Rat intestinal alkaline phosphatase II messenger RNA is present in duodenal crypt and villus cells

Xie, Qing; Zhang, Y; Mahmood, Safrun; Alpers, D. H.

doi:10.1053/gast.1997.v112.pm9024291

Cited by 20 publications

(15 citation statements)

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“…The reaction produces a red product as the indication of IAP activity. As expected (20,62), extensive IAP activity was observed along the brush-border membrane of duodenal epithelium in control mice (Fig. 5C).…”

Section: E G and I)supporting

confidence: 81%

“…5, C and D). In support of this finding, the spatial expression pattern of IAP in the rat intestine correlated with that of Pdx1, in that the highest expression levels are found in the duodenum, especially in the duodenal villi and crypts (20,62) (Figs. 1 and 2A).…”

Section: Discussionsupporting

confidence: 58%

“…IAP is associated with the brush-border membrane of intestinal epithelial cells (20,62); it is thought to transport dietary lipids as a component of the surfactant-like particles that surround the neutral fat droplets in the villous enterocytes during fat absorption (32,33,64). Moreover, fatty meals increase the levels of IAP in serum and lymph (15,35).…”

Section: Discussionmentioning

confidence: 99%

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Pdx1inactivation restricted to the intestinal epithelium in mice alters duodenal gene expression in enterocytes and enteroendocrine cells

Chen

Fang²,

Davis

et al. 2009

American Journal of Physiology-Gastrointestinal and Liver Physi

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Null mutant mice lacking the transcription factor pancreatic and duodenal homeobox 1 (Pdx1) are apancreatic and survive only a few days after birth. The role of Pdx1 in regulating intestinal gene expression has therefore yet to be determined in viable mice with normal pancreatic development. We hypothesized that conditional inactivation of Pdx1 restricted to the intestinal epithelium would alter intestinal gene expression and cell differentiation. Pdx1 flox/flox; VilCre mice with intestine-specific Pdx1 inactivation were generated by crossing a transgenic mouse strain expressing Cre recombinase, driven by a mouse villin 1 gene promoter fragment, with a mutant mouse strain homozygous for loxP site-flanked Pdx1. Pdx1 protein is undetectable in all epithelial cells in the intestinal epithelium of Pdx1 flox/flox; VilCre mice. Goblet cell number and mRNA abundance for mucin 3 and mucin 13 genes in the proximal small intestine are comparable between Pdx1 flox/flox; VilCre and control mice. Similarly, Paneth cell number and expression of Paneth cell-related genes Defa1, Defcr-rs1, and Mmp7 in the proximal small intestine remain statistically unchanged by Pdx1 inactivation. Although the number of enteroendocrine cells expressing chromogranin A/B, gastric inhibitory polypeptide (Gip), or somatostatin (Sst) is unaffected in the Pdx1 flox/flox; VilCre mice, mRNA abundance for Gip and Sst is significantly reduced in the proximal small intestine. Conditional Pdx1 inactivation attenuates intestinal alkaline phosphatase (IAP) activity in the duodenal epithelium, consistent with an average 91% decrease in expression of the mouse enterocyte IAP gene, alkaline phosphatase 3 (a novel Pdx1 target candidate), in the proximal small intestine following Pdx1 inactivation. We conclude that Pdx1 is necessary for patterning appropriate gene expression in enterocytes and enteroendocrine cells of the proximal small intestine.

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Section: E G and I)supporting

confidence: 81%

Section: Discussionsupporting

confidence: 58%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Pdx1inactivation restricted to the intestinal epithelium in mice alters duodenal gene expression in enterocytes and enteroendocrine cells

Chen

Fang²,

Davis

et al. 2009

American Journal of Physiology-Gastrointestinal and Liver Physi

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“…It was reported that the larger mRNA transcript, rIAP-2, exists in the proximal intestine (34). In the proximal intestine, both rIAP-1 and rIAP-2 isozymes are expressed, while only the rIAP-1 isozyme is expressed in the distal part of the intestine (35,36). However, the physiological functions of the two isozymes have not been clarified.…”

Section: Discussionmentioning

confidence: 99%

Enhancement Effects of Vitamin K1 (Phylloquinone) or Vitamin K2 (Menaquinone-4) on Intestinal Alkaline Phosphatase Activity in Rats

Sogabe

Maruyama

Hosoi

et al. 2007

J Nutr Sci Vitaminol

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Summary Alkaline phosphatase (ALP) hydrolyzes a variety of monophosphate esters into inorganic phosphoric acid and alcohol at a high optimal pH, and is thought to play an important role in phosphate metabolism. Intestinal ALP, located at the brush border of intestinal epithelial cells, is known to be affected by several kinds of nutrients, but little is known about the physiological function of intestinal ALP. Vitamin K is an essential cofactor for the post-translational carboxylation of glutamate residues into gamma-carboxy glutamate (Gla). Recently, novel functions of vitamin K have been clarified, but no data exist on the relation between vitamin K and intestinal ALP. The aim of this study was to examine the effects of both vitamin Ks (K 1 : phylloquinone, and K 2 : menaquinone) on ALP activity. Sprague-Dawley rats (6-wk-old) were divided into three groups: a control, phylloquinone (PK: 600 mg/kg diet), or menaquinone-4 (MK-4: 600 mg/kg diet) diet group. After 3 mo of feeding, we measured intestinal ALP activity by dividing it into five segments. In each segment, both PK and MK-4 increased intestinal ALP activity. The levels of intestinal ALP activity in the duodenum and proximal jejunum from the PK group were significantly higher than in the control group ( p Ͻ 0.05). Moreover, the levels of intestinal ALP activity from the proximal jejunum and distal ileum of the intestine in the MK group were significantly higher than in the control group ( p Ͻ 0.05). In this study, we clarified for the first time that both vitamin K 1 and K 2 as nutritional factors enhance intestinal ALP activity.

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“…SLP, which consist of PC and surfactant proteins A, B, and D, decrease the air-water interface tension. It has been demonstrated that the major IAP regulated by lipid feeding is IAP II (6,8,22,30). Additionally, it has been determined that the main source of lymphatic alkaline phosphatase is from cytosolic IAP, i.e., IAP II (19).…”

Section: Discussionmentioning

confidence: 99%

Intestinal alkaline phosphatase release is not associated with chylomicron formation

Nauli

Zheng

Yang

et al. 2003

American Journal of Physiology-Gastrointestinal and Liver Physi

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Intestinal alkaline phosphatase (IAP) is one of the major sources of alkaline phosphatase in circulation. It is secreted into the intestinal lumen, serum, and lymph. After the ingestion of lipid, lymphatic alkaline phosphatase secretion increases significantly. We have found that the nonabsorbable fat olestra is unable to stimulate lymphatic alkaline phosphatase secretion. We also found that the hydrophobic surfactant Pluronic L-81, which blocks chylomicron formation, fails to inhibit this increase in lymphatic alkaline phosphatase secretion. These results suggest that it is the lipid uptake into the mucosa and/or reesterification to form triacylglycerols, but not the formation of chylomicrons, that is necessary for the stimulation of the secretion of alkaline phosphatase into the lymph.

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Rat intestinal alkaline phosphatase II messenger RNA is present in duodenal crypt and villus cells

Cited by 20 publications

References 0 publications

Pdx1inactivation restricted to the intestinal epithelium in mice alters duodenal gene expression in enterocytes and enteroendocrine cells

Pdx1inactivation restricted to the intestinal epithelium in mice alters duodenal gene expression in enterocytes and enteroendocrine cells

Enhancement Effects of Vitamin K1 (Phylloquinone) or Vitamin K2 (Menaquinone-4) on Intestinal Alkaline Phosphatase Activity in Rats

Intestinal alkaline phosphatase release is not associated with chylomicron formation

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