Different types of peroxisomes in human duodenal epithelium.

Roels, Frank; Espeel, Marc; Pauwels, Marina; Craemer, Dirk De; Egberts, H. J. A.; Spek, Peter van der

doi:10.1136/gut.32.8.858

Cited by 55 publications

(28 citation statements)

References 49 publications

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“…Elongation of peroxisomes -a prerequisite for division Elongated, tubular peroxisomes have been described in several mammalian tissues and cell lines, but their exact function remained unclear (Hicks and Fahimi, 1977;Gorgas, 1984;Yamamoto and Fahimi, 1987;Roels et al, 1991). Since tubular peroxisomes were frequently observed under conditions of rapid cellular growth (Yamamoto and Fahimi, 1987) or after stimulation of cultured cells with growth factors, fatty acids or free radicals (Schrader et al, 1998a;Schrader et al, 1999), they have been proposed to contribute to peroxisome proliferation.…”

Section: Discussionmentioning

confidence: 99%

Peroxisome elongation and constriction but not fission can occur independently of dynamin-like protein 1

Koch

Schneider

Lüers

et al. 2004

Journal of Cell Science

136

132

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The mammalian dynamin-like protein DLP1 belongs to the dynamin family of large GTPases, which have been implicated in tubulation and fission events of cellular membranes. We have previously shown that the expression of a dominant-negative DLP1 mutant deficient in GTP hydrolysis (K38A) inhibited peroxisomal division in mammalian cells. In this study, we conducted RNA interference experiments to `knock down' the expression of DLP1 in COS-7 cells stably expressing a GFP construct bearing the C-terminal peroxisomal targeting signal 1. The peroxisomes in DLP1-silenced cells were highly elongated with a segmented morphology. Ultrastructural and quantitative studies confirmed that the tubular peroxisomes induced by DLP1-silencing retained the ability to constrict their membranes but were not able to divide into spherical organelles. Co-transfection of DLP1 siRNA with Pex11pβ, a peroxisomal membrane protein involved in peroxisome proliferation, induced further elongation and network formation of the peroxisomal compartment. Time-lapse microscopy of living cells silenced for DLP1 revealed that the elongated peroxisomes moved in a microtubule-dependent manner and emanated tubular projections. DLP1-silencing in COS-7 cells also resulted in a pronounced elongation of mitochondria, and in more dispersed, elongated Golgi structures, whereas morphological changes of the rER, lysosomes and the cytoskeleton were not detected. These observations clearly demonstrate that DLP1 acts on multiple membranous organelles. They further indicate that peroxisomal elongation, constriction and fission require distinct sets of proteins, and that the dynamin-like protein DLP1 functions primarily in the latter process.

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Section: Discussionmentioning

confidence: 99%

Peroxisome elongation and constriction but not fission can occur independently of dynamin-like protein 1

Koch

Schneider

Lüers

et al. 2004

Journal of Cell Science

136

132

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“…In the stereological analysis of peroxisomes in intes tinal epithelium of patients with Zellweger's syndrome and neonatal-onset adrenoleukodystrophy by Black and Cornacchia [11], the presence of tubular forms is obvious in chil dren. Roels et al [28] performed a detailed morphometric study of the two peroxisomal populations in human adult intestine. Elon gated peroxisomes coexist with larger oval forms in epithelial cells of human fetal [18] and adult [29] kidney.…”

Section: Discussionmentioning

confidence: 99%

Peroxisomes and Peroxisomal Enzymes in the Human Fetal Small Intestine

Dauça

Cablé²,

Calvert³

et al. 1996

Neonatology

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The appearance and development of peroxisomes and the expression of their enzymes in the human fetal intestine have been investigated between 11 and 22 weeks of gestation. In the youngest samples (11-16 weeks of age), cytochemistry at the ultrastructural level revealed the presence of rare, mostly circular peroxisomes. From 16 weeks of gestation onwards, an increase was noted in the number of peroxisomes. Two peroxisomal types were distinguished: round to oval forms and elongated and/or tailed organelles. Biochemical assays revealed that total and specific intestinal catalase activities increased gradually between 11 and 20 weeks of gestation. The activity of fatty acyl-CoA oxidase, the first enzyme of the peroxisomal β-oxidation system, was detectable as early as 11 weeks of gestation. Thereafter, total and specific activities of the enzyme increased steadily. Activities of other peroxisomal oxidases (D-amino acid oxidase, L-α-hydroxyacid oxidase) appeared more slowly in the fetal intestine during the period studied. This investigation establishes the presence and the morphological changes that occur in intestinal peroxisomes during human fetal development as well as the developmental patterns of associated enzymes.

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“…In human and rat liver, the organelles have more or less a spherical shape; the matrix is finely granular (Sternlieb and Quintana, 1977;Wedel and Berger, 1975). Slender, vermiform peroxisomes cooccurring with spherical organelles are present in human duodenal epithelium (Roels et al, 1991a). Elongated peroxisomes are also common in the proximal tubules of human kidney (Roels and Goldfischer, 1979).…”

Section: Introductionmentioning

confidence: 99%