title: The cell adhesion and proliferation activities of a peptide derived from human tenascin-C are dependent on two Ile residues.
abstract: A tenascin-C derived peptide (TNIIIA2 peptide, 1) stimulated β1 integrin-mediated cell adhesion via binding to syndecan-4. Ala-substituted peptides were synthesized to understand the structure-activity relationship. Peptides in which basic amino acids were substituted showed reduced cell adhesion activity, but their proliferation activities were similar to or higher than those mediated by peptide 1. In contrast, peptides in which the Ile residues of peptide 1 were replaced were inactive, indicating that the Ile residues are critical for the peptide's activity. CD analysis suggested that the Ile residues are necessary for the formation of a specific conformation required for binding to syndecan-4.
authors: Department of Chemistry, Graduate School of Science and Engineering, Saga University, 1 Honjo-machi, Saga 840-8502, Japan.
authors: Ryo
authors: R
authors: Hayashi
authors: Shogo
authors: S
authors: Miura
authors: Yohei
authors: Y
authors: Saito
authors: Satoshi
authors: S
authors: Osada
authors: Takuya
authors: T
authors: Iyoda
authors: Fumio
authors: F
authors: Fukai
authors: Hiroaki
authors: H
authors: Kodama
mesh_terms: D002448:Cell Adhesion / Q000187:drug effects; D049109:Cell Proliferation / Q000187:drug effects; D006801:Humans; D007532:Isoleucine / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry / Q000494:pharmacology*; D013329:Structure-Activity Relationship; D019063:Tenascin / Q000737:chemistry*
chemical_list: D010455:Peptides; D019063:Tenascin; D007532:Isoleucine