Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/8926
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Type: Journal article
Title: A novel activating anti-β1 integrin monoclonal antibody binds to the cysteine-rich repeats in the β1 chain
Other Titles: A novel activating anti-beta1 integrin monoclonal antibody binds to the cysteine-rich repeats in the beta1 chain
Author: Faull, R.
Wang, J.
Leavesley, D.
Puzon, W.
Russ, G.
Vestweber, D.
Takada, Y.
Citation: Journal of Biological Chemistry, 1996; 271(41):25099-25106
Publisher: American Society for Biochemistry and Molecular Biology
Issue Date: 1996
ISSN: 1083-351X
1083-351X
Statement of
Responsibility: 
Randall J. Faull, Jian Wang, David I. Leavesley, Wilma Puzon, Graeme R. Russ, Dietmar Vestweber and Yoshikazu Takada
Abstract: The functional status of an integrin depends on the conformation of its extracellular domain, which is controlled by the cell expressing that receptor. The transmission of regulatory signals from within the cell is considered to be via propagated conformational changes from the receptor's cytoplasmic tails to the extracellular ligand binding “pocket.” The end result is increased accessibility of the ligand binding pocket in the high affinity (“active”) form of integrins. We report a novel monoclonal antibody (QE.2E5) that binds within the cysteine-rich repeats in the integrin β1 chain and induces high affinity binding of fibronectin to the integrin α5β1. The QE.2E5 epitope is located approximately 200 residues both from the predicted binding site for fibronectin and from the epitopes recognized by other activating anti-β1 monoclonal antibodies. It is also expressed on β1 integrins from a number of nonhuman species. Although they have the same functional effects, the binding of QE.2E5 and another activating antibody (8A2) to the receptor have contrasting effects on the expression of an activation-dependent epitope in the β1 chain. We propose that the cysteine-rich repeats contain a regulatory region that is distinct from those previously described in the integrin β1 chain.
Keywords: Endothelium, Vascular
Umbilical Veins
Cell Line
Tumor Cells, Cultured
Animals
Mice, Inbred BALB C
Humans
Mice
Cysteine
Fibronectins
Recombinant Fusion Proteins
Antibodies, Monoclonal
Binding Sites, Antibody
Epitopes
Ligands
Cell Adhesion
Signal Transduction
Binding Sites
Amino Acid Sequence
Integrin beta1
Rights: © 1996 by The American Society for Biochemistry and Molecular Biology, Inc.
DOI: 10.1074/jbc.271.41.25099
Appears in Collections:Aurora harvest 4
Medicine publications

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