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Article

Proteomic Analysis of Zn Depletion/Repletion in the Hormone-Secreting Thyroid Follicular Cell Line FRTL-5

1
Research Centre for Food and Nutrition, CREA, Via Ardeatina 546, 00178 Rome, Italy
2
Department of Pharmacy, Division of Chemistry & Chemical Technologies “Luigi Gomez Paloma”, University of Salerno, Via Giovanni Paolo II, 132 84084 Fisciano (SA), Italy
3
Nouscom, via di Castel Romano 100, 00128 Rome, Italy
4
Department of Pharmacy Biomedical Division “Arturo Leone”, University of Salerno, Via Giovanni Paolo II, 132 84084 Fisciano (SA), Italy
5
Department of Medicine, Surgery and Dentistry “Schola Medica Salernitana”, University of Salerno, Via Salvador Allende, 84081 Baronissi (SA), Italy
6
Department of Nutrition, Dietetics and Food, Monash University, Melbourne, VIC 3168, Australia
*
Authors to whom correspondence should be addressed.
Nutrients 2018, 10(12), 1981; https://doi.org/10.3390/nu10121981
Received: 21 November 2018 / Revised: 10 December 2018 / Accepted: 12 December 2018 / Published: 14 December 2018
(This article belongs to the Special Issue Health Effects of Dietary Zinc)
Zinc deficiency predisposes to a wide spectrum of chronic diseases. The human Zn proteome was predicted to represent about 10% of the total human proteome, reflecting the broad array of metabolic functions in which this micronutrient is known to participate. In the thyroid, Zn was reported to regulate cellular homeostasis, with a yet elusive mechanism. The Fischer Rat Thyroid Cell Line FRTL-5 cell model, derived from a Fischer rat thyroid and displaying a follicular cell phenotype, was used to investigate a possible causal relationship between intracellular Zn levels and thyroid function. A proteomic approach was applied to compare proteins expressed in Zn deficiency, obtained by treating cells with the Zn-specific chelator N,N,N′,N′-tetrakis (2-pyridylmethyl) ethylene-diamine (TPEN), with Zn repleted cells. Quantitative proteomic analysis of whole cell protein extracts was performed using stable isotope dimethyl labelling coupled to nano-ultra performance liquid chromatography-mass spectrometry (UPLC-MS). TPEN treatment led to almost undetectable intracellular Zn, while decreasing thyroglobulin secretion. Subsequent addition of ZnSO4 fully reversed these phenotypes. Comparative proteomic analysis of Zn depleted/repleted cells identified 108 proteins modulated by either treatment. Biological process enrichment analysis identified functions involved in calcium release and the regulation of translation as the most strongly regulated processes in Zn depleted cells. View Full-Text
Keywords: endocrine tissues; metal ion; zinc transport; ribosomes; calcium channels endocrine tissues; metal ion; zinc transport; ribosomes; calcium channels
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MDPI and ACS Style

Guantario, B.; Capolupo, A.; Monti, M.C.; Leoni, G.; Ranaldi, G.; Tosco, A.; Marzullo, L.; Murgia, C.; Perozzi, G. Proteomic Analysis of Zn Depletion/Repletion in the Hormone-Secreting Thyroid Follicular Cell Line FRTL-5. Nutrients 2018, 10, 1981. https://doi.org/10.3390/nu10121981

AMA Style

Guantario B, Capolupo A, Monti MC, Leoni G, Ranaldi G, Tosco A, Marzullo L, Murgia C, Perozzi G. Proteomic Analysis of Zn Depletion/Repletion in the Hormone-Secreting Thyroid Follicular Cell Line FRTL-5. Nutrients. 2018; 10(12):1981. https://doi.org/10.3390/nu10121981

Chicago/Turabian Style

Guantario, Barbara, Angela Capolupo, Maria C. Monti, Guido Leoni, Giulia Ranaldi, Alessandra Tosco, Liberato Marzullo, Chiara Murgia, and Giuditta Perozzi. 2018. "Proteomic Analysis of Zn Depletion/Repletion in the Hormone-Secreting Thyroid Follicular Cell Line FRTL-5" Nutrients 10, no. 12: 1981. https://doi.org/10.3390/nu10121981

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