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Proteomic Analysis of Rat Liver Peroxisome
Open accessAbstract
Subcellular proteomics, which includes isolation of subcellular components prior to a proteomic analysis, is advantageous not only in characterizing large macro-molecular complexes such as organelles but also in elucidating mechanisms of protein transport and organelle biosynthesis. Because of the high sensitivity achieved by the present proteomics technology, the purity of samples to be analyzed is important for the interpretation of the results obtained. In the present study, peroxisomes isolated from rat liver by usual cell fractionation were further purified by immunoisolation using a specific antibody raised against a peroxisomal membrane protein, PMP70. The isolated peroxisomes were analyzed by SDS-PAGE combined with liquid chromatography/mass spectrometry. Altogether 34 known peroxisomal proteins were identified in addition to several mitochondrial and microsomal proteins. Some of the latter may reside in the peroxisomes as well. Analysis of membrane fractions identified all known peroxins except for Pex7. Two new peroxisomal proteins of unknown function were of high abundance. One is a bi-functional protein consisting of an aminoglycoside phosphotransferase-domain and an acyl-CoA dehydrogenase domain. The other is a newly identified peroxisome-specific isoform of Lon protease, an ATP-dependent protease with chaperone-like activity. The peroxisomal localization of the protein was confirmed by immunological techniques. The peroxisome-type Lon protease, which is distinct from the mitochondrial isoform, may play an important role in the peroxisomal biogenesis.
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“Previous proteomic studies using isolated mammalian peroxisomes have identified ACBD5 as a peroxisomal protein (16,17).”
From Deficiency of a Retinal Dystrophy Protein, Acyl-CoA Binding Domain-containing 5 (ACBD5), Impairs Peroxisomal β-Oxidation of Very-long-chain Fatty Acids (2017) · cites this paper as [16]
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Metadata
- Authors
- Kikuchi, M., Hatano, N., Yokota, S., Shimozawa, N., Imanaka, T., & Taniguchi, H.
- Affiliations
- SPring-8 (JP)
- University of Yamanashi (JP)
- Gifu University (JP)
- University of Toyama (JP)
- Corresponding author
- Taniguchi, Hisaaki
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-01
- Volume
- 279
- Issue
- 1
- Pages
- 421-428
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2063731065
- Cited by
- 258
- References
- 34
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 6 · 2023: 9 · 2022: 3 · 2021: 3 · 2020: 8 · 2019: 6 · 2018: 9 · 2017: 6 · 2016: 11 · 2015: 11 · 2014: 11 · 2013: 13 · 2012: 12
- FWCI
- 7.97
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Keywords
- peroxisomes, peroxisomal proteins, peroxisome biogenesis, PMP70, immunoisolation, subcellular proteomics, peroxins, Lon protease, protein localization, rat liver
- MeSH terms
- Animals, Cell Fractionation, Enzymes, Heat-Shock Proteins, Isoenzymes, Liver, Regression Analysis, Serine Endopeptidases, Microscopy, Immunoelectron, Proteome, Peroxisomes, Protein Transport, ATP-Dependent Proteases, Rats
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