Intracellular cholesterol transport

Seedorf, Udo; Brysch, P.; Engel, Thomas; Scheek, Sigrid; Raabe, Martin; Fobker, Manfred; Szyperski, Thomas; Wüthrich, Kurt; Maeda, Nobuyo; Assmann, Gerd

doi:10.1007/978-94-011-6585-3_5

Cited by 14 publications

(21 citation statements)

References 21 publications

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“…This larger transcript was found to code for a 58-kDa protein with two domains : a thiolase domain and a SCP domain. Seedorf et al [27] studied the thiolase activity of the 58-kDa protein and concluded that its substrate specificity was not much different from the original thiolase identified by Hashimoto et al [12]. However, in this study Seedorf et al [27] only tested the 3-ketoacyl-CoA esters of straight-chain fatty acids.…”

Section: Multiple Peroxisomal Thiolasesmentioning

confidence: 83%

“…Seedorf et al [27] studied the thiolase activity of the 58-kDa protein and concluded that its substrate specificity was not much different from the original thiolase identified by Hashimoto et al [12]. However, in this study Seedorf et al [27] only tested the 3-ketoacyl-CoA esters of straight-chain fatty acids. When we studied the reactivity of the two thiolases with the 3-ketoacyl-CoA esters of pristanic acid [25] and T H C A [28], clear differences between the two thiolases were found, with only the 58-kDa SCP/thiolase reactive with these branched-chain substrates.…”

Section: Multiple Peroxisomal Thiolasesmentioning

confidence: 83%

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Lipid metabolism in peroxisomes: enzymology, functions and dysfunctions of the fatty acid α- and β-oxidation systems in humans

Wanders

Grunsven

Jansen

2000

Biochemical Society Transactions

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Peroxisomes are subcellular organelles present in virtually all eukaryotic cells catalysing a number of indispensable functions in cellular metabolism. The importance of peroxisomes in man is stressed by the existence of an expanding group of genetic diseases in which there is an impairment in one or more peroxisomal functions. One of the major functions of peroxisomes concerns their role in lipid metabolism, which includes: (i) fatty acid betaoxidation; (ii) ether phospholipid synthesis; (iii) fatty acid alpha-oxidation; and (iv) isoprenoid biosynthesis. In this paper, we review the current state of knowledge concerning the peroxisomal fatty acid alpha- and beta-oxidation systems with particular emphasis on the enzymes involved and the various disorders of fatty acid oxidation in peroxisomes. We also pay attention to the fact that some of the metabolites that accumulate as the result of a defect in peroxisomal alpha- and/or beta-oxidation are activators of members of the family of nuclear receptors, including peroxisome-proliferator-activated receptor alpha.

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Section: Multiple Peroxisomal Thiolasesmentioning

confidence: 83%

Section: Multiple Peroxisomal Thiolasesmentioning

confidence: 83%

Lipid metabolism in peroxisomes: enzymology, functions and dysfunctions of the fatty acid α- and β-oxidation systems in humans

Wanders

Grunsven

Jansen

2000

Biochemical Society Transactions

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“…Initially it was observed that the first 400 amino acid residues of SCPx showed significant sequence homology with peroxisomal and mitochondria1 3-ketoacyl-CoA thiolase [ 15,161. Purified recombinant SCPx was indeed found to have thiolase activity with a preference for straight medium-chain acyl-CoA substrates but also sterol carrier and lipid transfer activity similar to that of nsL-TP [18]. Since the substrate specificity of SCPx did not appear to differ much from that of the conventional peroxisomal 3-ketoacyl-CoA thiolase (thiolase A, type 1) we wondered what purpose would be served by having two thiolases present in the peroxisomes.…”

Section: Scpxmentioning

confidence: 94%

The non-specific lipid transfer protein (sterol carrier protein 2) acts as a peroxisomal fatty acyl-CoA binding protein

Wirtz

Wouters

Bastiaens

et al. 1998

Biochemical Society Transactions

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“…From comparison with the GenBank\EMBL database it was noted that the sequence of the first 400 residues of the rat liver 58 kDa protein (the putative 46 kDa protein) was 50 % similar to those of the peroxisomal and mitochondrial 3-oxoacyl-CoA thiolases [67]. Recombinant 58 kDa protein (also denoted SCP x ) obtained after expression of the encoding gene in Escherichia coli indeed cleaved 3-oxo-acyl-CoA [16]. In addition, in itro this novel peroxisomal thiolase expressed nsL-TP activity.…”

Section: Function In Peroxisomesmentioning

confidence: 99%

“…Further studies on these and other known phospholipid transfer proteins are bound to reveal new insights in their important role as mediators between lipid metabolism and cell functions. related 58 kDa protein, is prominently present in peroxisomes [15] and that these proteins play a key role in the peroxisomal βoxidation of fatty acids ( [16] ; F. S. Wouters, P. I. H. Bastiaens, K. W. A. Wirtz and T. M. Jovin, unpublished work). This review will focus on PI-TP and nsL-TP with an emphasis on the most recent developments pertaining to the function of these proteins.…”

Section: Introductionmentioning

confidence: 99%

Phospholipid transfer proteins revisited

Wirtz

1997

Biochemical Journal

179

116

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Phosphatidylinositol transfer protein (PI-TP) and the non-specific lipid transfer protein (nsL-TP) (identical with sterol carrier protein 2) belong to the large and diverse family of intracellular lipid-binding proteins. Although these two proteins may express a comparable phospholipid transfer activity in vitro, recent studies in yeast and mammalian cells have indicated that they serve completely different functions. PI-TP (identical with yeast SEC14p) plays an important role in vesicle flow both in the budding reaction from the trans-Golgi network and in the fusion reaction with the plasma membrane. In yeast, vesicle budding is linked to PI-TP regulating Golgi phosphatidylcholine (PC) biosynthesis with the apparent purpose of maintaining an optimal PI/PC ratio of the Golgi complex. In mammalian cells, vesicle flow appears to be dependent on PI-TP stimulating phosphatidylinositol 4,5-bisphosphate (PIP2) synthesis. This latter process may also be linked to the ability of PI-TP to reconstitute the receptor-controlled PIP2-specific phospholipase C activity. The nsL-TP is a peroxisomal protein which, by its ability to bind fatty acyl-CoAs, is most likely involved in the beta-oxidation of fatty acids in this organelle. This protein constitutes the N-terminus of the 58 kDa protein which is one of the peroxisomal 3-oxo-acyl-CoA thiolases. Further studies on these and other known phospholipid transfer proteins are bound to reveal new insights in their important role as mediators between lipid metabolism and cell functions.

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Intracellular cholesterol transport

Cited by 14 publications

References 21 publications

Lipid metabolism in peroxisomes: enzymology, functions and dysfunctions of the fatty acid α- and β-oxidation systems in humans

Lipid metabolism in peroxisomes: enzymology, functions and dysfunctions of the fatty acid α- and β-oxidation systems in humans

The non-specific lipid transfer protein (sterol carrier protein 2) acts as a peroxisomal fatty acyl-CoA binding protein

Phospholipid transfer proteins revisited

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