Caseinphosphopeptide-induced calcium uptake in human intestinal cell lines HT-29 and Caco2 is correlated to cellular differentiation☆

Cosentino, S.; Gravaghi, Claudia; Donetti, Elena; Donida, B.M.; Lombardi, Giovanni; Bedoni, Marzia; Fiorilli, Amelia; Tettamanti, Guido; Ferraretto, Anita

doi:10.1016/j.jnutbio.2008.12.016

Cited by 59 publications

(40 citation statements)

References 54 publications

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“…The bioactivity of Calcium-CPPs, as well as of decalcified CPPs, was determined by directly measuring the [Ca 2þ ] i changes in HT-29 cells differentiated in culture before and after CPP administration, as previously described (Cosentino et al, 2010;Ferraretto et al, 2001). First of all, we analyzed the calcium-CPP bioactivity in a calcium-free KRH.…”

Section: Resultsmentioning

confidence: 99%

“…However, data published to date are inconclusive and sometimes controversial, due to different composition of the CPPs used (Ferraretto, Gravaghi, Fiorilli, & Tettamanti, 2003;Mora-Gutierrez, Farrell, Attaie, Mc Whinney, & Wang, 2007), to the experimental models used (animal or human) and the use of different CPPs sources (milk, calcium fortified milk, CPP endogenously present in milk, CPPs added to milk) or of different calcium sources (CaCO 3 , Ca-lactate) (Bennet et al, 2000;Heaney, Saito, & Orimo, 1994;Kopra, Scholz-Ahrens, & Barth, 1992;Lopez-Huertas et al, 2006;Narva, Kärkkäinen, Poussa, Lamberg-Allardt, & Korpela, 2003;Teucher et al, 2006;Tsuchita, Suzuki, & Kuwata, 2001). A better understanding of the relationships between intestinal calcium uptake and calciumeCPP interactions was provided by the observations that in cell models of the human intestine (HT-29 and Caco2 cells differentiated toward an intestinal phenotype) CPPs, a commercial preparation as well as single purified CPP, were able to promote calcium uptake (Cosentino et al, 2010;Ferraretto et al, 2003;Ferraretto, Signorile, Gravaghi, Fiorilli, & Tettamanti, 2001). A second relevant observation was that CPP-calcium aggregates, analogous to the ones formed by casein in milk (Holt, 1992;Rollema, 1992), constitute the form of CPPs needed for the calcium uptake effects (Gravaghi et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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Calcium ions enclosed in casein phosphopeptide aggregates are directly involved in the mineral uptake by differentiated HT-29 cells

Cosentino

Donida

Marasco

et al. 2010

International Dairy Journal

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Calcium ions enclosed in casein phosphopeptide aggregates are directly involved in the mineral uptake by differentiated HT-29 cells

Cosentino

Donida

Marasco

et al. 2010

International Dairy Journal

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“…The Caco-2 cell layer again serves here as a model for the intestinal barrier through which calcium transport will take place. 35 The…”

Section: Future: Nutrikinetic Studiesmentioning

confidence: 99%

NutriChip: nutrition analysis meets microfluidics

et al. 2013

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This focus article introduces the concept of NutriChip, an integrated microfluidic platform for investigating the potential of the immuno-modulatory function of dairy food. The core component of the NutriChip is a miniaturized artificial human gastrointestinal tract (GIT), which consists of a confluent layer of epithelial cells separated from a co-culture of immune cells by a permeable membrane. This setting creates conditions mimicking the human GIT and allows studying processes that characterize the passage of nutrients though the human GIT, including the activation of immune cells in response to the transfer of nutrients across the epithelial layer. The NutriChip project started by developing a biologically active in vitro cellular system in a commercial Transwell co-culture system. This Transwell system serves as a reference for the micro-scale device which is being developed. The microfluidic setup of NutriChip allows monitoring of the response of immune cells to pro-inflammatory stimuli, such as lipid polysaccharide (LPS), and to the application of potentially anti-inflammatory dairy food. This differential response will be quantified by measuring the variation in expression of pro-inflammatory cytokines, including interleukin 1 (IL-1) and interleukin 6 (IL-6), secreted by the immune cells, and this is achieved by using a dedicated optical imager. A series of dairy products will be screened for their anti-inflammatory properties using the NutriChip system and, finally, the outcome of the NutriChip will be validated by a human nutrition trial.Therefore, the NutriChip platform offers a new option to evaluate the influence of food quality on health, by monitoring the expression of relevant immune cell biomarkers.

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“…HT-29 cells were differentiated by reducing glucose levels through changing media to RPMI 1640, and Caco-2 cells underwent spontaneous differentiation, according to a previous report (28). During differentiation, the media were changed once a day.…”

Section: Experimental and Proceduresmentioning

confidence: 99%

Core2 O-Glycan Structure Is Essential for the Cell Surface Expression of Sucrase Isomaltase and Dipeptidyl Peptidase-IV during Intestinal Cell Differentiation

Lee

Nakayama

et al. 2010

Journal of Biological Chemistry

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Alterations in glycosylation play an important role during intestinal cell differentiation. Here, we compared expression of mucin-type O-glycan synthases from proliferating and differentiated HT-29 and Caco-2 cells. Mucin-type O-glycan structures were analyzed at both stages by mass spectrometry. Core2 ␤1,6-N-acetylglucosaminyltransferase-2 (C2GnT-2) was markedly increased in differentiated HT-29 and Caco-2 cells, but the core3 structure was hardly detectable. To determine whether such differential expression of mucin-type O-glycan structures has physiological significance in intestinal cell differentiation, expression of sucrase isomaltase (SI) and dipeptidylpeptidase IV (DPP-IV), two well known intestinal differentiation markers, was examined. Interestingly, the fully glycosylated mature form of SI was decreased in C2GnT-2 knock-out mice but not in core2 N-acetylglucosaminyltransferase-3 (C2GnT-3) nulls. In addition, expression of SI and DPP-IV was dramatically reduced in C2GnT-1-3 triple knock-out mice. These patterns were confirmed by RNAi analysis; C2GnT-2 knockdown significantly reduced cell surface expression of SI and DPP-IV in Caco-2 cells. Similarly, overexpression of the core3 structure in HT-29 cells attenuated cell surface expression of both enzymes. These findings indicate that core3 O-glycan structure regulates cell surface expression of SI and DPP-IV and that core2 O-glycan is presumably an essential mucin-type O-glycan structure found in both molecules in vivo. Finally, goblet cells in the upper part of the crypt showed impaired maturation in the core2 O-glycan-deficient mice. These studies are the first to clearly identify functional mucin-type O-glycan structures modulating cell surface expression of SI and DPP-IV during the intestinal cell differentiation.

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Caseinphosphopeptide-induced calcium uptake in human intestinal cell lines HT-29 and Caco2 is correlated to cellular differentiation☆

Cited by 59 publications

References 54 publications

Calcium ions enclosed in casein phosphopeptide aggregates are directly involved in the mineral uptake by differentiated HT-29 cells

Calcium ions enclosed in casein phosphopeptide aggregates are directly involved in the mineral uptake by differentiated HT-29 cells

NutriChip: nutrition analysis meets microfluidics

Core2 O-Glycan Structure Is Essential for the Cell Surface Expression of Sucrase Isomaltase and Dipeptidyl Peptidase-IV during Intestinal Cell Differentiation

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