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Titolo:
LUNG-FUNCTION IN PREMATURE RABBITS TREATED WITH RECOMBINANT HUMAN SURFACTANT PROTEIN-C
Autore:
HAWGOOD S; OGAWA A; YUKITAKE K; SCHLUETER M; BROWN C; WHITE T; BUCKLEY D; LESIKAR D; BENSON B;
Indirizzi:
UNIV CALIF SAN FRANCISCO,CARDIOVASC RES INST,BOX 0128 SAN FRANCISCO CA 94143 UNIV CALIF SAN FRANCISCO,DEPT PEDIAT SAN FRANCISCO CA 94143 SCIOS NOVA INC MT VIEW CA 94043
Titolo Testata:
American journal of respiratory and critical care medicine
fascicolo: 2, volume: 154, anno: 1996,
pagine: 484 - 490
SICI:
1073-449X(1996)154:2<484:LIPRTW>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
RESPIRATORY-DISTRESS SYNDROME; BOVINE PULMONARY SURFACTANT; AMINO-ACID SEQUENCES; SP-B; SYNTHETIC SURFACTANT; HYDROPHOBIC PROTEINS; BIOPHYSICAL ACTIVITY; DELIVERED RABBITS; PRETERM RABBITS; PHOSPHOLIPIDS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
S. Hawgood et al., "LUNG-FUNCTION IN PREMATURE RABBITS TREATED WITH RECOMBINANT HUMAN SURFACTANT PROTEIN-C", American journal of respiratory and critical care medicine, 154(2), 1996, pp. 484-490

Abstract

We report the activity of recombinant human surfactant apoprotein-C (rSP-C[Cys](2)) and various phospholipids in a preterm rabbit model of respiratory distress syndrome (RDS). Mixtures of rSP-C(Cys)(2) and certain phospholipids had similar activity (lung compliance and lung pressure-volume behavior) to rabbit surfactant in this model. The activityof rSP-C(Cys)(2) was maximal at 1 mol% protein and varied significantly with the phospholipid composition. Chemically synthesized SP-C had similar activity to rSP-C(Cys)(2). Deletion of six amino-terminal residues did not affect function. Substitution of cysteines and cysteines with adjacent serines (rSP-C[Ser](2)) by site-specific mutagenesis minimized aggregation of rSP-C but did not affect activity. Palmitoylation of cysteines and cysteines in rSP-C (rSP-C[C16](2)) did not enhance the activity of rSP-C(Cys)(2). We conclude that bacterial expression is a practical source of functional SP-C, and that nonacylated forms ofSP-C may be useful adjuvants to phospholipids in the treatment of RDSand possibly other forms of acute lung injury.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 10:47:23