Induction of heme oxygenase in intestinal epithelial cells: studies in Caco-2 cell cultures

Cable, Julia W.; Cable, Edward Earl; Bonkovsky, Herbert L.

doi:10.1007/bf00926580

Cited by 28 publications

(25 citation statements)

References 37 publications

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“…The HO-1 is present in many tissues, including the intestine, with the highest levels observed in the duodenum (4). HO-1 activity can be increased 10-to 100fold by various conditions, including hyperthermia, heme, and heavy metals such as cobalt and cadmium (36,37). It was suggested that increased HO-1 activity and expression might be responsible for the increased heme iron absorption and a rapid export of heme iron (38,39).…”

Section: Discussionmentioning

confidence: 98%

Bioactive Dietary Polyphenols Decrease Heme Iron Absorption by Decreasing Basolateral Iron Release in Human Intestinal Caco-2 Cells

Kim

Han

2010

The Journal of Nutrition

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Because dietary polyphenolic compounds have a wide range of effects in vivo and vitro, including chelation of metals such as iron, it is prudent to test whether the regular consumption of dietary bioactive polyphenols impair the utilization of dietary iron. Because our previous study showed the inhibitory effect of (-) -epigallocatechin-3-gallate (EGCG) and grape seed extract (GSE) on nonheme iron absorption, we investigated whether EGCG and GSE also affect iron absorption from heme. The fully differentiated intestinal Caco-2 cells grown on microporous membrane inserts were incubated with heme (55)Fe in uptake buffer containing EGCG or GSE in the apical compartment for 7 h. Both EGCG and GSE decreased (P < 0.05) transepithelial transport of heme-derived iron. However, apical heme iron uptake was increased (P < 0.05) by GSE. Despite the increased cellular levels of heme (55)Fe, the transfer of iron across the intestinal basolateral membrane was extremely low, indicating that basolateral export was impaired by GSE. In contrast, EGCG moderately decreased the cellular assimilation of heme (55)Fe, but the basolateral iron transfer was extremely low, suggesting that the basolateral efflux of heme iron was also inhibited by EGCG. Expression of heme oxygenase, ferroportin, and hephaestin protein was not changed by EGCG and GSE. The apical uptake of heme iron was temperature dependent and saturable in fully differentiated Caco-2 cells. Our data show that bioactive dietary polyphenols inhibit heme iron absorption mainly by reducing basolateral iron exit rather than decreasing apical heme iron uptake in intestinal cells.

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Section: Discussionmentioning

confidence: 98%

Bioactive Dietary Polyphenols Decrease Heme Iron Absorption by Decreasing Basolateral Iron Release in Human Intestinal Caco-2 Cells

Kim

Han

2010

The Journal of Nutrition

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“…Because the majority of dietary iron is not bioavailable, two-thirds of iron absorbed through intestines is in the heme form (7). After its absorption as an intact molecule, heme is degraded by the intestinal epithelial cell HO-1 to biliverdin, CO, and Fe 2ϩ (38,45); biliverdin is then converted to bilirubin by biliverdin reductase (6). It is not known if heme acquired by intestinal epithelial cells can influence fluid and electrolyte transport by inducing cGMP directly or via its metabolite CO.…”

mentioning

confidence: 99%

Hemin induces active chloride secretion in Caco-2 cells

Uç

Husted

Giriyappa

et al. 2005

American Journal of Physiology-Gastrointestinal and Liver Physi

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Enterocytes maintain fluid-electrolyte homeostasis by keeping a tight barrier and regulating ion channels. Carbon monoxide (CO), a product of heme degradation, modulates electrolyte transport in kidney and lung epithelium, but its role in regulating intestinal fluid-electrolyte homeostasis has not been studied. The major source of endogenous CO formation comes from the degradation of heme via heme oxygenase. We hypothesized that heme activates electrolyte transport in intestinal epithelial cells. Basolateral hemin treatment increased baseline Caco-2 cell short-circuit currents ( Isc) twofold (control = 1.96 ± 0.14 μA/cm2 vs. hemin = 4.07 ± 0.16 μA/cm2, P < 0.01); apical hemin had no effect. Hemin-induced Isc was caused by Cl− secretion because it was inhibited in Cl−-free medium, with ouabain, 5-nitro-2-(3-phenylpropylamino) benzoic acid (NPPB), or DIDS. Apical electrogenic Na+ channel inhibitor benzamil had no effect on hemin-induced Isc. Hemin did not alter the ability of Caco-2 cells to respond maximally to forskolin, but a soluble guanylate cyclase inhibitor, [1,2,4]oxadiazolo-[4,3-a]quinoxalin-1-one (ODQ) inhibited the effects of hemin. A CO-releasing molecule, tricarbonyldichlororuthenium II, induced active Cl− secretion that was also inhibited with ODQ. We conclude that hemin induces active Cl− secretion in Caco-2 cells via a cGMP-dependent pathway. These effects are probably the consequence of CO formation. Heme and CO may be important regulators of intestinal fluid-electrolyte homeostasis.

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“…Parameters such as ionisation and molecular size largely determine intestinal absorption (Ferruzzi, Failla, & Schwartz, 2001). Another possibility is that it may have been partially metabolised within the cell, since activities such as that of haem oxygenase and biliverdin reductase have been reported in Caco-2 cells (Cable, Cable, & Bonkovsky, 1993).…”

Section: Uptake Of Nccs By Intestinal Epithelial Cellsmentioning

confidence: 99%

In vitro digestive stability and uptake by Caco-2 human intestinal cells of nonfluorescent chlorophyll catabolites

Roca

2012

Food Chemistry

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Induction of heme oxygenase in intestinal epithelial cells: studies in Caco-2 cell cultures

Cited by 28 publications

References 37 publications

Bioactive Dietary Polyphenols Decrease Heme Iron Absorption by Decreasing Basolateral Iron Release in Human Intestinal Caco-2 Cells

Bioactive Dietary Polyphenols Decrease Heme Iron Absorption by Decreasing Basolateral Iron Release in Human Intestinal Caco-2 Cells

Hemin induces active chloride secretion in Caco-2 cells

In vitro digestive stability and uptake by Caco-2 human intestinal cells of nonfluorescent chlorophyll catabolites

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