Medizinische Universität Graz - Research portal
Selected Publication:
Nöhammer, C; El-Shabrawi, Y; Schauer, S; Hiden, M; Berger, J; Forss-Petter, S; Winter, E; Eferl, R; Zechner, R; Hoefler, G.
cDNA cloning and analysis of tissue-specific expression of mouse peroxisomal straight-chain acyl-CoA oxidase.
EUR J BIOCHEM 2000 267: 1254-1260.
Doi: 10.1046%2Fj.1432-1327.2000.01128.x
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- Leading authors Med Uni Graz
- Höfler Gerald
- Co-authors Med Uni Graz
- El-Shabrawi Yosuf
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- Abstract:
- Straight-chain acyl-CoA oxidase is the first and rate limiting enzyme in the peroxisomal beta-oxidation pathway catalysing the desaturation of acyl-CoAs to 2-trans-enoyl-CoAs, thereby producing H2O2. To study peroxisomal beta-oxidation we cloned and characterized the cDNA of mouse peroxisomal acyl-CoA oxidase. It consists of 3778 bp, including a 1983-bp ORF encoding a polypeptide of 661 amino-acid residues. Like the rat and human homologue the C-terminus contains an SKL motif, an import signal present in several peroxisomal matrix proteins. Sequence analysis revealed high amino-acid homology with rat (96%) and human (87%) acyl-CoA oxidase in addition to minor homology ( approximately 40%) with other related proteins, such as rabbit trihydroxy-cholestanoyl-CoA oxidase, human branched chain acyl-CoA oxidase and rat trihydroxycoprostanoyl-CoA oxidase. Acyl-CoA oxidase mRNA and protein expression were most abundant in liver followed by kidney, brain and adipose tissue. During mouse brain development acyl-CoA oxidase mRNA expression was highest during the suckling period indicating that peroxisomal beta-oxidation is most critical during this developmental stage. Comparing tissue mRNA levels of peroxisome proliferator-activated receptor alpha and acyl-CoA oxidase, we noticed a constant relationship in all tissues investigated, except heart and adipose tissue in which much more, and respectively, much less, peroxisome proliferator-activated receptor alpha mRNA in proportion to acyl-CoA oxidase mRNA was found. Our data show that acyl-CoA oxidase is an evolutionary highly conserved enzyme with a distinct pattern of expression and indicate an important role in lipid metabolism.
- Find related publications in this database (using NLM MeSH Indexing)
- Acyl-CoA Oxidase -
- Amino Acid Motifs -
- Animals -
- Blotting, Western -
- Brain - embryology
- Cloning, Molecular - embryology
- Gene Expression Profiling - embryology
- Gene Expression Regulation, Developmental - embryology
- Humans - embryology
- Isoenzymes - chemistry
- Liver - enzymology
- Mice - enzymology
- Molecular Sequence Data - enzymology
- Molecular Weight - enzymology
- Organ Specificity - enzymology
- Oxidoreductases - chemistry
- Peroxisomes - enzymology
- Protein Sorting Signals - chemistry
- RNA, Messenger - analysis
- Receptors, Cytoplasmic and Nuclear - genetics
- Research Support, Non-U.S. Gov't - genetics
- Sequence Alignment - genetics
- Sequence Homology, Amino Acid - genetics
- Transcription Factors - genetics
- Find related publications in this database (Keywords)
- acyl-CoA oxidase
- beta-oxidation
- fatty acids
- peroxisomes
- PPAR alpha