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Titolo:
Covalently conjugated VEGF-fibrin matrices for endothelialization
Autore:
Zisch, AH; Schenk, U; Schense, JC; Sakiyama-Elbert, SE; Hubbell, JA;
Indirizzi:
ETH Zurich, Dept Mat, CH-8044 Zurich, Switzerland ETH Zurich Zurich Switzerland CH-8044 t Mat, CH-8044 Zurich, Switzerland ETH Zurich, Inst Biomed Engn, CH-8044 Zurich, Switzerland ETH Zurich Zurich Switzerland CH-8044 Engn, CH-8044 Zurich, Switzerland Univ Zurich, CH-8044 Zurich, Switzerland Univ Zurich Zurich Switzerland CH-8044 rich, CH-8044 Zurich, Switzerland
Titolo Testata:
JOURNAL OF CONTROLLED RELEASE
fascicolo: 1-3, volume: 72, anno: 2001,
pagine: 101 - 113
SICI:
0168-3659(20010514)72:1-3<101:CCVMFE>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
FIBROBLAST GROWTH-FACTOR; EXPANDED POLYTETRAFLUOROETHYLENE GRAFTS; INTRAMUSCULAR GENE-TRANSFER; ENHANCES NEURITE EXTENSION; SMOOTH-MUSCLE; MYOCARDIAL ANGIOGENESIS; ISCHEMIC MYOCARDIUM; CELL-PROLIFERATION; VESSEL DEVELOPMENT; GLUE SUSPENSIONS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Zisch, AH ETH Zurich, Dept Mat, Moussonstr 18, CH-8044 Zurich, SwitzerlandETH Zurich Moussonstr 18 Zurich Switzerland CH-8044 Switzerland
Citazione:
A.H. Zisch et al., "Covalently conjugated VEGF-fibrin matrices for endothelialization", J CONTR REL, 72(1-3), 2001, pp. 101-113

Abstract

Vascular endothelial growth factor (VEGF) is a key factor in endothelial cell biology and blood vessel formation and a candidate therapeutic for the stimulation of angiogenesis-dependent tissue regeneration. The objective ofthis study was to confer the angiogenic activity of VEGF(121) upon the biomaterial fibrin, a natural substrate for endothelial cell growth and clinically accepted as 'fibrin glue'. To achieve this, we engineered fibrin-basedhydrogels that were covalently modified with VEGF(121). Our laboratory hasrecently developed novel methodology that allows the covalent incorporation of exogenous bioactive peptides by the transglutominase activity of factor XIIIa into fibrin during cogulation. Here, this ability of factor XIIIa to crosslink additional proteins within fibrin was employed to covalently incorporate VEGF(121). By recombinant DNA methodology, a mutant VEGF(121) variant, alpha (2)-PI1-8-VEGF(121), which contains an additional factor XIIIa substrate sequence NQEQVSPL at the aminoterminus, was expressed in E. coli. In soluble form, the mutant protein fully retained its mitogenic activity for endothelial cells. Using I-125-labeled alpha (2)-PI1-8-VEGF(121), its covalent incorporation and the efficiency of incorporation into fibrin was demonstrated and characterized. The immobilized, fibrin-conjugated VEGF(121)protein remained an active and very efficient mitogen for human endothelial cells grown on two-dimensional VEGF(121)-modified fibrin surfaces, and the incorporation of increasing amounts of alpha (2)-PI1-8-VEGF(121) resultedin dose-dependent enhancement of endothelial cell growth. The VEGF-modified fibrin matrices can be formed as injectable gels in a single-step reaction under physiological conditions in vivo. When used as a ingrowth matrix, such VEGF incorporating materials could be useful in a variety of clinical situations that require an angiogenic response into an ischemic region or inplant. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 04:02:52