Abstract
We have used an Escherichia coli expression system to produce forms of vascular cell-adhesion molecule-1 (VCAM-1) containing the first two and three supposed immunoglobulin-like domains. A form consisting of the first two domains of VCAM-1 is shown to promote very-late antigen-4-dependent spreading of a melanoma cell line comparable to that found for the equivalent region in the full seven-domain form. Preliminary structural analysis by CD and NMR is consistent with an immunoglobulin fold which is predicted from sequence comparison studies.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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Cell Adhesion
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Cell Adhesion Molecules / chemistry*
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Cell Adhesion Molecules / genetics
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Cell Adhesion Molecules / pharmacology
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Circular Dichroism
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Escherichia coli / genetics
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Gene Expression*
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Humans
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Integrin alpha4beta1
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Integrins / metabolism*
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Magnetic Resonance Spectroscopy
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Melanoma / pathology
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Peptide Fragments / chemistry*
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Peptide Fragments / genetics
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Peptide Fragments / pharmacology
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Protein Structure, Secondary
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Receptors, Very Late Antigen / metabolism*
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Recombinant Proteins / chemistry
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Recombinant Proteins / pharmacology
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Structure-Activity Relationship
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Tumor Cells, Cultured
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Vascular Cell Adhesion Molecule-1
Substances
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Cell Adhesion Molecules
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Integrin alpha4beta1
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Integrins
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Peptide Fragments
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Receptors, Very Late Antigen
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Recombinant Proteins
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Vascular Cell Adhesion Molecule-1