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Titolo:
Domains of surfactant protein A that affect protein oligomerization, lipidstructure and surface tension
Autore:
Palaniyar, N; Ikegami, M; Korfhagen, T; Whitsett, J; McCormack, FX;
Indirizzi:
Univ Oxford, Dept Biochem, MRC, Immunochem Unit, Oxford OX1 3QU, England Univ Oxford Oxford England OX1 3QU unochem Unit, Oxford OX1 3QU, England Univ Cincinnati, Dept Internal Med, Div Pulm Crit Care Med, Cincinnati, OH45267 USA Univ Cincinnati Cincinnati OH USA 45267 Care Med, Cincinnati, OH45267 USA Childrens Hosp, Med Ctr, Div Pulm Biol, Cincinnati, OH 43229 USA ChildrensHosp Cincinnati OH USA 43229 ulm Biol, Cincinnati, OH 43229 USA
Titolo Testata:
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-MOLECULAR AND INTEGRATIVE PHYSIOLOGY
fascicolo: 1, volume: 129, anno: 2001,
pagine: 109 - 127
SICI:
1095-6433(200105)129:1<109:DOSPAT>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
MANNOSE-BINDING PROTEIN; CARBOHYDRATE-RECOGNITION DOMAIN; PULMONARY ALVEOLAR PROTEINOSIS; SITE-DIRECTED MUTAGENESIS; RAT LUNG SURFACTANT; HELICAL COILED-COIL; GENE TARGETED MICE; A-DEFICIENT MICE; TUBULAR MYELIN; II CELLS;
Keywords:
collectins; innate immunity; myelin figure; SP-A; SP-D; surfactant inhibition; surface activity; tubular myelin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
112
Recensione:
Indirizzi per estratti:
Indirizzo: Palaniyar, N Univ Oxford, Dept Biochem, MRC, Immunochem Unit, S Parks Rd, Oxford OX1 3QU, England Univ Oxford S Parks Rd Oxford England OX1 3QU 1 3QU, England
Citazione:
N. Palaniyar et al., "Domains of surfactant protein A that affect protein oligomerization, lipidstructure and surface tension", COMP BIOC A, 129(1), 2001, pp. 109-127

Abstract

Surfactant protein A (SP-A) is an abundant protein found in pulmonary surfactant which has been reported to have multiple functions. In this review, we focus on the structural importance of each domain of SP-A in the functions of protein oligomerization, the structural organization of lipids and the surface-active properties of surfactant, with an emphasis on ultrastructural analyses. The N-terminal domain of SP-A is required for disulfide-dependent protein oligomerization, and for binding and aggregation of phospholipids, but there is no evidence that this domain directly interacts with lipid membranes. The collagen-like domain is important for the stability and oligomerization of SP-A. It also contributes shape and dimension to the molecule, and appears to determine membrane spacing in lipid aggregates such as common myelin and tubular myelin. The neck domain of SP-A is primarily involved in protein trimerization, which is critical for many protein functions, but it does not appear to be directly involved in lipid interactions. Theglobular C-terminal domain of SP-A clearly plays a central role in lipid binding, and in more complex functions such as the formation and/or stabilization of curved membranes. In recent work, we have determined that the maintenance of low surface tension of surfactant in the presence of serum protein inhibitors requires cooperative interactions between the C-terminal and N-terminal domains of the molecule. This effect of SP-A requires a high degree of oligomeric assembly of the protein, and may be mediated by the activity of the protein to alter the form or physical state of surfactant lipid aggregates. (C) 2001 Elsevier Science Inc. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/12/17 alle ore 23:34:52