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KMID : 0043320070300121584
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Archives of Pharmacal Research
2007 Volume.30 No. 12 p.1584 ~ p.1589
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ProteoChip-based Library Screening of Integrin α5β1 Antagonists from Korean Medicinal Plant ExtractsIntegrins consist of transmembrane glycoproteins noncovalently associated to form αβ heterodimers. Various α/β associations determine binding specieficities for cell surface molecules of the immunoglobulin superfamily as well as for extracellular matrix components. Through their cytoplasmic domains, integrins are responsible for the transmission of signals between the intracellular and the extracellular environment. We immobilized an integrin α5β1 microarray on a ProteoChip to screen Korean medicinal plant extracts for binding activity. The microarray preserved the integrin α5β1-fibronectin interaction, and was suppressed by the synthetic RGD peptide. We identified ten extracts with high integrin affinity using a high-throughput, competitive inhibition assay. We also demonstrate the biological function of these extracts in HUVECs.
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Bang Ji-Young
Kim Eung-Yoon
Seong Nak-Sul
Shin Yoo-Soo
Kang In-Cheol
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Abstract
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Integrins consist of transmembrane glycoproteins noncovalently associated to form αβ heterodimers. Various α/β associations determine binding specieficities for cell surface molecules of the immunoglobulin superfamily as well as for extracellular matrix components. Through their cytoplasmic domains, integrins are responsible for the transmission of signals between the intracellular and the extracellular environment. We immobilized an integrin α5β1 microarray on a ProteoChip to screen Korean medicinal plant extracts for binding activity. The microarray preserved the integrin α5β1-fibronectin interaction, and was suppressed by the synthetic RGD peptide. We identified ten extracts with high integrin affinity using a high-throughput, competitive inhibition assay. We also demonstrate the biological function of these extracts in HUVECs.
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KEYWORD
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Library Screening, ProteoChip, Integrin, Angiogenesis, Medicinal plants
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