Surfactant protein a in cystic fibrosis: supratrimeric structure and pulmonary outcome.

<h4>Background</h4>The state of oligomerization of surfactant associated protein-A (SP-A) monomers differs between individuals. This likely affects SP-A's functional properties and could thereby influence clinical status in patients with lung diseases. In this study we focus on SP-A...

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Autores principales:	Matthias Griese, Stephanie Heinrich, Felix Ratjen, Michael Kabesch, Karl Paul, Manfred Ballmann, Ernst Rietschel, Matthias Kappler
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/6c19f95277bf4bc9809a832beca101af
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spelling	oai:doaj.org-article:6c19f95277bf4bc9809a832beca101af2021-11-18T08:06:00ZSurfactant protein a in cystic fibrosis: supratrimeric structure and pulmonary outcome.1932-620310.1371/journal.pone.0051050https://doaj.org/article/6c19f95277bf4bc9809a832beca101af2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23236429/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>The state of oligomerization of surfactant associated protein-A (SP-A) monomers differs between individuals. This likely affects SP-A's functional properties and could thereby influence clinical status in patients with lung diseases. In this study we focus on SP-A structure in cystic fibrosis (CF) compared to both healthy subjects and disease controls.<h4>Methods</h4>SP-A composition and function were assessed in both bronchoalveolar lavage (BAL) fluid and serum of 46 CF patients with mild disease, 25 patients with chronic bronchitis and 22 healthy subjects by gel chromatography and a functional agglutination assay. Relation of SP-A agglutination ability to disease severity of the subjects was explored.<h4>Results</h4>SP-A was present in seven major oligomeric forms with the majority of SP-A being structurally organized as complex oligomeric forms. More complex oligomeric forms were associated with better SP-A function with regard to its agglutination ability. These forms were more frequently observed in BAL than in serum, but there were no differences between disease groups. In CF patients, more complex forms of SP-A were associated with better lung function.<h4>Conclusions</h4>Organizational structure of SP-A affects its functional activity and is linked to disease severity in CF.Matthias GrieseStephanie HeinrichFelix RatjenMichael KabeschKarl PaulManfred BallmannErnst RietschelMatthias KapplerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 12, p e51050 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Matthias Griese Stephanie Heinrich Felix Ratjen Michael Kabesch Karl Paul Manfred Ballmann Ernst Rietschel Matthias Kappler Surfactant protein a in cystic fibrosis: supratrimeric structure and pulmonary outcome.
description	<h4>Background</h4>The state of oligomerization of surfactant associated protein-A (SP-A) monomers differs between individuals. This likely affects SP-A's functional properties and could thereby influence clinical status in patients with lung diseases. In this study we focus on SP-A structure in cystic fibrosis (CF) compared to both healthy subjects and disease controls.<h4>Methods</h4>SP-A composition and function were assessed in both bronchoalveolar lavage (BAL) fluid and serum of 46 CF patients with mild disease, 25 patients with chronic bronchitis and 22 healthy subjects by gel chromatography and a functional agglutination assay. Relation of SP-A agglutination ability to disease severity of the subjects was explored.<h4>Results</h4>SP-A was present in seven major oligomeric forms with the majority of SP-A being structurally organized as complex oligomeric forms. More complex oligomeric forms were associated with better SP-A function with regard to its agglutination ability. These forms were more frequently observed in BAL than in serum, but there were no differences between disease groups. In CF patients, more complex forms of SP-A were associated with better lung function.<h4>Conclusions</h4>Organizational structure of SP-A affects its functional activity and is linked to disease severity in CF.
format	article
author	Matthias Griese Stephanie Heinrich Felix Ratjen Michael Kabesch Karl Paul Manfred Ballmann Ernst Rietschel Matthias Kappler
author_facet	Matthias Griese Stephanie Heinrich Felix Ratjen Michael Kabesch Karl Paul Manfred Ballmann Ernst Rietschel Matthias Kappler
author_sort	Matthias Griese
title	Surfactant protein a in cystic fibrosis: supratrimeric structure and pulmonary outcome.
title_short	Surfactant protein a in cystic fibrosis: supratrimeric structure and pulmonary outcome.
title_full	Surfactant protein a in cystic fibrosis: supratrimeric structure and pulmonary outcome.
title_fullStr	Surfactant protein a in cystic fibrosis: supratrimeric structure and pulmonary outcome.
title_full_unstemmed	Surfactant protein a in cystic fibrosis: supratrimeric structure and pulmonary outcome.
title_sort	surfactant protein a in cystic fibrosis: supratrimeric structure and pulmonary outcome.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/6c19f95277bf4bc9809a832beca101af
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Surfactant protein a in cystic fibrosis: supratrimeric structure and pulmonary outcome.

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