title: ProteoChip-based library screening of integrin alpha5beta1 antagonists from Korean medicinal plant extracts.
abstract: Integrins consist of transmembrane glycoproteins noncovalently associated to form alphabeta heterodimers. Various alpha/beta 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 alpha5beta1 microarray on a ProteoChip to screen Korean medicinal plant extracts for binding activity. The microarray preserved the integrin alpha5beta1-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.
authors.affiliation: BioChip Research Center, Hoseo University, Asan 336-795, Korea.
authors.forename: J I Young
authors.initials: JI
authors.lastname: Bang
authors.forename: Eung-Yoon
authors.initials: EY
authors.lastname: Kim
authors.forename: Nak Sul
authors.initials: NS
authors.lastname: Seong
authors.forename: Yoo Soo
authors.initials: YS
authors.lastname: Shin
authors.forename: In-Cheol
authors.initials: IC
authors.lastname: Kang
mesh_terms: D002448:Cell Adhesion / Q000187:drug effects; D002465:Cell Movement / Q000187:drug effects; D049109:Cell Proliferation / Q000187:drug effects; D002478:Cells, Cultured; D042783:Endothelial Cells / Q000166:cytology / Q000187:drug effects; D006801:Humans; D039081:Integrin alpha5beta1 / Q000037:antagonists & inhibitors*; D007723:Korea; D010936:Plant Extracts / Q000494:pharmacology*; D010946:Plants, Medicinal; D040081:Protein Array Analysis / Q000379:methods*
chemical_list: D039081:Integrin alpha5beta1; D010936:Plant Extracts