Recent aspects of zinc absorption and bioavailability and correlations with physiology of the testicular Angiotensin-Converting Enzyme

Authors

  • Gilberto Simeone HENRIQUES Universidade de São Paulo
  • Mário Hiroiuki HIRATA Universidade de São Paulo
  • Sílvia Maria Franciscato COZZOLINO Universidade de São Paulo

Keywords:

zinc, angiotensin-converting enzyme, biological availability, testicular function, enzymes

Abstract

The stable association with macromolecules and the flexibility of the coordination geometry are particular properties of zinc and its essentiality has been associated with the biological functions assigned to the metal, either by participating directly in chemical catalysis or by helping to mantain protein and nucleic acid structures and stability. Zinc is the second most abundant essential trace element in the human organism and it is necessary to the activity of more than 300 enzymes, covering all 6 classes of them. These properties make this metal and its ligands subjects of great interest for experimental nutrition, leading to the determination of zinc
bioavailability. Among these ligands, the testicular Angiotensin- Converting Enzyme, synthesized by male germ cells, is an important example of the molecular regulation by zinc binding, determining both the activity and the concentrations of this enzyme, and affecting the testicular function.

References

Blanchard RK, Cousins RJ. Differential display of intestinal mRNA’s regulated by dietary zinc. Proc Natl Acad Sci USA 1996; 93:6863-8.

Chen X, Agarwal A, Giedroc DP. Structural and functional heterogeneity among the zinc fingers of human MRE-binding transcription factor-1. Biochemistry 1998; 37(32):11152-61.3. Blanchard RK, Cousins RJ. Regulation of intestinal gene expression by dietary zinc: Induction of uroguanylin mRNA by zinc deficiency. J Nutr 2000; 130:1393S-8S.

Coleman JE. Zinc proteins: enzymes, storage proteins, transcription factors and replication proteins. Ann Rev Biochem 1992; 61:897-946.

Valee BL, Falchuk KH. The biochemical basis of zinc physiology. Physiol Rev 1993; 73:79-111.

Valee BL, Auld DS. Zinc coordination, function and structure of zinc enzymes and other proteins. Biochemistry 1990; 29:5647-59.

Valee BL, Auld DS. New perspectives on zinc biochemistry: cocatalytic sites in multi-zinc enzymes. Biochemistry 1993; 32:6493-500.

Ippolito JA, Baird TT, McGee SA, Christianson DW, Fierke CA. Structure-assisted redesign of a protein- -zinc binding site with femtomolar affinity. Proc Natl Acad Sci 1995; 92:5017-21.

Butler A. Acquisition and utilization of transition metal ions by marine organisms. Sci Am 1998; 281:207-9.

Kaim W, Schwederski B. Zinc: structural gene- -regulatory functions and the enzymatic catalysis of hydrolysis or condensation reactions. In: Kaim W, Schwederski B, editors. Bioinorganic chemistry: inorganic elements in the chemistry of life, an introduction and guide. West Sussex: Wiley; 1996. p.242-64.

Margoshes M, Valee BL. A cadmium-and-zinc containing protein from equine kidney cortex. J Am Chem Soc 1957; 79(17):4813-4.

Kägi JHR. Metallothionein III. Experientia 1993; 53(suppl):29-55.

Salgueiro MJ, Zubillaga M, Lysionek A, Sarabia MI, Caro R, De Paoli T, et al. Zinc as an essential micronutrient: a review. Nutr Res 2000; 20(5):737-55.

Hempe JM, Cousins RJ. Cysteine-rich intestinal protein and intestinal metallothionein: an inverse relationship as a conceptual model for zinc absorption in rats. J Nutr 1992; 122(1):89-95.

Finley JW, Briske-Anderson M, Reeves PG, Johnson LK. Zinc uptake and transcellular movement by CACO-2 cells: studies with media containing fetal bovine serum. J Nutr Biochem 1995; 6:137-44.

Cousins RJ, MCmahon RJ. Integrative aspects of zinc transporters. J Nutr 2000; 30:1384S-7S.

Cozzolino SMF. Biodisponibilidade mineral. Rev Nutr 1997; 10(2):87-98.

Krebs NF. Overview of zinc absorption and excretion in the human gastrointestinal tract. J Nutr 2000; 130:1374S-7S.

King JC, Shames DM, Woodhouse LR. Zinc homeostasis in humans. J Nutr 2000; 130:1360S-6S.

Beshgetoor D, Lönerdal B. Effect of marginal maternal zinc deficiency in rats on mammary gland zinc metabolism. J Nutr Biochem 1997; 8:573-8.

Cousins RJ. Zinc. In: Ziegler EE, Filer LJ, editors. Present Knowledge in nutrition. Washington: ILSI Press; 1996. p.293-306.

O’Dell BL. Effect of dietary components upon zinc availability. Am J Clin Nutr 1969; 22(10):1315-22.

Hoadley JE, Leinart AS, Cousins AS. Kinetic analisys of zinc uptake and serosal transfer by vascularly perfused rat intestine. Am J Physiol 1987; 252:G825-31.

Mason KE, Burns WA, Smith JC. Testicular damage associated with zinc deficiency in pre-and postpubertal rats: Response to zinc repletion. J Nutr 1982; 112:1019-28.

Reeves PG, O’Dell BL. Effects of dietary zinc deprivation on the activity of angiotensin-converting enzyme in serum of rats and guinea pigs. J Nutr 1986; 116:128-34.

Jackson MJ. The assessments of bioavailability of micronutrients: Introduction. Eur J Clin Nutr 1997; 51(suppl):S1-S2.

Mawson CA, Fischer MI. Zinc in genital organs of rat. Nature 1951; 167(4156):859.

Reeves PG. Copper status of adult male rats is not affected by feeding an AIN 93G-based diet containing high concentrations of zinc. J Nutr Biochem 1996; 7:166-72.

Skeggs LT, Marsh WH, Kahn JR., Shumway NP. The existence of two forms of hypertensin. J Exp Med 1954; 99:275-82.

Skeggs LT, Kahn JR, Shumway NP. The preparation and function of the hypertensin-converting enzyme. J Exp Med 1956; 103:295.

Ehlers MRW, Riordan JF. Angiotensin-converting enzyme: Zinc-and inhibitor-binding stoichiometries of the somatic and testis isozymes. Biochemistry 1991; 30:7118-26.

Velletri PA, Aquilano DR, Brucknick E, Tsai-Morris CH, Dufau ML, Lovemberg W. Endocrinological control and cellular localization of rat testicular

angiotensin-converting enzyme (EC 3.4.15.1). Endocrinology 1985; 116(6):2516-22.

Ehlers MR, Fox EA, Strydom DJ, Riordan JF. Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme. Proc Natl Acad Sci USA1989; 86(20):7741-5.

Howard TE, Shai S, Langford KG, Martin BM, Bernstein KE. Transcription of testicular angiotensin-converting enzyme (ACE) is initiated within the 12th intron of the somatic ACE gene. Mol Cell Biol 1990; 10(8):4294-303.

Kessler SP, Rowe TM, Blendy JA, Erickson RP, Sem GC. A cyclic AMP response element in the angiotensin-converting enzyme gene and the transcription factor CREM are required for transcription of the mRNA for the testicular isozyme. J Biol Chem 1998; 273:9971-5.

Delmas V, Sassone-Corsi P. The key role of CREM in the cAMP signaling pathway in the testis. Mol Cell Endocrinol 1994; 100:121-4.

Ha H., van Wijnen AJ, Hecht NB. Tissue-specific protein-DNA interactions of the mouse protamine 2 gene promoter. J Cell Biochem 1997; 64: 95-105.

Reeves PG, Rossow KL. Zinc deficiency affects the activity and protein concentration of angiotensinconverting enzyme in rat testes. Proc Soc Exp Biol Med 1993; 203:336-42.

Stallard L, Reeves PG. Zinc deficiency in adult rats reduces the relative abundance of testis-specific Angiotensin-converting enzyme mRNA. J Nutr 1997; 127:25-9.

Henriques GS, Cozzolino SMF. Determination of metallothionein levels in tissues of young rats fed zinc-enriched diets. Rev Nutr 2001; 14(3):163-9.

Om AS, Chung KW. Dietary zinc deficiency alters 5 α-reduction and aromatization of testosterone and androgen and estrogen receptors in rat liver. J Nutr 1996; 126:842-8.

Foresta C, Mioni R, Rossato M, Varotto A, Zorzi M. Evidence for the involvement of sperm angiotensin converting enzyme in fertilization. Int J Androl 1991; 14:333-9.

Hagaman JR, Moyer JS, Bachman ES, Sibony M, Magyar PL, Welch JE, et al. Angiotensin-converting enzyme and male fertility. Proc Natl Acad Sci USA 1998; 95(5):2552-7.

Ramaraj P, Kessler SP, Colmenares C, Sem GC. Selective restoration of male fertility in mice lacking angiotensin-converting enzymes by sperm-specific expression of the testicular enzyme. J Clin Invest 1998; 102:371-78.

Published

2003-09-25

How to Cite

HENRIQUES, G. S., Hiroiuki HIRATA, M. ., & Franciscato COZZOLINO, S. M. . (2003). Recent aspects of zinc absorption and bioavailability and correlations with physiology of the testicular Angiotensin-Converting Enzyme. Brazilian Journal of Nutrition, 16(3). Retrieved from https://periodicos.puc-campinas.edu.br/nutricao/article/view/9147

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ARTIGOS DE REVISÃO