Localization of the epitope of a monoclonal antibody against human insulin-like growth factor binding protein-1, functionally interfering with insulin-like growth factor binding. 1993

A G Schuller, and D J Lindenbergh-Kortleve, and W I de Boer, and E C Zwarthoff, and S L Drop
Department of Pediatrics, Erasmus University/Sophia Childrens Hospital, Rotterdam, The Netherlands.

In order to identify regions in insulin-like growth factor binding protein-1 involved in the binding of IGFs, we tested three monoclonal antibodies, designated MAb A, B, and C on their interference with IGF-binding. Monoclonal A interfered with the binding of IGF to IGFBP-1 as determined by immunoprecipitation whereas monoclonal B and C did not. Furthermore MAb A was found to abolish IGFBP-1 inhibition of IGF stimulation in an in vitro proliferation assay. The epitopes of all three monoclonal antibodies were found to be located within the C-terminal part of IGFBP-1. The regions surrounding residue 188-196 and 222-227 are especially important for antibody recognition. These results indicate that MAb A functionally interferes with the binding of IGF to IGFBP-1. Furthermore, we suggest that part of the epitope of MAb A is located at or sterically near the IGF binding domain of IGFBP-1.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011993 Recombinant Fusion Proteins Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes. Fusion Proteins, Recombinant,Recombinant Chimeric Protein,Recombinant Fusion Protein,Recombinant Hybrid Protein,Chimeric Proteins, Recombinant,Hybrid Proteins, Recombinant,Recombinant Chimeric Proteins,Recombinant Hybrid Proteins,Chimeric Protein, Recombinant,Fusion Protein, Recombinant,Hybrid Protein, Recombinant,Protein, Recombinant Chimeric,Protein, Recombinant Fusion,Protein, Recombinant Hybrid,Proteins, Recombinant Chimeric,Proteins, Recombinant Fusion,Proteins, Recombinant Hybrid
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D006825 Hybridomas Cells artificially created by fusion of activated lymphocytes with neoplastic cells. The resulting hybrid cells are cloned and produce pure MONOCLONAL ANTIBODIES or T-cell products, identical to those produced by the immunologically competent parent cell. Hybridoma
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D000911 Antibodies, Monoclonal Antibodies produced by a single clone of cells. Monoclonal Antibodies,Monoclonal Antibody,Antibody, Monoclonal

Related Publications

A G Schuller, and D J Lindenbergh-Kortleve, and W I de Boer, and E C Zwarthoff, and S L Drop
February 1982, The Journal of clinical endocrinology and metabolism,
A G Schuller, and D J Lindenbergh-Kortleve, and W I de Boer, and E C Zwarthoff, and S L Drop
February 1992, Early human development,
A G Schuller, and D J Lindenbergh-Kortleve, and W I de Boer, and E C Zwarthoff, and S L Drop
January 2003, BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy,
A G Schuller, and D J Lindenbergh-Kortleve, and W I de Boer, and E C Zwarthoff, and S L Drop
November 2001, Thyroid : official journal of the American Thyroid Association,
A G Schuller, and D J Lindenbergh-Kortleve, and W I de Boer, and E C Zwarthoff, and S L Drop
January 1995, Annals of clinical and laboratory science,
A G Schuller, and D J Lindenbergh-Kortleve, and W I de Boer, and E C Zwarthoff, and S L Drop
July 1996, British journal of obstetrics and gynaecology,
A G Schuller, and D J Lindenbergh-Kortleve, and W I de Boer, and E C Zwarthoff, and S L Drop
December 2009, Zhongguo yi xue ke xue yuan xue bao. Acta Academiae Medicinae Sinicae,
A G Schuller, and D J Lindenbergh-Kortleve, and W I de Boer, and E C Zwarthoff, and S L Drop
January 1991, Annals of the New York Academy of Sciences,
A G Schuller, and D J Lindenbergh-Kortleve, and W I de Boer, and E C Zwarthoff, and S L Drop
March 1993, Growth regulation,
A G Schuller, and D J Lindenbergh-Kortleve, and W I de Boer, and E C Zwarthoff, and S L Drop
August 2018, Research in pharmaceutical sciences,
Copied contents to your clipboard!