Proteomic and Bioinformatics Analyses of Mouse Liver Microsomes. (20th March 2012)
- Record Type:
- Journal Article
- Title:
- Proteomic and Bioinformatics Analyses of Mouse Liver Microsomes. (20th March 2012)
- Main Title:
- Proteomic and Bioinformatics Analyses of Mouse Liver Microsomes
- Authors:
- Peng, Fang
Zhan, Xianquan
Li, Mao-Yu
Fang, Fan
Li, Guoqing
Li, Cui
Zhang, Peng-Fei
Chen, Zhuchu - Other Names:
- Thongboonkerd Visith Academic Editor.
- Abstract:
- Abstract : Microsomes are derived mostly from endoplasmic reticulum and are an ideal target to investigate compound metabolism, membrane-bound enzyme functions, lipid-protein interactions, and drug-drug interactions. To better understand the molecular mechanisms of the liver and its diseases, mouse liver microsomes were isolated and enriched with differential centrifugation and sucrose gradient centrifugation, and microsome membrane proteins were further extracted from isolated microsomal fractions by the carbonate method. The enriched microsome proteins were arrayed with two-dimensional gel electrophoresis (2DE) and carbonate-extracted microsome membrane proteins with one-dimensional gel electrophoresis (1DE). A total of 183 2DE-arrayed proteins and 99 1DE-separated proteins were identified with tandem mass spectrometry. A total of 259 nonredundant microsomal proteins were obtained and represent the proteomic profile of mouse liver microsomes, including 62 definite microsome membrane proteins. The comprehensive bioinformatics analyses revealed the functional categories of those microsome proteins and provided clues into biological functions of the liver. The systematic analyses of the proteomic profile of mouse liver microsomes not only reveal essential, valuable information about the biological function of the liver, but they also provide important reference data to analyze liver disease-related microsome proteins for biomarker discovery and mechanism clarification ofAbstract : Microsomes are derived mostly from endoplasmic reticulum and are an ideal target to investigate compound metabolism, membrane-bound enzyme functions, lipid-protein interactions, and drug-drug interactions. To better understand the molecular mechanisms of the liver and its diseases, mouse liver microsomes were isolated and enriched with differential centrifugation and sucrose gradient centrifugation, and microsome membrane proteins were further extracted from isolated microsomal fractions by the carbonate method. The enriched microsome proteins were arrayed with two-dimensional gel electrophoresis (2DE) and carbonate-extracted microsome membrane proteins with one-dimensional gel electrophoresis (1DE). A total of 183 2DE-arrayed proteins and 99 1DE-separated proteins were identified with tandem mass spectrometry. A total of 259 nonredundant microsomal proteins were obtained and represent the proteomic profile of mouse liver microsomes, including 62 definite microsome membrane proteins. The comprehensive bioinformatics analyses revealed the functional categories of those microsome proteins and provided clues into biological functions of the liver. The systematic analyses of the proteomic profile of mouse liver microsomes not only reveal essential, valuable information about the biological function of the liver, but they also provide important reference data to analyze liver disease-related microsome proteins for biomarker discovery and mechanism clarification of liver disease. … (more)
- Is Part Of:
- International journal of proteomics. Volume 2012(2012)
- Journal:
- International journal of proteomics
- Issue:
- Volume 2012(2012)
- Issue Display:
- Volume 2012, Issue 2012 (2012)
- Year:
- 2012
- Volume:
- 2012
- Issue:
- 2012
- Issue Sort Value:
- 2012-2012-2012-0000
- Page Start:
- Page End:
- Publication Date:
- 2012-03-20
- Subjects:
- Proteomics -- Periodicals
Proteomics
Proteomics
Electronic journals
Periodical
Fulltext
Internet Resources
Periodicals
Periodicals
572.6 - Journal URLs:
- http://bibpurl.oclc.org/web/44802 ↗
https://www.hindawi.com/journals/ijpro/ ↗
http://bibpurl.oclc.org/web/44803 ↗
http://www.ncbi.nlm.nih.gov/pmc/journals/1629/ ↗ - DOI:
- 10.1155/2012/832569 ↗
- Languages:
- English
- ISSNs:
- 2090-2166
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library HMNTS - ELD Digital store
- Ingest File:
- 10557.xml