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A novel arachidonate-preferring acyl-CoA synthetase is present in steroidogenic cells of the rat adrenal, ovary, and testis
Open accessAbstract
We report herein the cDNA cloning of a novel rat acyl-CoA synthetase (ACS) that preferentially uses arachidonate and eicosapentaenoate. This newly identified ACS (designated ACS4) contains 670 amino acids and is 68% identical to rat ACS3, a previously characterized ACS that is highly expressed in brain. ACS4 was overproduced in Escherichia coli and the resulting enzyme was purified to homogeneity. The purified enzyme utilizes arachidonate and eicosapentaenoate most preferentially among C 8 –C 22 saturated fatty acids and C 14 –C 22 unsaturated fatty acids. Kinetic analyses revealed that the enzyme has a high affinity for arachidonate and eicosapentaenoate and low affinity for palmitate. ACS4 transcripts are detectable in a wide range of tissues, with the highest level in adrenal gland. Immunoreactivity to ACS4 was detected in the zona fasciculata and reticularis of adrenal gland, in the corpus luteum and stromal luteinized cells in ovary, and in the Leydig cells of testis.
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Cites
Primer-Directed Enzymatic Amplification of DNA with a Thermostable DNA Polymerase
Saiki, R. K., Gelfand, D. H., Stoffel, S., Scharf, S. J., Higuchi, R., Horn, G. T., Mullis, K. B., & Erlich, H. A. (1988) · Science · doi:10.1126/science.2448875 · Cited by 17,719
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Control of mitochondrial β-oxidation flux
Eaton, S. (2002) · Progress in Lipid Research · doi:10.1016/s0163-7827(01)00024-8 · Cited by 411
Westerbacka, J., Kolak, M., Kiviluoto, T., Arkkila, P., Sirén, J., Hamsten, A., Fisher, R. M., & Yki-Järvinen, H. (2007) · Diabetes · doi:10.2337/db07-0156 · Cited by 355
Shockey, J. M., Fulda, M. S., & Browse, J. A. (2002) · Plant Physiology · doi:10.1104/pp.003269 · Cited by 326
Dietary lipids fuel GPX4-restricted enteritis resembling Crohn’s disease
Mayr, L., Grabherr, F., Schwärzler, J., Reitmeier, I., Sommer, F., Gehmacher, T., Niederreiter, L., He, G.-W., Ruder, B., Kunz, K. T. R., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15646-6 · Cited by 292
Lewin, T. M., Kim, J.-H., Granger, D. A., Vance, J. E., & Coleman, R. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102036200 · Cited by 284
Metadata
- Authors
- Kang, M.-J., Fujino, T., Sasano, H., Minekura, H., Yabuki, N., Nagura, H., Iijima, H., & Yamamoto, T. T.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1997-04
- Volume
- 94
- Issue
- 7
- Pages
- 2880-2884
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2064702379
- Cited by
- 274
- References
- 1
- FWCI
- 4.20
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: A novel arachidonate-preferring acyl-CoA synthetase is present in steroidogenic cells of the rat adrenal, ovary, and testis. https://app.cochat.ai/papers/10.1073/pnas.94.7.2880
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- Kang, M.-J., Fujino, T., Sasano, H., Minekura, H., Yabuki, N., Nagura, H., Iijima, H., & Yamamoto, T. T. (1997). A novel arachidonate-preferring acyl-CoA synthetase is present in steroidogenic cells of the rat adrenal, ovary, and testis. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.94.7.2880
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