Developmental aspects of lipid and lipoprotein synthesis and secretion in human gut

Lévy, Émile; Ménard, Daniel

doi:10.1002/(sici)1097-0029(20000515)49:4<363::aid-jemt5>3.0.co;2-2

Cited by 29 publications

(13 citation statements)

References 64 publications

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“…As MTP large subunit is a critical factor for chylomicron and VLDL formation, the tissue specificity of its gene expression during development and in adults could be correlated with the synthesis and secretion of apoB‐containing lipoproteins (Raabe et al,1998,1999; Hussain et al,2003). This lipoprotein synthesis has been demonstrated in mammalian liver, fetal and adult small intestine (Sabesin and Frase,1977; Green and Glickman,1981; Lin et al,1994; Levy and Menard,2000; Levy et al,2001), and heart (Nielsen et al,1998). Similarly, mtp high expression observed in zebrafish anterior intestine and liver could be associated with an intense lipoprotein particles synthesis and transfer in these fish tissues (Iwai,1969; Gauthier and Landis,1972; Noaillac‐Depeyre and Gas,1974,1976; Sire et al,1981; Rombout et al,1984; Wallaert and Babin,1992; André et al,2000).…”

Section: Discussionmentioning

confidence: 84%

Developmental expression and nutritional regulation of a zebrafish gene homologous to mammalian microsomal triglyceride transfer protein large subunit

Marza¹,

Barthe²,

André³

et al. 2004

Developmental Dynamics

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The microsomal triglyceride transfer protein (MTP) large subunit is required for the assembly and secretion of apolipoprotein B-containing lipoproteins. We have found a zebrafish mtp homologous gene coding a protein with 54% identity with human MTP large subunit with the most conserved regions distributed in the corresponding predicted ␣-helical and C-and A-sheet domains. In situ hybridizations showed that zebrafish mtp transcripts were distributed in the yolk syncytial layer during early embryogenesis and in anterior intestine and liver from 48 hr postfertilization onward. Real-time quantitative RT-PCR confirmed the developmental regulation and tissue-specificity of mtp expression. A significant pretranslational up-regulation of mtp expression was observed in the anterior intestine after feeding. The nutritional regulation of zebrafish mtp expression observed in the anterior intestine supports the notion that this protein, similar to mammalian MTP large subunit, could be a factor implicated directly or indirectly in large lipid droplets accumulation observed in the fish enterocyte after feeding.

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Section: Discussionmentioning

confidence: 84%

Developmental expression and nutritional regulation of a zebrafish gene homologous to mammalian microsomal triglyceride transfer protein large subunit

Marza¹,

Barthe²,

André³

et al. 2004

Developmental Dynamics

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“…Differentiated epithelial cells of the small intestine share several metabolic characteristics with the mature hepatocyte. Fat absorption, transport, and lipid metabolism take place in enterocytes (28,29,37). These cells are crucial contributors to apolipoprotein component synthesis as well as chylomicrons, very low density sized particles, and high-density lipoproteins (28,47).…”

Section: Discussionmentioning

confidence: 99%

“…absorption, and transport (42) as well as lipid metabolism (29,42). Differential molecular mechanisms along both the vertical and horizontal axes of the intestine account for the tight control of these intestinal epithelial cell functions.…”

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confidence: 99%

Hepatocyte nuclear factor 4α contributes to an intestinal epithelial phenotype in vitro and plays a partial role in mouse intestinal epithelium differentiation

Babeu

Darsigny²,

Lussier³

et al. 2009

American Journal of Physiology-Gastrointestinal and Liver Physi

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Hepatocyte nuclear factor 4alpha (HNF4alpha) is a regulator of hepatocyte and pancreatic transcription. Hnf4alpha deletion in the mouse is embryonically lethal with severe defects in visceral endoderm formation. It has been concluded in the past that the role of Hnf4alpha in the developing colon was much less important than in the liver. However, the precise role of Hnf4alpha in the homeostasis of the small intestinal epithelium remains unclear. Our aim was to evaluate the potential of Hnf4alpha to support an intestinal epithelial phenotype. First, Hnf4alpha potential to dictate this phenotype was assessed in nonintestinal cell lines in vitro. Forced expression of Hnf4alpha in fibroblasts showed an induction of features normally restricted to epithelial cells. Combinatory expression of Hnf4alpha with specific transcriptional regulators of the intestine resulted in the induction of intestinal epithelial genes in this context. Second, the importance of Hnf4alpha in maintaining the homeostasis of the intestinal epithelium was investigated in mice. Mice conditionally deficient for intestinal Hnf4alpha developed normally throughout adulthood with an epithelium displaying normal morphological and functional structures with minor alterations. Subtle but statistical differences were observed at the proliferation and the cytodifferentiation levels. Hnf4alpha mutant mice displayed an increase in the number of goblet and enteroendocrine cells compared with controls. Given the fundamental role of this transcription factor in other tissues, these findings dispute the crucial role for this regulator in the maintenance of intestinal epithelial cell function at a period of time that follows cytodifferentiation but may suggest a functional role in instructing cells to become specific to the intestinal epithelium.

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“…In particular, its epithelial cells, the enterocytes, are constantly challenged by the complex process of fat absorption (Davidson and Shelness 2000;Levy and Menard 2000;Phan and Tso 2001). Fatty acids (FAs) must cross the apical membrane and traverse the cytoplasm to reach the endoplasmic reticulum (ER) where most of the events related to chylomicron packaging take place.…”

Section: Introductionmentioning

confidence: 99%

Localization, function and regulation of the two intestinal fatty acid-binding protein types

Lévy

Ménard

Delvin

et al. 2009

Histochem Cell Biol

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Although intestinal (I) and liver (L) fatty acid binding proteins (FABP) have been widely studied, the physiological significance of the presence of the two FABP forms (I- and L-FABP) in absorptive cells remains unknown as do the differences related to their distribution along the crypt-villus axis, regional expression, ontogeny and regulation in the human intestine. Our morphological experiments supported the expression of I- and L-FABP as early as 13 weeks of gestation. Whereas cytoplasmic immunofluorescence staining of L-FABP was barely detectable in the lower half of the villus and in the crypt epithelial cells, I-FABP was visualized in epithelial cells of the crypt-villus axis in all intestinal segments until the adult period in which the staining was maximized in the upper part of the villus. Immunoelectron microscopy revealed more intense labeling of L-FABP compared with I-FABP, accompanied with a heterogeneous distribution in the cytoplasm, microvilli and basolateral membranes. By western blot analysis, I- and L-FABP at 15 weeks of gestation appeared predominant in jejunum compared with duodenum, ileum, proximal and distal colon. Exploration of the maturation aspect documented a rise in L-FABP in adult tissues. Permanent transfections of Caco-2 cells with I-FABP cDNA resulted in decreased lipid export, apolipoprotein (apo) biogenesis and chylomicron secretion. Additionally, supplementation of Caco-2 with insulin, hydrocortisone and epidermal growth factor differentially modulated the expression of I- and L-FABP, apo B-48 and microsomal triglyceride transfer protein (MTP), emphasizing that these key proteins do not exhibit a parallel modulation. Overall, our findings indicate that the two FABPs display differences in localization, regulation and developmental pattern.

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Developmental aspects of lipid and lipoprotein synthesis and secretion in human gut

Cited by 29 publications

References 64 publications

Developmental expression and nutritional regulation of a zebrafish gene homologous to mammalian microsomal triglyceride transfer protein large subunit

Developmental expression and nutritional regulation of a zebrafish gene homologous to mammalian microsomal triglyceride transfer protein large subunit

Hepatocyte nuclear factor 4α contributes to an intestinal epithelial phenotype in vitro and plays a partial role in mouse intestinal epithelium differentiation

Localization, function and regulation of the two intestinal fatty acid-binding protein types

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