The non-specific lipid-transfer protein (sterol carrier protein 2) and its relationship to peroxisomes

Defective peroxisomal catabolism of branched fatty acyl coenzyme A in mice lacking the sterol carrier protein-2/sterol carrier protein-x gene function

“…Thus, the Scp2 gene is somewhat reminiscent of a bacterial operon, in which distinct functions that act in the same metabolic pathway are combined in a common transcriptional unit. This role is consistent with its genetic organization, the well-established peroxisomal localization of SCP2 and SCPx (Keller et al 1989;Ossendorp and Wirtz 1993), the ability of SCP2 to bind phytanoyl-CoA in vitro, high 3-ketopristanoyl-CoA thiolase activity of the SCPx protein (Wanders et al 1997), and the expression pattern that correlates with lipid uptake of cells and thus phytanic acid exposition (Ossendorp et al 1991;Seedorf and Assmann 1991;Yamamoto et al 1991;Hirai et al 1994;McLean et al 1995).…”

Defective peroxisomal catabolism of branched fatty acyl coenzyme A in mice lacking the sterol carrier protein-2/sterol carrier protein-x gene function

“…Thus, the Scp2 gene is somewhat reminiscent of a bacterial operon, in which distinct functions that act in the same metabolic pathway are combined in a common transcriptional unit. This role is consistent with its genetic organization, the well-established peroxisomal localization of SCP2 and SCPx (Keller et al 1989;Ossendorp and Wirtz 1993), the ability of SCP2 to bind phytanoyl-CoA in vitro, high 3-ketopristanoyl-CoA thiolase activity of the SCPx protein (Wanders et al 1997), and the expression pattern that correlates with lipid uptake of cells and thus phytanic acid exposition (Ossendorp et al 1991;Seedorf and Assmann 1991;Yamamoto et al 1991;Hirai et al 1994;McLean et al 1995).…”

Further Characterization of the Peroxisomal 3‐Hydroxyacyl‐Coa Dehydrogenases from Rat Liver

“…Subsequent cloning of the porcine enzyme, and of its human homologue [26], revealed that both enzymes possess a multidomain structure. As has been shown for the porcine estradiol 17P-dehydrogenase [25,271, MFP-2 can be subdivided in three domains: (a) an N-terminal domain (amino acids 1-254) that is similar to the two short-chain alcohol dehydrogenase domains [28], located Nterminally and centrally, of the peroxisomal multifunctional Poxidation protein from Saccharomyces cerevisiae [9] and Candida tropicalis [29], and that harbours the estradiol 17P-dehydrogenase and 3-hydroxyacyl-CoA dehydrogenase (see further) activities; (b) a central domain (amino acids 336-603) similar to the C-terminal domain of the yeast multifunctional protein and that presumably displays the 2-enoyl-CoA hydratase activity; and (c) a C-terminal domain that is similar to sterol carrier protein-2, a protein supposedly involved in intracellular cholesterol transport [30]. In view of our findings, the presence of the 3-hydroxyacyl-CoA dehydrogenase and 2-enoyl-CoA hydratase domains is now readily explained, while the sterol carrier protein-2 domain might be involved in substrate binding.…”

Association of insulin-degrading enzyme with a 70 kDa cytosolic protein in hepatoma cells

“…Since both biochemical ( [5] ; this study) and morphological evaluations [6,7] of the subcellular distribution of IDE revealed a genuine cytosolic location for the peroxisomal protease, it is likely that IDE functions not only in peroxisomes. A dual cytosolic and peroxisomal location has also been observed for sterol carrier protein-2, another protein that possesses the peroxisomal targeting signal -AKL at its C-terminus, and the cytosolic location has been implicated in the functioning of this transport protein [23]. Also, a member of the epoxide hydrolase family having a putative type-I PTS (SKI) exists in both cytosolic and peroxisomal locations [24].…”

Defective peroxisomal catabolism of branched fatty acyl coenzyme A in mice lacking the sterol carrier protein-2/sterol carrier protein-x gene function

“…Thus, the Scp2 gene is somewhat reminiscent of a bacterial operon, in which distinct functions that act in the same metabolic pathway are combined in a common transcriptional unit. This role is consistent with its genetic organization, the well-established peroxisomal localization of SCP2 and SCPx (Keller et al 1989;Ossendorp and Wirtz 1993), the ability of SCP2 to bind phytanoyl-CoA in vitro, high 3-ketopristanoyl-CoA thiolase activity of the SCPx protein (Wanders et al 1997), and the expression pattern that correlates with lipid uptake of cells and thus phytanic acid exposition (Ossendorp et al 1991;Seedorf and Assmann 1991;Yamamoto et al 1991;Hirai et al 1994;McLean et al 1995).…”

Further Characterization of the Peroxisomal 3‐Hydroxyacyl‐Coa Dehydrogenases from Rat Liver

“…Subsequent cloning of the porcine enzyme, and of its human homologue [26], revealed that both enzymes possess a multidomain structure. As has been shown for the porcine estradiol 17P-dehydrogenase [25,271, MFP-2 can be subdivided in three domains: (a) an N-terminal domain (amino acids 1-254) that is similar to the two short-chain alcohol dehydrogenase domains [28], located Nterminally and centrally, of the peroxisomal multifunctional Poxidation protein from Saccharomyces cerevisiae [9] and Candida tropicalis [29], and that harbours the estradiol 17P-dehydrogenase and 3-hydroxyacyl-CoA dehydrogenase (see further) activities; (b) a central domain (amino acids 336-603) similar to the C-terminal domain of the yeast multifunctional protein and that presumably displays the 2-enoyl-CoA hydratase activity; and (c) a C-terminal domain that is similar to sterol carrier protein-2, a protein supposedly involved in intracellular cholesterol transport [30]. In view of our findings, the presence of the 3-hydroxyacyl-CoA dehydrogenase and 2-enoyl-CoA hydratase domains is now readily explained, while the sterol carrier protein-2 domain might be involved in substrate binding.…”

Association of insulin-degrading enzyme with a 70 kDa cytosolic protein in hepatoma cells

“…Since both biochemical ( [5] ; this study) and morphological evaluations [6,7] of the subcellular distribution of IDE revealed a genuine cytosolic location for the peroxisomal protease, it is likely that IDE functions not only in peroxisomes. A dual cytosolic and peroxisomal location has also been observed for sterol carrier protein-2, another protein that possesses the peroxisomal targeting signal -AKL at its C-terminus, and the cytosolic location has been implicated in the functioning of this transport protein [23]. Also, a member of the epoxide hydrolase family having a putative type-I PTS (SKI) exists in both cytosolic and peroxisomal locations [24].…”

Defective peroxisomal catabolism of branched fatty acyl coenzyme A in mice lacking the sterol carrier protein-2/sterol carrier protein-x gene function

“…Thus, the Scp2 gene is somewhat reminiscent of a bacterial operon, in which distinct functions that act in the same metabolic pathway are combined in a common transcriptional unit. This role is consistent with its genetic organization, the well-established peroxisomal localization of SCP2 and SCPx (Keller et al 1989;Ossendorp and Wirtz 1993), the ability of SCP2 to bind phytanoyl-CoA in vitro, high 3-ketopristanoyl-CoA thiolase activity of the SCPx protein (Wanders et al 1997), and the expression pattern that correlates with lipid uptake of cells and thus phytanic acid exposition (Ossendorp et al 1991;Seedorf and Assmann 1991;Yamamoto et al 1991;Hirai et al 1994;McLean et al 1995).…”

Further Characterization of the Peroxisomal 3‐Hydroxyacyl‐Coa Dehydrogenases from Rat Liver

“…Subsequent cloning of the porcine enzyme, and of its human homologue [26], revealed that both enzymes possess a multidomain structure. As has been shown for the porcine estradiol 17P-dehydrogenase [25,271, MFP-2 can be subdivided in three domains: (a) an N-terminal domain (amino acids 1-254) that is similar to the two short-chain alcohol dehydrogenase domains [28], located Nterminally and centrally, of the peroxisomal multifunctional Poxidation protein from Saccharomyces cerevisiae [9] and Candida tropicalis [29], and that harbours the estradiol 17P-dehydrogenase and 3-hydroxyacyl-CoA dehydrogenase (see further) activities; (b) a central domain (amino acids 336-603) similar to the C-terminal domain of the yeast multifunctional protein and that presumably displays the 2-enoyl-CoA hydratase activity; and (c) a C-terminal domain that is similar to sterol carrier protein-2, a protein supposedly involved in intracellular cholesterol transport [30]. In view of our findings, the presence of the 3-hydroxyacyl-CoA dehydrogenase and 2-enoyl-CoA hydratase domains is now readily explained, while the sterol carrier protein-2 domain might be involved in substrate binding.…”

Association of insulin-degrading enzyme with a 70 kDa cytosolic protein in hepatoma cells

“…Since both biochemical ( [5] ; this study) and morphological evaluations [6,7] of the subcellular distribution of IDE revealed a genuine cytosolic location for the peroxisomal protease, it is likely that IDE functions not only in peroxisomes. A dual cytosolic and peroxisomal location has also been observed for sterol carrier protein-2, another protein that possesses the peroxisomal targeting signal -AKL at its C-terminus, and the cytosolic location has been implicated in the functioning of this transport protein [23]. Also, a member of the epoxide hydrolase family having a putative type-I PTS (SKI) exists in both cytosolic and peroxisomal locations [24].…”