Triton X-114 phase separation in the isolation and purification of mouse liver microsomal membrane proteins
Integral membrane proteins (IMPs) mediate several cellular functions including cell adhesion, ion and nutrient transport, and cell signalling. IMPs are typically hard to isolate and purify due to their hydrophobic nature and low cellular abundance, however, microsomes are small lipid vesicles rich i...
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Published in | Methods (San Diego, Calif.) Vol. 54; no. 4; pp. 396 - 406 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
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United States
Elsevier Inc
01.08.2011
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Abstract | Integral membrane proteins (IMPs) mediate several cellular functions including cell adhesion, ion and nutrient transport, and cell signalling. IMPs are typically hard to isolate and purify due to their hydrophobic nature and low cellular abundance, however, microsomes are small lipid vesicles rich in IMPs, which form spontaneously when cells are mechanically disrupted. In this study, we have employed mouse liver microsomes as a model for optimising a method for IMP isolation and characterisation. Microsomes were collected by differential centrifugation, purified with sodium carbonate, and subjected to GeLC–MS/MS analysis. A total of 1124 proteins were identified in the microsome fraction, with 47% (524/1124) predicted by TMHMM to contain at least one transmembrane domain (TMD). The ability of phase partitioning using the detergent Triton X-114 (TX-114) to further enrich for membrane proteins was evaluated. Microsomes were subjected to successive rounds of solubility-based phase separation, with proteins partitioning into the aqueous phase, detergent phase, or TX-114-insoluble pellet fraction. GeLC–MS/MS analysis of the three TX-114 fractions identified 1212 proteins, of which 146 were not detected in the un-fractionated microsome sample. Conspicuously, IMPs partitioned to the detergent phase, with 56% (435/770) of proteins identified in that fraction containing at least one TMD. GO Slim characterisation of the microsome proteome revealed enrichment of proteins from the endoplasmic reticulum, mitochondria, Golgi apparatus, endosome, and cytoplasm. Further, enzymes including monooxygenases were well represented with 35 cytochrome P450 identifications (CYPs 1A2, 2A5, 2A12, 2B10, 2C29, 2C37, 2C39, 2C44, 2C50, 2C54. 2C67, 2C68, 2C70, 2D10, 2D11, 2D22, 2D26, 2D9, 2E1, 2F2, 2J5, 2U1, 3A11, 3A13, 3A25, 4A10, 4A12A, 4A12B, 4F13, 4F14, 4F15, 4V3, 51,7B1, and 8B1). Evaluation of biological processes showed enrichment of proteins involved in fatty acid biosynthesis and elongation, as well as steroid synthesis. In addition, transport proteins including 24 members of the Rab family of GTPases were identified. Comparison of this dataset with the current mouse liver microsome proteome contributes an additional 648 protein identifications, of which 50% (326/648) contain at least one TMD. |
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AbstractList | Integral membrane proteins (IMPs) mediate several cellular functions including cell adhesion, ion and nutrient transport, and cell signalling. IMPs are typically hard to isolate and purify due to their hydrophobic nature and low cellular abundance, however, microsomes are small lipid vesicles rich in IMPs, which form spontaneously when cells are mechanically disrupted. In this study, we have employed mouse liver microsomes as a model for optimising a method for IMP isolation and characterisation. Microsomes were collected by differential centrifugation, purified with sodium carbonate, and subjected to GeLC-MS/MS analysis. A total of 1124 proteins were identified in the microsome fraction, with 47% (524/1124) predicted by TMHMM to contain at least one transmembrane domain (TMD). The ability of phase partitioning using the detergent Triton X-114 (TX-114) to further enrich for membrane proteins was evaluated. Microsomes were subjected to successive rounds of solubility-based phase separation, with proteins partitioning into the aqueous phase, detergent phase, or TX-114-insoluble pellet fraction. GeLC-MS/MS analysis of the three TX-114 fractions identified 1212 proteins, of which 146 were not detected in the un-fractionated microsome sample. Conspicuously, IMPs partitioned to the detergent phase, with 56% (435/770) of proteins identified in that fraction containing at least one TMD. GO Slim characterisation of the microsome proteome revealed enrichment of proteins from the endoplasmic reticulum, mitochondria, Golgi apparatus, endosome, and cytoplasm. Further, enzymes including monooxygenases were well represented with 35 cytochrome P450 identifications (CYPs 1A2, 2A5, 2A12, 2B10, 2C29, 2C37, 2C39, 2C44, 2C50, 2C54. 2C67, 2C68, 2C70, 2D10, 2D11, 2D22, 2D26, 2D9, 2E1, 2F2, 2J5, 2U1, 3A11, 3A13, 3A25, 4A10, 4A12A, 4A12B, 4F13, 4F14, 4F15, 4V3, 51,7B1, and 8B1). Evaluation of biological processes showed enrichment of proteins involved in fatty acid biosynthesis and elongation, as well as steroid synthesis. In addition, transport proteins including 24 members of the Rab family of GTPases were identified. Comparison of this dataset with the current mouse liver microsome proteome contributes an additional 648 protein identifications, of which 50% (326/648) contain at least one TMD. |
Author | Greening, David W. Kapp, Eugene A. Chen, Yuan-Shou Mathias, Rommel A. Mathivanan, Suresh Simpson, Richard J. |
Author_xml | – sequence: 1 givenname: Rommel A. surname: Mathias fullname: Mathias, Rommel A. organization: Ludwig Institute for Cancer Research, Parkville, Victoria, Australia – sequence: 2 givenname: Yuan-Shou surname: Chen fullname: Chen, Yuan-Shou organization: Ludwig Institute for Cancer Research, Parkville, Victoria, Australia – sequence: 3 givenname: Eugene A. surname: Kapp fullname: Kapp, Eugene A. organization: Ludwig Institute for Cancer Research, Parkville, Victoria, Australia – sequence: 4 givenname: David W. surname: Greening fullname: Greening, David W. organization: Ludwig Institute for Cancer Research, Parkville, Victoria, Australia – sequence: 5 givenname: Suresh surname: Mathivanan fullname: Mathivanan, Suresh organization: Ludwig Institute for Cancer Research, Parkville, Victoria, Australia – sequence: 6 givenname: Richard J. surname: Simpson fullname: Simpson, Richard J. email: Richard.Simpson@ludwig.edu.au organization: Ludwig Institute for Cancer Research, Parkville, Victoria, Australia |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21272644$$D View this record in MEDLINE/PubMed |
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Keywords | IPI Liver DP TMHMM LC–MS/MS TX-114 CMC MF Membrane CYP Detergent Cytochrome P450 2-D TMD 3-D IMP ER MGF Microsomes AP PF GRAVY Proteomics Triton X-114 Mass spectrometry |
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Snippet | Integral membrane proteins (IMPs) mediate several cellular functions including cell adhesion, ion and nutrient transport, and cell signalling. IMPs are... |
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SubjectTerms | Animals Chemical Fractionation - methods Cytochrome P450 Detergent Liver Mass spectrometry Membrane Membrane Proteins - isolation & purification Mice Microsomes Microsomes, Liver - metabolism Polyethylene Glycols - chemistry Proteome Proteomics Triton X-114 |
Title | Triton X-114 phase separation in the isolation and purification of mouse liver microsomal membrane proteins |
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