. We have searched for binding proteins for oligomannosidic structures using the L3 antibody directed against high mannose-type glycans in an anti-idiotypic approach. A selected monoclonal anti-idiotype antibody was used for affinity chromatography and identified basigin as a binding protein from mouse brain detergent lysates. Basigin was found to bind to high mannose-carrying cell recognition molecules, such as myelin-associated glycoprotein, L1, the beta2-subunit of Na+/K+-ATPase and an oligomannosidic neoglycolipid. Furthermore, basigin was involved in outgrowth of astrocytic processes in vitro. A striking homology between the first immunoglobulin (Ig)-like domain of basigin and the fourth Ig-like domain of NCAM, previously shown to bind to oligomannosidic glycans, and the lectin domain of the mannose receptor confirms that basigin is an oligomannose binding lectin. To our knowledge this is the first report that anti-idiotypic antibodies can be used to identify binding partners for carbohydrates.

AB - Recognition molecules that carry carbohydrate structures regulate cell interactions during development and play important roles in synaptic plasticity and regeneration in the adult. Glycans appear to be involved in these interactions. We have searched for binding proteins for oligomannosidic structures using the L3 antibody directed against high mannose-type glycans in an anti-idiotypic approach. A selected monoclonal anti-idiotype antibody was used for affinity chromatography and identified basigin as a binding protein from mouse brain detergent lysates. Basigin was found to bind to high mannose-carrying cell recognition molecules, such as myelin-associated glycoprotein, L1, the beta2-subunit of Na+/K+-ATPase and an oligomannosidic neoglycolipid. Furthermore, basigin was involved in outgrowth of astrocytic processes in vitro. A striking homology between the first immunoglobulin (Ig)-like domain of basigin and the fourth Ig-like domain of NCAM, previously shown to bind to oligomannosidic glycans, and the lectin domain of the mannose receptor confirms that basigin is an oligomannose binding lectin. To our knowledge this is the first report that anti-idiotypic antibodies can be used to identify binding partners for carbohydrates.

KW - Animals

KW - Cells, Cultured

KW - Mice

KW - Amino Acid Sequence

KW - Molecular Sequence Data

KW - Sequence Homology, Amino Acid

KW - Brain Chemistry

KW - Neural Cell Adhesion Molecule L1/metabolism

KW - Antigens, CD147

KW - Chromatography, Affinity

KW - Antibody Specificity

KW - Antibodies, Anti-Idiotypic/chemistry/metabolism

KW - Antibodies, Monoclonal/chemistry/metabolism

KW - Antigens, CD

KW - Antigens, Neoplasm

KW - Antigens, Surface

KW - Astrocytes/cytology/metabolism

KW - Avian Proteins

KW - Blood Proteins

KW - Carrier Proteins/genetics/immunology/metabolism

KW - Immunoglobulins/genetics/immunology/metabolism

KW - Membrane Glycoproteins/genetics/immunology/metabolism

KW - Myelin-Associated Glycoprotein/metabolism

KW - Neural Cell Adhesion Molecules/genetics

KW - Oligosaccharides/immunology/metabolism

KW - Polysaccharides/chemistry/metabolism

KW - Protein Structure, Tertiary/physiology

KW - Sodium-Potassium-Exchanging ATPase/metabolism