File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
  • Find via Find It@HKUL
Supplementary

Conference Paper: Proteomics of Macrophage: An Approach to Understand Lipopolysaccharide Challenged Inflammation

TitleProteomics of Macrophage: An Approach to Understand Lipopolysaccharide Challenged Inflammation
Authors
Issue Date2005
PublisherAmerican Society for Biochemistry and Molecular Biology
Citation
HUPO 4th Annual World Congress, Munich, Germany, 28 August-1 September 2005. In Molecular & Cellular Proteomics: MCP, 2005, v. 4 n. 8 suppl 1, p. S231 How to Cite?
AbstractLipopolysaccharide (LPS) has been implicated as one of the major cause of inflammation, sepsis and shock, that are, life-threatening syndromes often occurring in intensive care unit patients. In order to detect diseaserelevant process and biomarkers for alleviating the inflammation or sepsis shock upon bacterial infection, proteome of macrophage cell line RAW 264.7 primed with LPS for 24 hours in vitro was determined using 2DE. Isoelectric focusing was performed on whole cell extracts using 11cm pH 4 –7 IPG strips. Focused proteins were resolved in 12% SDS-polyacrylamide gels and visualized by silver-stain. The proteomes patterns were analyzed by the Melanie III 2D analysis software. Three proteins out of approximately 720 detected were decreased in abundance as a result of the priming with LPS. These proteins were isolated and identified by comparing the masses of their tryptic digested peptides with those of the known proteins, using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and the SWISSPROT database. The putative identities of these proteins were mitochondrial respiratory chain enzymes, glyceraldehyde-3-phosphate dehydrogenase, putative tumor suppressor molecule, prohibitin, pyrimidine nucleotides synthesis enzymes, and UMP/CMP kinase. Many of these proteins possess important functions in inflammation. This high-resolution 2DE and protein identification technique allows one to rapidly discover new potential candidate proteins which can be used to develop targeted drugs proteins for the prevention and treatment of endotoxemia.
Persistent Identifierhttp://hdl.handle.net/10722/113189
ISSN
2015 Impact Factor: 5.912
2015 SCImago Journal Rankings: 3.213

 

DC FieldValueLanguage
dc.contributor.authorLiu, SYKen_HK
dc.contributor.authorTsang, JSHen_HK
dc.contributor.authorLeung, PCen_HK
dc.contributor.authorChow, BKCen_HK
dc.contributor.authorWan, JMFen_HK
dc.date.accessioned2010-09-26T04:04:53Z-
dc.date.available2010-09-26T04:04:53Z-
dc.date.issued2005en_HK
dc.identifier.citationHUPO 4th Annual World Congress, Munich, Germany, 28 August-1 September 2005. In Molecular & Cellular Proteomics: MCP, 2005, v. 4 n. 8 suppl 1, p. S231-
dc.identifier.issn1535-9476-
dc.identifier.urihttp://hdl.handle.net/10722/113189-
dc.description.abstractLipopolysaccharide (LPS) has been implicated as one of the major cause of inflammation, sepsis and shock, that are, life-threatening syndromes often occurring in intensive care unit patients. In order to detect diseaserelevant process and biomarkers for alleviating the inflammation or sepsis shock upon bacterial infection, proteome of macrophage cell line RAW 264.7 primed with LPS for 24 hours in vitro was determined using 2DE. Isoelectric focusing was performed on whole cell extracts using 11cm pH 4 –7 IPG strips. Focused proteins were resolved in 12% SDS-polyacrylamide gels and visualized by silver-stain. The proteomes patterns were analyzed by the Melanie III 2D analysis software. Three proteins out of approximately 720 detected were decreased in abundance as a result of the priming with LPS. These proteins were isolated and identified by comparing the masses of their tryptic digested peptides with those of the known proteins, using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and the SWISSPROT database. The putative identities of these proteins were mitochondrial respiratory chain enzymes, glyceraldehyde-3-phosphate dehydrogenase, putative tumor suppressor molecule, prohibitin, pyrimidine nucleotides synthesis enzymes, and UMP/CMP kinase. Many of these proteins possess important functions in inflammation. This high-resolution 2DE and protein identification technique allows one to rapidly discover new potential candidate proteins which can be used to develop targeted drugs proteins for the prevention and treatment of endotoxemia.-
dc.languageengen_HK
dc.publisherAmerican Society for Biochemistry and Molecular Biology-
dc.relation.ispartofMolecular & Cellular Proteomics: MCPen_HK
dc.titleProteomics of Macrophage: An Approach to Understand Lipopolysaccharide Challenged Inflammationen_HK
dc.typeConference_Paperen_HK
dc.identifier.emailTsang, JSH: jshtsang@hkucc.hku.hken_HK
dc.identifier.emailLeung, PC: pcleung@hkucc.hku.hken_HK
dc.identifier.emailChow, BKC: bkcc@hkusua.hku.hken_HK
dc.identifier.emailWan, JMF: jmfwan@hkusua.hku.hken_HK
dc.identifier.authorityTsang, JSH=rp00792en_HK
dc.identifier.authorityLeung, PC=rp00735en_HK
dc.identifier.authorityChow, BKC=rp00681en_HK
dc.identifier.authorityWan, JMF=rp00798en_HK
dc.identifier.hkuros104576en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats