title: Screening of integrin-binding peptides from the laminin α4 and α5 chain G domain peptide library.
abstract: Laminins, a multifunctional protein family of extracellular matrix, interact with various types of integrin. Here, integrin-mediated cell adhesive peptides have been systematically screened in the laminin α4 and α5 chain G domain peptide library consisting of 211 peptides by both the peptide-coated plastic plates and peptide-conjugated Sepharose bead assays using human dermal fibroblasts. Thirteen peptides promoted cell spreading and the activity was specifically inhibited by EDTA. Cell attachment to 11 peptides was inhibited by anti-integrin β1 antibody. Additionally, cell attachment to the A5G81 (AGQWHRVSVRWG) and A5G84 (TWSQKALHHRVP) peptides was specifically inhibited by anti-integrin α3 and α6 antibodies. These results suggest that the A5G81 and A5G84 peptides promote integrin α3β1- and α6β1-mediated cell attachment. Further, most of the integrin-mediated cell adhesive peptides are located in the loop regions in the G domains, suggesting that structure is important for the integrin specific recognition. Integrin binding peptides are useful for understanding laminin functions and have a potential to use for biomaterials and drug development.
authors.affiliation: Laboratory of Clinical Biochemistry, School of Pharmacy, Tokyo University of Pharmacy and Life Sciences, 1432-1 Horinouchi, Hachioji, Tokyo 192-0392, Japan.
authors.forename: Fumihiko
authors.initials: F
authors.lastname: Katagiri
authors.forename: Masaya
authors.initials: M
authors.lastname: Ishikawa
authors.forename: Yuji
authors.initials: Y
authors.lastname: Yamada
authors.forename: Kentaro
authors.initials: K
authors.lastname: Hozumi
authors.forename: Yamato
authors.initials: Y
authors.lastname: Kikkawa
authors.forename: Motoyoshi
authors.initials: M
authors.lastname: Nomizu
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002448:Cell Adhesion; D002478:Cells, Cultured; D005347:Fibroblasts / Q000378:metabolism; D051417:Focal Adhesion Kinase 1 / Q000378:metabolism; D006801:Humans; D039422:Integrin alpha3 / Q000378:metabolism; D039503:Integrin alpha6 / Q000378:metabolism; D019012:Integrin beta1 / Q000378:metabolism; D016023:Integrins / Q000378:metabolism*; D007797:Laminin / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D019151:Peptide Library; D017434:Protein Structure, Tertiary; D016596:Vinculin / Q000378:metabolism
chemical_list: D002352:Carrier Proteins; D039422:Integrin alpha3; D039503:Integrin alpha6; D019012:Integrin beta1; D016023:Integrins; C501370:Lama4 protein, mouse; D007797:Laminin; D010446:Peptide Fragments; D019151:Peptide Library; C488955:VCL protein, human; C097043:laminin alpha5; D016596:Vinculin; D051417:Focal Adhesion Kinase 1; C496050:PTK2 protein, human