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Titolo:
Purification and refolding of vascular endothelial growth factor-B
Autore:
Scrofani, SDB; Fabri, LJ; Xu, P; Maccarone, P; Nash, AD;
Indirizzi:
AMRAD Operat Pty Ltd, Richmond, Vic 3121, Australia AMRAD Operat Pty Ltd Richmond Vic Australia 3121 ond, Vic 3121, Australia
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 10, volume: 9, anno: 2000,
pagine: 2018 - 2025
SICI:
0961-8368(200010)9:10<2018:PAROVE>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECEPTOR TYROSINE KINASES; ESCHERICHIA-COLI; VEGF-C; EXPRESSION; CELLS; BINDING; FLT-1; ANGIOGENESIS; NEUROPILIN-1; FLK-1/KDR;
Keywords:
angiogenesis; inclusion bodies; purification; VEGF-B;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Nash, AD AMRAD Operat Pty Ltd, 576 Swan St, Richmond, Vic 3121, Australia AMRAD Operat Pty Ltd 576 Swan St Richmond Vic Australia 3121 alia
Citazione:
S.D.B. Scrofani et al., "Purification and refolding of vascular endothelial growth factor-B", PROTEIN SCI, 9(10), 2000, pp. 2018-2025

Abstract

Vascular endothelial growth factor (VEGF)-A interacts with the receptor tyrosine kinases VEGF-R1 and R2, and the importance of this interaction in endothelial cell (EC) function and blood vessel development has been well documented. Other ligands that interact differentially with these receptors and that are structurally related to VEGF-A include VEGF-B, VEGF-C, VEGF-D, and placenta growth factor (PLGF). Compared with VEGF-A, relatively little is known about the biological role of the VEGF-R1 specific ligand, VEGF-B. Two splice variant isoforms that differ at the COOH-terminus and which retain unique solubility characteristics are widely expressed throughout embryonic and postnatal development. Recent analysis of mice with a targeted deletion of the VEGF-B gene has revealed a defect in heart development and function consistent with an important role in vascularization of the myocardium (Bellomo D et al., 2000, Circ Res 86:E29-E35). To facilitate further characterization of VEGF-B, we have developed a protocol for expression and purification of refolded recombinant protein from Escherichia coli inclusion bodies (IBs). The approach developed resolves a number of significant issues associated with VEGF-B, including the ability to heterodimerize with endogenous VEGF-A when co-expressed in mammalian cells, a complex secondary structure incorporating inter- and intrachain disulfide bonds and hydrophobic characteristics that preclude the use of standard chromatographic resins. The resulting purified disulfide-linked homodimer was demonstrated to bind to VEGF-R1 and to compete with VEGF-A for binding to this receptor.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 10:56:09