Engineering of Artificial Cell Adhesion Proteins by Grafting the Arg-Gly-Asp Cell Adhesive Signal to a Calpastatin Segment
Autor: | Toshinaga Maeda, Fusao Kimizuka, Kiyotoshi Sekiguchi, Ikunoshin Kato, Kimikazu Hashino, Koiti Titani, Tomoko Shimojo |
---|---|
Rok vydání: | 1992 |
Předmět: |
Recombinant Fusion Proteins
Molecular Sequence Data Cell Integrin Cell Communication Receptors Cytoadhesin Biochemistry Receptors Fibronectin Cell Adhesion medicine Receptors Vitronectin Amino Acid Sequence Molecular Biology Calpastatin chemistry.chemical_classification Base Sequence biology Calpain Cell adhesion molecule Calcium-Binding Proteins General Medicine Cell biology Fibronectin medicine.anatomical_structure chemistry Mutagenesis Site-Directed biology.protein Vitronectin Glycoprotein Cell Adhesion Molecules Oligopeptides Signal Transduction |
Zdroj: | The Journal of Biochemistry. 112:547-551 |
ISSN: | 1756-2651 0021-924X |
DOI: | 10.1093/oxfordjournals.jbchem.a123936 |
Popis: | A new artificial cell adhesive protein was engineered by grafting the Arg-Gly-Asp (RGD) sequence, the minimal recognition signal of fibronectin for interaction with integrins, to a calpastatin segment by in vitro mutagenesis. The mutagenized protein showed cell adhesive activity in addition to calpain inhibitory activity. The RGD signal grafted to the calpastatin segment was recognized by the vitronectin receptor but not by the fibronectin receptor. |
Databáze: | OpenAIRE |
Externí odkaz: |