The University of Southampton
University of Southampton Institutional Repository

Lipidomic analysis of cellular and secreted phospholipids from human fetal type II alveolar epithelial cells: effects of differentiation

Lipidomic analysis of cellular and secreted phospholipids from human fetal type II alveolar epithelial cells: effects of differentiation
Lipidomic analysis of cellular and secreted phospholipids from human fetal type II alveolar epithelial cells: effects of differentiation
Maturation of fetal alveolar type II epithelial cells in utero is characterized by specific changes to lung surfactant phospholipids. Here we quantified the effects of hormonal differentiation in vitro on the molecular specificity of cellular and secreted phospholipids from human fetal type II epithelial cells, using electrospray ionization mass spectrometry. Differentiation, assessed by morphology and changes in gene expression, was accompanied by restricted and specific modifications to cell phospholipids, principally enrichments of shorter chain species of phosphatidylcholine (PC) and phosphatidylinositol (PI) that were not observe in fetal lung fibroblasts. Treatment of differentiated epithelial cells with secretagogues stimulated secretion of functional surfactant containing surfactant proteins B and C. Secreted material was further enriched in this same set of phospholipid species, but was characterized by increased contents of short chain monounsaturated and disaturated species other than dipalmitoyl PC (PC16:0/16:0), principally palmitoylmyristoyl PC (PC16:0/14:0) and palmitoylpalmitoleoyl PC (PC16:0/16:1). Mixtures of these PC molecular species, phosphatidylglycerol and SP-B/C were functionally active and rapidly generated low surface tension on compression in a pulsating bubble surfactometer. These results suggest that hormonally differentiated human fetal Type II cells do not select the molecular composition of surfactant phospholipid on the basis of saturation but, more probably, on acyl chain length.
phosphatidylcholine, phosphatidylinositol, electrospray ionization mass spectrometry, differentiation
0022-2275
1322-1331
Postle, A.D.
0fa17988-b4a0-4cdc-819a-9ae15c5dad66
Gonzales, L.W.
5f6aa687-1c60-4e48-aaf4-cc00544618fc
Bernhard, W.
8d110ea4-e769-4369-9316-1845ba2af485
Clark, G.T.
7a3aed07-f59f-4a97-92ad-1658c89c8a57
Godinez, M.H.
e4d91477-28ea-45eb-be41-0a4a146a9115
Godinez, R.I.
8e76b760-1b06-466f-b102-97f5e3aa3c77
Ballard, P.L.
2e431737-2c0c-415d-aab1-4965d3a2c471
Postle, A.D.
0fa17988-b4a0-4cdc-819a-9ae15c5dad66
Gonzales, L.W.
5f6aa687-1c60-4e48-aaf4-cc00544618fc
Bernhard, W.
8d110ea4-e769-4369-9316-1845ba2af485
Clark, G.T.
7a3aed07-f59f-4a97-92ad-1658c89c8a57
Godinez, M.H.
e4d91477-28ea-45eb-be41-0a4a146a9115
Godinez, R.I.
8e76b760-1b06-466f-b102-97f5e3aa3c77
Ballard, P.L.
2e431737-2c0c-415d-aab1-4965d3a2c471

Postle, A.D., Gonzales, L.W., Bernhard, W., Clark, G.T., Godinez, M.H., Godinez, R.I. and Ballard, P.L. (2006) Lipidomic analysis of cellular and secreted phospholipids from human fetal type II alveolar epithelial cells: effects of differentiation. Journal of Lipid Research, 47 (6), 1322-1331. (doi:10.1194/jlr.M600054-JLR200).

Record type: Article

Abstract

Maturation of fetal alveolar type II epithelial cells in utero is characterized by specific changes to lung surfactant phospholipids. Here we quantified the effects of hormonal differentiation in vitro on the molecular specificity of cellular and secreted phospholipids from human fetal type II epithelial cells, using electrospray ionization mass spectrometry. Differentiation, assessed by morphology and changes in gene expression, was accompanied by restricted and specific modifications to cell phospholipids, principally enrichments of shorter chain species of phosphatidylcholine (PC) and phosphatidylinositol (PI) that were not observe in fetal lung fibroblasts. Treatment of differentiated epithelial cells with secretagogues stimulated secretion of functional surfactant containing surfactant proteins B and C. Secreted material was further enriched in this same set of phospholipid species, but was characterized by increased contents of short chain monounsaturated and disaturated species other than dipalmitoyl PC (PC16:0/16:0), principally palmitoylmyristoyl PC (PC16:0/14:0) and palmitoylpalmitoleoyl PC (PC16:0/16:1). Mixtures of these PC molecular species, phosphatidylglycerol and SP-B/C were functionally active and rapidly generated low surface tension on compression in a pulsating bubble surfactometer. These results suggest that hormonally differentiated human fetal Type II cells do not select the molecular composition of surfactant phospholipid on the basis of saturation but, more probably, on acyl chain length.

This record has no associated files available for download.

More information

Published date: 1 June 2006
Additional Information: Abbreviations: DCI, dexamethasone + 8-bromo-cAMP + isobutylmethylxanthine; ESI-MS, electrospray ionization mass spectrometry; PA, phosphatidic acid; PC, phosphatidylcholine; PE, phosphatidylethanolamine; PG, phosphatidylglycerol; PI, phosphatidylinositol; PS, phosphatidylserine; SP-A, -B or -C, surfactant proteins A, B or C
Keywords: phosphatidylcholine, phosphatidylinositol, electrospray ionization mass spectrometry, differentiation

Identifiers

Local EPrints ID: 59391
URI: http://eprints.soton.ac.uk/id/eprint/59391
ISSN: 0022-2275
PURE UUID: 90a618d9-30c0-4ac7-9d62-73a9c98f59d7
ORCID for A.D. Postle: ORCID iD orcid.org/0000-0001-7361-0756

Catalogue record

Date deposited: 03 Sep 2008
Last modified: 16 Mar 2024 02:32

Export record

Altmetrics

Contributors

Author: A.D. Postle ORCID iD
Author: L.W. Gonzales
Author: W. Bernhard
Author: G.T. Clark
Author: M.H. Godinez
Author: R.I. Godinez
Author: P.L. Ballard

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×