Adrenoleukodystrophy protein enhances association of very long-chain acyl-coenzyme a synthetase with the peroxisome

Takeshi Yamada, T. Taniwaki, N. Shinnoh, A. Uchiyama, N. Shimozawa, Y. Ohyagi, H. Asahara, J. Kira

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Objective: To clarify the function of adrenoleukodystrophy protein (ALDP) using our ALDP-deficient mice established by gene targeting: Background: X-linked adrenoleukodystrophy (ALD) is characterized biochemically by the accumulation of very long-chain fatty acids (VLCFA) in tissues and body fluids, and is caused by impairment of peroxisomal β- oxidation. In ALD, very long-chain acyl-coenzyme A synthetase (VLACS), which is necessary for peroxisoreal β-oxidation, does not function. Methods: The ALDP-deficient mice and C57BL/6J mice were used. VLACS or ALDP were transiently expressed by lipofection in murine fibroblasts, and VLCFA β- oxidation was assayed. Liver peroxisomes were purified by sequential centrifugations and a Nycodenz gradient centrifugation. The peroxisomal localization of VLACS was compared between the mutant and control mice using a Western blot analysis. Results: Impairment of VLCFA β-oxidation in ALDP- deficient fibroblasts was not corrected by the additional expression of VLACS alone but was by the coexpression of VLACS and ALDP. Although the tissue- specific expression of VLACS was similar in ALDP-deficient and normal mice, peroxisomal VLACS was clearly lower in ALDP-deficient than in normal mice. Conclusions: ALDP plays a role in the peroxisomal localization of VLACS, and VLACS does not function unless localized in the peroxisome.

Original languageEnglish
Pages (from-to)614-616
Number of pages3
JournalNeurology
Volume52
Issue number3
Publication statusPublished - Feb 1 1999

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Adrenoleukodystrophy
Peroxisomes
Coenzyme A Ligases
Coenzymes
Ligases
Proteins
Fatty Acids
Centrifugation
Fibroblasts
Iohexol
Gene Targeting
Body Fluids
Inbred C57BL Mouse

All Science Journal Classification (ASJC) codes

  • Clinical Neurology

Cite this

Yamada, T., Taniwaki, T., Shinnoh, N., Uchiyama, A., Shimozawa, N., Ohyagi, Y., ... Kira, J. (1999). Adrenoleukodystrophy protein enhances association of very long-chain acyl-coenzyme a synthetase with the peroxisome. Neurology, 52(3), 614-616.

Adrenoleukodystrophy protein enhances association of very long-chain acyl-coenzyme a synthetase with the peroxisome. / Yamada, Takeshi; Taniwaki, T.; Shinnoh, N.; Uchiyama, A.; Shimozawa, N.; Ohyagi, Y.; Asahara, H.; Kira, J.

In: Neurology, Vol. 52, No. 3, 01.02.1999, p. 614-616.

Research output: Contribution to journalArticle

Yamada, T, Taniwaki, T, Shinnoh, N, Uchiyama, A, Shimozawa, N, Ohyagi, Y, Asahara, H & Kira, J 1999, 'Adrenoleukodystrophy protein enhances association of very long-chain acyl-coenzyme a synthetase with the peroxisome', Neurology, vol. 52, no. 3, pp. 614-616.
Yamada T, Taniwaki T, Shinnoh N, Uchiyama A, Shimozawa N, Ohyagi Y et al. Adrenoleukodystrophy protein enhances association of very long-chain acyl-coenzyme a synthetase with the peroxisome. Neurology. 1999 Feb 1;52(3):614-616.
Yamada, Takeshi ; Taniwaki, T. ; Shinnoh, N. ; Uchiyama, A. ; Shimozawa, N. ; Ohyagi, Y. ; Asahara, H. ; Kira, J. / Adrenoleukodystrophy protein enhances association of very long-chain acyl-coenzyme a synthetase with the peroxisome. In: Neurology. 1999 ; Vol. 52, No. 3. pp. 614-616.
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AU - Taniwaki, T.

AU - Shinnoh, N.

AU - Uchiyama, A.

AU - Shimozawa, N.

AU - Ohyagi, Y.

AU - Asahara, H.

AU - Kira, J.

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