Characterization of mouse homolog of brain acyl-CoA hydrolase: molecular cloning and neuronal localization

Kuramochi, Yu; Takagi-Sakuma, Mitsuhiro; Kitahara, Mari; Emori, Ryoko; Asaba, Yusuke; Sakaguchi, Reiko; Watanabe, Takafumi; Kuroda, Junji; Hiratsuka, Kazuyuki; Nagae, Yusuke; Suga, Tetsuya; Yamada, Junji

doi:10.1016/s0169-328x(01)00323-0

Cited by 37 publications

(34 citation statements)

References 36 publications

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“…There is evidently a poor correlation between mRNA and protein levels in testis and brain, with much higher protein levels in brain compared to mRNA, while testis contains a higher amount of mRNA than protein (similar to what has previously been reported in rat and mouse, see (11,16)), suggesting regulation also at the post-transcriptional level. In addition, strong expression was detected in lung, with weak expression in kidney, heart, spleen and WAT.…”

Section: Tissue Expression Of Acot7 Mrna Transcriptssupporting

confidence: 79%

“…Kuramochi et al identified a 5'-RACE cDNA in mouse (called MBACH-K2), resulting in a protein that is 29 amino acids longer in the N-terminal end (16). We have now identified one EST (CX225643) that corresponds to a differently spliced version of Exon Ic, lacking the in-frame stop codon (see Fig.…”

Section: Identification Of Three Further Putative 1 St Exonsmentioning

confidence: 94%

“…Previous data has shown that in rat (24) and mouse (16), the expression of the Acot7_v1 transcript and protein is mainly confined to brain and testis. To further investigate the tissue expression of Acot isoenzymes, we examined the mRNA and protein levels in both male and female mouse tissues.…”

Section: Tissue Expression Of Acot7 Mrna Transcriptsmentioning

confidence: 95%

“…In human brain, ACOT7 is expressed in neurons, e.g pyramidal cells in the cerebral cortex and Purkinje cells in the cerebellum (14). In developing mouse brain, Acot7 was shown to be expressed during embryogenesis in association with neuronal differentiation (15), and in adult mouse brain ACOT7 is exclusively localized to neurons (16). Recently, the genomic structure of the Acot7 gene family was characterized in both human and mouse (14,16).…”

Section: Introductionmentioning

confidence: 99%

“…In developing mouse brain, Acot7 was shown to be expressed during embryogenesis in association with neuronal differentiation (15), and in adult mouse brain ACOT7 is exclusively localized to neurons (16). Recently, the genomic structure of the Acot7 gene family was characterized in both human and mouse (14,16). Although these works showed that several isoforms of Acot7 are generated from a single gene following alternative splicing of different first exons, with the resulting proteins being expressed mainly in brain and testis, the function of Acot7 is still unknown in these tissues.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Alternative exon usage selectively determines both tissue distribution and subcellular localization of the acyl-CoA thioesterase 7 gene products

Hunt

Greene

Hultenby

et al. 2007

Cell. Mol. Life Sci.

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Section: Tissue Expression Of Acot7 Mrna Transcriptssupporting

confidence: 79%

Section: Identification Of Three Further Putative 1 St Exonsmentioning

confidence: 94%

Section: Tissue Expression Of Acot7 Mrna Transcriptsmentioning

confidence: 95%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Alternative exon usage selectively determines both tissue distribution and subcellular localization of the acyl-CoA thioesterase 7 gene products

Hunt

Greene

Hultenby

et al. 2007

Cell. Mol. Life Sci.

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Intratesticular localization of the organic solute carrier protein, OSCP1, in spermatogenic cells in mice

Hiratsuka

Yin

Ohtomo

et al. 2008

Molecular Reproduction Devel

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Organic solute carrier protein 1 (OSCP1) is a recently described human gene that facilitates the transport of various organic solutes into the cell, when expressed in frog eggs. In this study, we cloned a mouse ortholog of OSCP1 encoding 379 amino acid protein, with 94% homology to the human counterpart. The mouse OSCP1 mRNA was predominantly expressed in the testis, in which it was attributed to the spermatogenic cells, except the spermatogonia. Immunohistochemistry confirmed that OSCP1 protein is continuously expressed during spermatogenesis in a stage- and cell type-specific manner, in the leptotene spermatocytes at stage IX through step 15 spermatids. Subcellular fractionation of mouse testis homogenates indicated that OSCP1 is a 45-kDa cytosolic protein. Moreover, when green fluorescent protein-OSCP1 fusion constructs were transfected into cultured cells, the fluorescence localized evenly in the cytoplasm. These results suggest that mouse testis OSCP1 may indirectly mediate substrate uptake into meiotic and spermiogenic germ cells, within the cytosol.

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Acyl-CoA thioesterase 9 (ACOT9) in mouse may provide a novel link between fatty acid and amino acid metabolism in mitochondria

Tillander

Nordström

Reilly

et al. 2013

Cell. Mol. Life Sci.

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Acyl-CoA thioesterase (ACOT) activities are found in prokaryotes and in several compartments of eukaryotes where they hydrolyze a wide range of acyl-CoA substrates and thereby regulate intracellular acyl-CoA/CoA/fatty acid levels. ACOT9 is a mitochondrial ACOT with homologous genes found from bacteria to humans and in this study we have carried out an in-depth kinetic characterization of ACOT9 to determine its possible physiological function. ACOT9 showed unusual kinetic properties with activity peaks for short-, medium-, and saturated long-chain acyl-CoAs with highest V max with propionyl-CoA and (iso) butyryl-CoA while K cat/K m was highest with saturated long-chain acyl-CoAs. Further characterization of the short-chain acyl-CoA activity revealed that ACOT9 also hydrolyzes a number of short-chain acyl-CoAs and short-chain methyl-branched CoA esters that suggest a role for ACOT9 in regulation also of amino acid metabolism. In spite of markedly different K ms, ACOT9 can hydrolyze both short- and long-chain acyl-CoAs simultaneously, indicating that ACOT9 may provide a novel regulatory link between fatty acid and amino acid metabolism in mitochondria. Based on similar acyl-CoA chain-length specificities of recombinant ACOT9 and ACOT activity in mouse brown adipose tissue and kidney mitochondria, we conclude that ACOT9 is the major mitochondrial ACOT hydrolyzing saturated C2-C20-CoA in these tissues. Finally, ACOT9 activity is strongly regulated by NADH and CoA, suggesting that mitochondrial metabolic state regulates the function of ACOT9.

show abstract

Characterization of mouse homolog of brain acyl-CoA hydrolase: molecular cloning and neuronal localization

Cited by 37 publications

References 36 publications

Alternative exon usage selectively determines both tissue distribution and subcellular localization of the acyl-CoA thioesterase 7 gene products

Alternative exon usage selectively determines both tissue distribution and subcellular localization of the acyl-CoA thioesterase 7 gene products

Intratesticular localization of the organic solute carrier protein, OSCP1, in spermatogenic cells in mice

Acyl-CoA thioesterase 9 (ACOT9) in mouse may provide a novel link between fatty acid and amino acid metabolism in mitochondria

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