Ovotransferrin Supplementation Improves the Iron Absorption: An In Vitro Gastro-Intestinal Model

doi:10.3390/biomedicines9111543

. 2021 Oct 26;9(11):1543.

doi: 10.3390/biomedicines9111543.

Ovotransferrin Supplementation Improves the Iron Absorption: An In Vitro Gastro-Intestinal Model

Rebecca Galla¹, Paride Grisenti², Mahitab Farghali¹, Laura Saccuman¹, Patrizia Ferraboschi³, Francesca Uberti¹

Affiliations

¹ Laboratory Physiology, Department of Translational Medicine, University of Eastern Piedmont, Via Solaroli 17, 28100 Novara, Italy.
² Bioseutica B.V., Landbouwweg 83, 3899 BD Zeewolde, The Netherlands.
³ Department of Medical Biotechnology and Translational Medicine, Università degli Studi di Milano, Via Saldini 50, 20133 Milan, Italy.

PMID: 34829772
PMCID: PMC8615417
DOI: 10.3390/biomedicines9111543

Ovotransferrin Supplementation Improves the Iron Absorption: An In Vitro Gastro-Intestinal Model

Rebecca Galla et al. Biomedicines. 2021.

. 2021 Oct 26;9(11):1543.

doi: 10.3390/biomedicines9111543.

Authors

Rebecca Galla¹, Paride Grisenti², Mahitab Farghali¹, Laura Saccuman¹, Patrizia Ferraboschi³, Francesca Uberti¹

Affiliations

¹ Laboratory Physiology, Department of Translational Medicine, University of Eastern Piedmont, Via Solaroli 17, 28100 Novara, Italy.
² Bioseutica B.V., Landbouwweg 83, 3899 BD Zeewolde, The Netherlands.
³ Department of Medical Biotechnology and Translational Medicine, Università degli Studi di Milano, Via Saldini 50, 20133 Milan, Italy.

PMID: 34829772
PMCID: PMC8615417
DOI: 10.3390/biomedicines9111543

Abstract

Transferrins constitute the most important iron regulation system in vertebrates and some invertebrates. Soluble transferrins, such as bovine lactoferrin and hen egg white ovotransferrin, are glycoproteins with a very similar structure with lobes that complex with iron. In this in vitro study, a comparison of bovine lactoferrin and ovotransferrin was undertaken to confirm the comparability of biological effects. An in vitro gastric barrier model using gastric epithelial cells GTL-16 and an in vitro intestinal barrier model using CaCo-2 cells was employed to evaluate iron absorption and barrier integrity. An analysis of the molecular pathways involving DMT-1 (divalent metal transporter 1), ferritin and ferroportin was also carried out. These in vitro data demonstrate the activity of both 15% saturated and 100% saturated ovotransferrin on the iron regulation system. Compared with the commercial bovine lactoferrin, both 15% saturated and 100% saturated ovotransferrin were found to act in a more physiological manner. Based on these data, it is possible to hypothesise that ovotransferrin may be an excellent candidate for iron supplementation in humans; in particular, 15% saturated ovotransferrin is the overall best performing product. In vivo studies should be performed to confirm this in vitro data.

Keywords: bovine lactoferrin; gastro-intestinal barrier; iron absorption; iron metabolism; iron transportation; ovotransferrin.

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Conflict of interest statement

The authors declare that they have no competing interests. F.U. and C.M. are co-founders of the Noivita Srls start-up at the University of Eastern Piedmont. P.G. is funded by BIOSEUTICA B.V. but had no role in the design of the study, analyses, or interpretation of data or in the decision to publish the results.

Figures

**Figure 1**
Dose-response study of cell viability on GTL-16 cells treated with different concentrations and different iron saturation types of OvT and bLact. Data are expressed as means ± SD compared to control (0% line) of four independent experiments produced in triplicate. (a) holo-OvT 100% saturated iron * p < 0.05 vs. control; ** p < 0.05 vs. holo-Ovt 100% 200 μg/mL; α p < 0.05 vs. holo-Ovt 100% 100 μg/mL; αα p < 0.05 vs. holo-Ovt 100% 50 μg/mL. (b) holo-OvT 15% saturated iron * p < 0.05 vs. control; β p < 0.05 vs. holo-Ovt 15% 200 μg/mL; γ p < 0.05 vs. holo-Ovt 15% 100 μg/mL. (c) bLact = bovine lactoferrin * p < 0.05 vs. control; δ p < 0.05 vs. bLact 200 μg/mL; (d) apo-Ovt * p < 0.05 vs. control; φ p < 0.05 vs. apo-Ovt 200 μg/mL.

**Figure 2**
Dose-response study of cell viability on Caco-2 cell treated with different concentrations and different iron saturation types of OvT and bLact. Data are expressed as means ± SD compared to control (0% line) of four independent experiments produced in triplicate. (a) holo-OvT 100% saturated iron. * p < 0.05 vs. control; ** p < 0.05 vs. holo-Ovt 100% 200 μg/mL; α p < 0.05 vs. holo-Ovt 100% 100 μg/mL. (b) holo-OvT 15% saturated iron * p < 0.05 vs. control; β p < 0.05 vs. holo-Ovt 15% 200 μg/mL; γ p < 0.05 vs. holo-Ovt 15% 100 μg/mL; γγ p < 0.05 vs. holo-Ovt 15% 50 μg/mL. (c) bLact = bovine lactoferrin * p < 0.05 vs. control; δ p < 0.05 vs. bLact 200 μg/mL; ε p < 0.05 vs. bLact 100 μg/mL; εε p < 0.05 vs. bLact 50 μg/mL. (d) apo-Ovt * p < 0.05 vs. control; φ p < 0.05 vs. apo-Ovt 200 μg/mL; κ p < 0.05 vs. apo-Ovt 100 μg/mL.

**Figure 3**
Time-course study of cell viability on GTL-16 cells treated with 50 and 30 μg/mL of OvT and bLact for 1, 2 and 3 h. (a) 1 h of stimulation * p < 0.05 vs. control; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; φ p < 0.05 vs. apo-Ovt 50 μg/mL. (b) 2 h of stimulation * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL. (c) 3 h of stimulation * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL; φ p < 0.05 vs. apo-Ovt 50 μg/mL. The abbreviations are the same reported in Figure 1. Data are expressed as means ± SD (%) compared to control (0% line) of four independent experiments produced in triplicate.

**Figure 4**
Time-course study of cell viability on Caco-2 cells treated with 50 and 30 μg/mL of OvT and bLact for 1, 3 and 6 h. (a) 1 h of stimulation * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL; φ p < 0.05 vs. apo-Ovt 50 μg/mL. (b) 3 h of stimulation * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL. (c) 6 h of stimulation * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL; φ p < 0.05 vs. apo-Ovt 50 μg/mL. The abbreviations are the same reported in Figure 1. Data are expressed as means ± SD (%) compared to control (0% line) of four independent experiments produced in triplicate.

**Figure 5**
Transferrin absorption measured at the basolateral level on Transwell^® over time. GTL-16 cells treated with 50 and 30 μg/mL of different holo-OvT and bLact. In (a) the measurement at 1 h * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL. (b) at 2 h * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL. (c) at 3 h of stimulation * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL. The abbreviations are the same as reported in Figure 1. Data are expressed as means ± SD (%) calculated on ng/mL compared to control (0% line) of four independent experiments produced in triplicate.

**Figure 6**
Transferrin absorption measured at the basolateral level on Transwell^® during time. Caco-2 cells treated with 50 and 30 μg/mL of different holo-OvT and bLact. In (a) the measurement at 1 h * p < 0.05 vs. control; δ p < 0.05 vs. bLact 50 μg/mL. In (b) at 3 h * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL. In (c) at 6 h of stimulation * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL. The abbreviations are the same as reported in Figure 1. Data are expressed as means ± SD (%) calculated on ng/mL compared to control (0% line) of four independent experiments produced in triplicate.

**Figure 7**
Transferrin absorption measured in a VITVO^® basolateral environment after Caco-2 cells. The stimulation includes 50 and 30 μg/mL of different holo-OvT and bLact. In (a) the measurement at 1 h * p < 0.05 vs. control; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL. In (b) at 3 h * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL. In (c) at 6 h of stimulation * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL. The abbreviations are the same as reported in Figure 1. Data are expressed as means ± SD (%) calculated on ng/mL compared to control (0% line) of four independent experiments produced in triplicate.

**Figure 8**
SOD activity measured on VITVO^® after Caco-2 cells. The stimulation includes 50 and 30 μg/mL of different holo-OvT and bLact. In (a) the measurement at 1 h * p < 0.05 vs. control; δ p < 0.05 vs. bLact 50 μg/mL. In (b) at 3 h * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL. In (c) at 6 h of stimulation * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL. The abbreviations are the same as reported in Figure 1. Data are expressed as means ± SD (%) calculated on U/mg compared to control (0% line) of four independent experiments produced in triplicate.

**Figure 9**
Western blot and densitometric analysis of DMT-1 on total lysates of GTL-16 (a) and Caco-2 cells (b) of the VITVO^® system. The cells were treated with 50 and 30 μg/mL of different OvT and bLact. The images shown are an example of each protein of four independent experiments reproduced in triplicate. The abbreviations are the same as reported in Figure 1. Data are expressed as means ± SD (%) of four independent experiments normalised and verified on β-actin detection. In (a) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL. In (b) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL.

**Figure 10**
Western blot and densitometric analysis of Ferritin on total lysates of GTL-16 (a) and Caco-2 cells (b) of the VITVO^® system. The cells were treated with 50 and 30 μg/mL of different OvT and bLact. The images shown are an example of each protein of four independent experiments reproduced in triplicates. The abbreviations are the same as reported in Figure 1. Data are expressed as means ± SD (%) of four independent experiments normalised and verified on β-actin detection. In (a) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL. In (b) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL.

**Figure 11**
Western blot and densitometric analysis of ferroportin on total lysates of GTL-16 (a) and Caco-2 cells (b) of the VITVO^® system. The cells were treated with 50 and 30 μg/mL of different OvT and bLact. The images shown are an example of each protein of four independent experiments reproduced in triplicate. The abbreviations are the same as reported in Figure 1. Data are expressed as means ± SD (%) of four independent experiments normalised and verified on β-actin detection. In (a) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL. In (b) * p < 0.05 vs. control.

**Figure 12**
Analysis of TJ on Caco-2 lysates. (a) Zo-1; (b) claudin; (c) occludin measured by ELISA test. The cells were treated with 50 and 30 μg/mL of different OvT and bLact. The abbreviations are the same as reported in Figure 1. Data are expressed as means ± SD (%) of four independent experiments normalised to control the sample (0% line). In (a) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL. In (b) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL. In (c) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL.

**Figure 13**
Effects of Ovt and bLact on transferrin (a,b) and iron (c,d) absorption in cells pre-treated with 50 μMFe³⁺ over time (3 and 6 h). The abbreviations are the same as reported in Figure 1. Iron = pre-stimulation with 50 μM Fe³⁺. Data are expressed as means ± SD (%) compared to control of four independent experiments produced in triplicate. In (a–c) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL; φ p < 0.05 vs. apo-Ovt 50 μg/mL. In (d) * p < 0.05 vs. control; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL; φ p < 0.05 vs. apo-Ovt 50 μg/mL.

**Figure 14**
Western blot and densitometric analysis of DMT1 on total lysates of GTL-16 (a) and Caco-2 cells (b) of the VITVO^® system. The cells were treated with 50 and 30 μg/mL of different OvT and bLact. The images shown are an example of each protein of four independent experiments reproduced in triplicate. Iron= 50 μM Fe³⁺ and the abbreviations are the same as reported in Figure 1. Data are expressed as means ± SD (%) of four independent experiments normalised and verified on β-actin detection. In (a) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL; φ p < 0.05 vs. apo-Ovt 50 μg/mL. In (b) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL; φ p < 0.05 vs. apo-Ovt 50 μg/mL.

**Figure 15**
Western blot and densitometric analysis of ferritin on total lysates of GTL-16 (a) and Caco-2 cells (b) of the VITVO^® system. The cells were treated with 50 and 30 μg/mL of different OvT and bLact. The images shown are an example of each protein of four independent experiments reproduced in triplicate. Iron= 50 μM Fe³⁺ and the abbreviations are the same as reported in Figure 1. Data are expressed as means ± SD (%) of four independent experiments normalised and verified on β-actin detection. In (a) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; φ p < 0.05 vs. apo-Ovt 50 μg/mL. In (b) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL; φ p < 0.05 vs. apo-Ovt 50 μg/mL.

**Figure 16**
Western blot and densitometric analysis of ferroportin on total lysates of GTL-16 (a) and Caco-2 cells (b) of the VITVO^® system. The cells were treated with 50 and 30 μg/mL of different OvT and bLact. The images shown are an example of each protein of four independent experiments reproduced in triplicate. Iron= 50 μM Fe³⁺ and the abbreviations are the same as reported in Figure 1. Data are expressed as means ± SD (%) of four independent experiments normalised and verified on β-actin detection. In (a) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL; φ p < 0.05 vs. apo-Ovt 50 μg/mL. In (b) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; φ p < 0.05 vs. apo-Ovt 50 μg/mL.

**Figure 17**
Analysis of TJ on Caco-2 lysates. (a) Zo-1; (b) claudin; (c) occludin measured by ELISA test. The cells were treated with 50 and 30 μg/mL of different OvT and bLact. The abbreviations are the same as reported in Figure 1. Data are expressed as means ± SD (%) of four independent experiments normalised to control sample (0% line). In (a) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; φ p < 0.05 vs. apo-Ovt 50 μg/mL. In (b) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; δ p < 0.05 vs. bLact 50 μg/mL; φ p < 0.05 vs. apo-Ovt 50 μg/mL. In (c) * p < 0.05 vs. control; α p < 0.05 vs. holo-Ovt 100% 50 μg/mL; β p < 0.05 vs. holo-Ovt 15% 50 μg/mL; φ p < 0.05 vs. apo-Ovt 50 μg/mL.

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References

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[1] Bresson J.L., Burlingame B., Dean T., Fairweather-Tait S., Heinonen M., Hirsch-Ernst K.I., Mangelsdorf I., McArdle H., Naska A., Neuhauser-Berthold M., et al. Scientific Opinion on Dietary Reference Values for iron. EFSA J. 2015;13 doi: 10.2903/j.efsa.2015.4254. - DOI

[2] Bresson J.L., Burlingame B., Dean T., Fairweather-Tait S., Heinonen M., Hirsch-Ernst K.I., Mangelsdorf I., McArdle H., Naska A., Neuhauser-Berthold M., et al. Scientific Opinion on Dietary Reference Values for iron. EFSA J. 2015;13 doi: 10.2903/j.efsa.2015.4254. - DOI

[3] Goroll A.H., Mulley A.G. Primary Care Medicine. Volume 82. Ergodebooks; Houston, TX, USA: 2009. Office evaluation and management of the adult patient; pp. 607–608.

[4] Goroll A.H., Mulley A.G. Primary Care Medicine. Volume 82. Ergodebooks; Houston, TX, USA: 2009. Office evaluation and management of the adult patient; pp. 607–608.

[5] Theil E.C. Ferritin: Structure, gene regulation, and cellular function in animals, plants, and microorganism. Annu. Rev. Biochem. 1987;56:289–315. doi: 10.1146/annurev.bi.56.070187.001445. - DOI - PubMed

[6] Theil E.C. Ferritin: Structure, gene regulation, and cellular function in animals, plants, and microorganism. Annu. Rev. Biochem. 1987;56:289–315. doi: 10.1146/annurev.bi.56.070187.001445. - DOI - PubMed

[7] Qamar K., Saboor M., Qudsia F., Khosa S.M., Moinuddin Usman M. Malabsorption of iron as a cause of iron deficiency anemia in postmenopausal women. Pak. J. Med. Sci. 2015;31:304–308. - PMC - PubMed

[8] Qamar K., Saboor M., Qudsia F., Khosa S.M., Moinuddin Usman M. Malabsorption of iron as a cause of iron deficiency anemia in postmenopausal women. Pak. J. Med. Sci. 2015;31:304–308. - PMC - PubMed

[9] WHO . INT WHO. Report: Priorities in the Assessment of Vitamin A and Iron Status in Populations, Panama City, Panama, 15–17 September 2010. World Health Organization; Geneva, Switzerland: 2012.

[10] WHO . INT WHO. Report: Priorities in the Assessment of Vitamin A and Iron Status in Populations, Panama City, Panama, 15–17 September 2010. World Health Organization; Geneva, Switzerland: 2012.

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Ovotransferrin Supplementation Improves the Iron Absorption: An In Vitro Gastro-Intestinal Model

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Ovotransferrin Supplementation Improves the Iron Absorption: An In Vitro Gastro-Intestinal Model

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