title: Genetically engineered epidermal growth factor conjugate crosses cell membrane.
abstract: Epidermal growth factor (EGF) is a well-known pleiotropic growth factor in mammal, and has been attempted to be used in many different fields. However, the application of EGF is limited because of its poor cell permeation. In order to increase membrane permeation ability of EGF, a genetically modified recombinant EGF (GST-TAT-EGF) was prepared through conjugation of EGF with two protein transduction domains, glutathione-S-transferase and TAT47-57. The results showed that the GST-TAT-EGF fusion protein exhibited higher ability in biomembrane penetration than that of the EGF alone. The results also implied that two different mechanisms (EGF receptor-mediated endocytosis and direct penetration) might be involved in GST-TAT-EGF transmembrane delivery.
authors.affiliation: Institute of Pharmacology and Toxicology, Academy of Military Medical Sciences, Beijing, 100850, China.
authors.forename: Baoquan
authors.initials: B
authors.lastname: Zhao
authors.forename: Yanru
authors.initials: Y
authors.lastname: Guo
authors.forename: Ailing
authors.initials: A
authors.lastname: Fu
mesh_terms: D000818:Animals; D041702:BALB 3T3 Cells; D002453:Cell Cycle; D002462:Cell Membrane / Q000378:metabolism*; D002463:Cell Membrane Permeability; D049109:Cell Proliferation; D004705:Endocytosis; D004815:Epidermal Growth Factor / Q000378:metabolism*; D066246:ErbB Receptors / Q000378:metabolism; D005818:Genetic Engineering / Q000379:methods*; D005822:Genetic Vectors / Q000378:metabolism; D005982:Glutathione Transferase / Q000378:metabolism; D018859:Hair Follicle / Q000378:metabolism; D051379:Mice; D010957:Plasmids / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012867:Skin / Q000378:metabolism; D012995:Solubility; D013552:Swine
chemical_list: D011993:Recombinant Fusion Proteins; D004815:Epidermal Growth Factor; D005982:Glutathione Transferase; D066246:ErbB Receptors