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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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TitleThe presence and activity of SP-D in porcine coronary endothelial cells depend on Akt/PI3K, Erk and nitric oxide and decrease after multiple passaging
 
AuthorsLee, MYK1
Sørensen, GL2
Holmskov, U2
Vanhoutte, PM1
 
KeywordsEndothelial cells
Nitric oxide
SP-D
TNF-α
 
Issue Date2009
 
PublisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/molimm
 
CitationMolecular Immunology, 2009, v. 46 n. 6, p. 1050-1057 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.molimm.2008.09.027
 
AbstractSurfactant 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.
 
ISSN0161-5890
2012 Impact Factor: 2.645
2012 SCImago Journal Rankings: 1.159
 
DOIhttp://dx.doi.org/10.1016/j.molimm.2008.09.027
 
ISI Accession Number IDWOS:000264693200005
Funding AgencyGrant Number
Research Grant Council of Hong KongHKU7490/06M
Research Centre of Heart, Brain, Hormone & Healthy Aging of The University of Hong Kong
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.

 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorLee, MYK
 
dc.contributor.authorSørensen, GL
 
dc.contributor.authorHolmskov, U
 
dc.contributor.authorVanhoutte, PM
 
dc.date.accessioned2010-05-31T03:52:31Z
 
dc.date.available2010-05-31T03:52:31Z
 
dc.date.issued2009
 
dc.description.abstractSurfactant 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.naturepostprint
 
dc.identifier.citationMolecular 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.doihttp://dx.doi.org/10.1016/j.molimm.2008.09.027
 
dc.identifier.epage1057
 
dc.identifier.hkuros161389
 
dc.identifier.isiWOS:000264693200005
Funding AgencyGrant Number
Research Grant Council of Hong KongHKU7490/06M
Research Centre of Heart, Brain, Hormone & Healthy Aging of The University of Hong Kong
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.issn0161-5890
2012 Impact Factor: 2.645
2012 SCImago Journal Rankings: 1.159
 
dc.identifier.issue6
 
dc.identifier.openurl
 
dc.identifier.pmid19010548
 
dc.identifier.scopuseid_2-s2.0-61449196879
 
dc.identifier.spage1050
 
dc.identifier.urihttp://hdl.handle.net/10722/59549
 
dc.identifier.volume46
 
dc.languageeng
 
dc.publisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/molimm
 
dc.publisher.placeUnited Kingdom
 
dc.relation.ispartofMolecular Immunology
 
dc.relation.referencesReferences in Scopus
 
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License
 
dc.subject.meshEndothelial Cells - metabolism
 
dc.subject.meshEndothelium, Vascular - cytology - metabolism
 
dc.subject.meshExtracellular Signal-Regulated MAP Kinases - metabolism
 
dc.subject.meshNitric Oxide - metabolism
 
dc.subject.meshProto-Oncogene Proteins c-akt - metabolism
 
dc.subjectEndothelial cells
 
dc.subjectNitric oxide
 
dc.subjectSP-D
 
dc.subjectTNF-α
 
dc.titleThe 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.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong Li Ka Shing Faculty of Medicine
  2. Syddansk Universitet