Article: The presence and activity of SP-D in porcine coronary endothelial cells depend on Akt/PI3K, Erk and nitric oxide and decrease after multiple passaging
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- Publisher Website: 10.1016/j.molimm.2008.09.027
- Scopus: eid_2-s2.0-61449196879
- PMID: 19010548
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| Title | The presence and activity of SP-D in porcine coronary endothelial cells depend on Akt/PI3K, Erk and nitric oxide and decrease after multiple passaging |
|---|---|
| Authors | Lee, MYK1 Sørensen, GL2 Holmskov, U2 Vanhoutte, PM1 |
| Keywords | Endothelial cells Nitric oxide SP-D TNF-α |
| Issue Date | 2009 |
| Publisher | Pergamon. The Journal's web site is located at http://www.elsevier.com/locate/molimm |
| Citation | Molecular Immunology, 2009, v. 46 n. 6, p. 1050-1057 [How to Cite?] DOI: http://dx.doi.org/10.1016/j.molimm.2008.09.027 |
| Abstract | Surfactant protein D (SP-D) mediates clearance of microorganisms and modulates inflammation in response to cytotoxic stimulation. It is present in various epithelia, but also in vascular smooth muscle and endothelial cells. Experiments were designed to determine whether or not SP-D is present in porcine coronary arterial endothelial cells and if so, to investigate the molecular mechanisms underlying this presence. The expression of SP-D, NO synthase, Akt 1/2 and Erk 1/2 proteins was determined in cultures at passages 1 (#1) and 4 (#4). SP-D in primary cells existed in three isoforms (37-38 kDa and 50 kDa). The 37-38 kDa SP-D forms were the dominant isoforms in the porcine endothelium and were prominent at #1 but partially lost at #4. Tumor necrosis factor-α (TNF-α) significantly augmented the level of SP-D expression at #1 but not at #4. The basal level of 37-38 kDa SP-D isoforms at #1 was reduced by L-NAME, wortmannin and PD 98059. The low basal expression at #4 could be increased by DETA NONOate (donor of NO) or insulin (activator of PI3K/Akt). The presence of nitric oxide synthase was reduced while that of Akt 1/2 and Erk 1/2 was increased at #4. In cells both at passages 1 and 4, TNF-α downregulated NO synthase and up-regulated p-Erk 1/2 protein. The present findings demonstrate the presence of SP-D in endothelial cells which is NO-, PI3K/Akt- and Erk-dependent. They suggest a protective role of SP-D in these cells. © 2008 Elsevier Ltd. All rights reserved. |
| ISSN | 0161-5890 2011 Impact Factor: 2.897 2011 SCImago Journal Rankings: 0.401 |
| DOI | http://dx.doi.org/10.1016/j.molimm.2008.09.027 |
| References | References in Scopus |
| dc.contributor.author | Lee, MYK | ||||||
|---|---|---|---|---|---|---|---|
| dc.contributor.author | Sørensen, GL | ||||||
| dc.contributor.author | Holmskov, U | ||||||
| dc.contributor.author | Vanhoutte, PM | ||||||
| dc.date.accessioned | 2010-05-31T03:52:31Z | ||||||
| dc.date.available | 2010-05-31T03:52:31Z | ||||||
| dc.date.issued | 2009 | ||||||
| dc.description.abstract | Surfactant protein D (SP-D) mediates clearance of microorganisms and modulates inflammation in response to cytotoxic stimulation. It is present in various epithelia, but also in vascular smooth muscle and endothelial cells. Experiments were designed to determine whether or not SP-D is present in porcine coronary arterial endothelial cells and if so, to investigate the molecular mechanisms underlying this presence. The expression of SP-D, NO synthase, Akt 1/2 and Erk 1/2 proteins was determined in cultures at passages 1 (#1) and 4 (#4). SP-D in primary cells existed in three isoforms (37-38 kDa and 50 kDa). The 37-38 kDa SP-D forms were the dominant isoforms in the porcine endothelium and were prominent at #1 but partially lost at #4. Tumor necrosis factor-α (TNF-α) significantly augmented the level of SP-D expression at #1 but not at #4. The basal level of 37-38 kDa SP-D isoforms at #1 was reduced by L-NAME, wortmannin and PD 98059. The low basal expression at #4 could be increased by DETA NONOate (donor of NO) or insulin (activator of PI3K/Akt). The presence of nitric oxide synthase was reduced while that of Akt 1/2 and Erk 1/2 was increased at #4. In cells both at passages 1 and 4, TNF-α downregulated NO synthase and up-regulated p-Erk 1/2 protein. The present findings demonstrate the presence of SP-D in endothelial cells which is NO-, PI3K/Akt- and Erk-dependent. They suggest a protective role of SP-D in these cells. © 2008 Elsevier Ltd. All rights reserved. | ||||||
| dc.description.nature | postprint | ||||||
| dc.identifier.citation | Molecular Immunology, 2009, v. 46 n. 6, p. 1050-1057 [How to Cite?] DOI: http://dx.doi.org/10.1016/j.molimm.2008.09.027 | ||||||
| dc.identifier.doi | http://dx.doi.org/10.1016/j.molimm.2008.09.027 | ||||||
| dc.identifier.epage | 1057 | ||||||
| dc.identifier.hkuros | 161389 | ||||||
| dc.identifier.isi | WOS:000264693200005
Funding Information: We thank Ms. Chung Yee Hat for her technical support in the laboratory. This work was supported by grants from the Research Grant Council of Hong Kong (HKU7490/06M) and the Research Centre of Heart, Brain, Hormone & Healthy Aging of The University of Hong Kong. | ||||||
| dc.identifier.issn | 0161-5890 2011 Impact Factor: 2.897 2011 SCImago Journal Rankings: 0.401 | ||||||
| dc.identifier.issue | 6 | ||||||
| dc.identifier.openurl | | ||||||
| dc.identifier.pmid | 19010548 | ||||||
| dc.identifier.scopus | eid_2-s2.0-61449196879 | ||||||
| dc.identifier.spage | 1050 | ||||||
| dc.identifier.uri | http://hdl.handle.net/10722/59549 | ||||||
| dc.identifier.volume | 46 | ||||||
| dc.language | eng | ||||||
| dc.publisher | Pergamon. The Journal's web site is located at http://www.elsevier.com/locate/molimm | ||||||
| dc.publisher.place | United Kingdom | ||||||
| dc.relation.ispartof | Molecular Immunology | ||||||
| dc.relation.references | References in Scopus | ||||||
| dc.rights | Creative Commons: Attribution 3.0 Hong Kong License | ||||||
| dc.subject.mesh | Endothelial Cells - metabolism | ||||||
| dc.subject.mesh | Endothelium, Vascular - cytology - metabolism | ||||||
| dc.subject.mesh | Extracellular Signal-Regulated MAP Kinases - metabolism | ||||||
| dc.subject.mesh | Nitric Oxide - metabolism | ||||||
| dc.subject.mesh | Proto-Oncogene Proteins c-akt - metabolism | ||||||
| dc.subject | Endothelial cells | ||||||
| dc.subject | Nitric oxide | ||||||
| dc.subject | SP-D | ||||||
| dc.subject | TNF-α | ||||||
| dc.title | The presence and activity of SP-D in porcine coronary endothelial cells depend on Akt/PI3K, Erk and nitric oxide and decrease after multiple passaging | ||||||
| dc.type | Article |
Author Affiliations
- The University of Hong Kong Li Ka Shing Faculty of Medicine
- Syddansk Universitet