NDLI: Lipid Specificity of Surfactant Protein B Studied by Time-of-Flight Secondary Ion Mass Spectrometry

Content Provider	PubMed Central
Author	Breitenstein, D. Batenburg, J. J. Hagenhoff, B. Galla, H. J.
Copyright Year	2006
Abstract	One of the key functions of mammalian pulmonary surfactant is the reduction of surface tension to minimal values. To fulfill this function it is expected to become enriched in dipalmitoylphosphatidylcholine either on its way from the alveolar type II pneumocytes to the air/water interface of the lung or within the surface film during compression and expansion of the alveoli during the breathing cycle. One protein that may play a major role in this enrichment process is the surfactant protein B. The aim of this study was to identify the lipidic interaction partner of this protein. Time-of-flight secondary ion mass spectrometry was used to analyze the lateral distribution of the components in two SP-B-containing model systems. Either native or partly isotopically labeled lipids were analyzed. The results of both setups give strong indications that, at least under the specific conditions of the chosen model systems (e.g., concerning pH and lipid composition), the lipid interacting with surfactant protein B is not phosphatidylglycerol as generally accepted, but dipalmitoylphosphatidylcholine instead.
Related Links	http://dx.doi.org/10.1529/biophysj.105.073247
Ending Page	1356
Page Count	10
Starting Page	1347
File Format	PDF
ISSN	00063495
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	4
Volume Number	91
Language	English
Publisher	Biophysical Society
Publisher Date	2006-08-01
Access Restriction	Open
Rights Holder	Biophysical Society
Subject Keyword	Biophysics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

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