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1 The Children's Hospital of Philadelphia, Philadelphia, PA, USA
2 Institute of Pharmacological and Biological Sciences, University of Parma, Parma, Italy
3 The Institute for Environmental Medicine, University of Pennsylvania School of Medicine, Philadelphia, PA, USA
4 Pfizer, Inc., Groton, CT, USA
5 University of Pennsylvania Medical Center, Philadelphia, PA, USA
* To whom correspondence should be addressed. E-mail: batekenn{at}mail.med.upenn.edu.
ATP-binding cassette transporter A1 (ABCA1) promotes transfer of cholesterol and phospholipid from cells to lipid-free serum apolipoproteins. ABCA1 mRNA and protein expression in primary cultures of rodent type II cells was sensitive to up-regulation with 9-cis-retinoic-acid (9cRA, 5 µM) and 22-hydroxycholesterol (22-OH, 6.2 µM). The increase in ABCA1 protein levels was time-dependent and was maximal after 16 h of exposure to 9cRA/22-OH. Inducible ABCA1 was also found in transformed cell lines of lung origin, WI38/VA13, A549, and NIH-H441 cells. Stimulation of ABCA1 in rat type II cells by 9cRA/22-OH resulted in a 4- or 5-fold enhancement of efflux of radioactive phospholipid or cholesterol, respectively, from the pneumocytes to apolipoprotein AI (apo AI), while cAMP (0.3 mM) had no effect. ABCA1-mediated lipid efflux to apo AI was independent of the surfactant secretion pathway as up-regulation of ABCA1 resulted in a reduction of secretagogue-stimulated surfactant phospholipid release. These studies demonstrate the presence of functional ABCA1 in type II cells from lung.
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