The Complex Relationship between Metals and Carbonic Anhydrase: New Insights and Perspectives
Abstract
:1. Introduction
2. Metals and CA Catalytic Site
CA Families | Metals as Physiologically-Relevant CA Cofactors | Ref. |
---|---|---|
α-CA | Zn2+ | [21] |
β-CA | Zn2+ | [7] |
γ-CA | Fe2+; Zn2+ | [9,22] |
δ-CA | Zn2+ | [10] |
ζ-CA | Cd2+; Zn2+ | [12] |
η-CA | Zn2+ | [2] |
2.1. Metals as Physiologically-Relevant Cofactors of CA
2.2. Metals as Displacers of the Native Metal Cofactor
2.3. Metal Binding to Other Sites in the CA Protein
3. Metals and CA Activity Inhibition
Species | Tissue | Cd2+ (mM) | Cu2+ | Hg2+ | Zn2+ | Co2+ | Pb2+ | Ag+ | Ref. |
---|---|---|---|---|---|---|---|---|---|
Callinectes sapidus | gills | Ki 0.1 × 10−3 | Ki 3.6 × 10−3 | Ki 2–6 × 10−3 | Ki 0.05 × 10-3 | [51] | |||
Carcinus maenas | gills | Ki 0.6–2.5 | Ki 0.6–2.5 | Ki 0.6–2.5 | [51] | ||||
Anguilla anguilla | gills | IC50 9.9 × 10−3 | [46] | ||||||
Anguilla anguilla | intestine | IC50 36.4 × 10−3 | [46] | ||||||
Sparus aurata | liver | Ki 17.7 (non-competitive) | Ki 36.2 (non-competitive) | Ki 0.02 (non-competitive) | [48] | ||||
Ictalurus punctatus | erythrocyte | IC50 0.9 | IC50 0.065 | IC50 0.7 | IC50 0.035 | [44] | |||
Oncorhynchus mykiss | brain | Ki 94.2 × 10−3 | Ki 27.6 × 10−3 (non-competitive) | Ki 1.20 | Ki 0.035 | [49] | |||
Acipenser gueldenstaedti | erythrocyte | IC50 5.2 | IC50 2.8 | IC50 1.7 | [53] | ||||
Dicentrarchus labrax | liver | Ki 0.76 | Ki 0.72 (competitive) | Ki 0.53 (competitive) | Ki 0.24 (competitive) | [47] | |||
Gallus | erythrocyte | Ki 2.78 (competitive) | Ki 1.26 (competitive) | Ki 0.97 (competitive) | [55] | ||||
Ovis aries | kidney | Ki 1.04 (competitive) | Ki 4.70 (competitive) | Ki 0.96 (competitive) | [54] | ||||
Homo sapiens | Erythrocyte, CA I | Ki 3.22 | Ki 3.22 (uncompetitive) | Ki 1.45 (competitive) | Ki 1 (non-competitive) | [52] | |||
Homo sapiens | Erythrocyte, CA II | Ki 0.312 | Ki 0.312 (uncompetitive) | Ki 1.7 (non-competitive) | Ki 0.056 (competitive) | [52] |
4. Metals and CA Protein Expression
5. CA and Trace Metals: Applicative Insights and Perspectives
5.1. CA Metallovariants
5.2. CA-Based Biosensors for Metal Ions
5.3. CA-Based Ecotoxicological Biomarkers and Bioassays for Metal Pollution Assessment
6. Conclusions
Acknowledgments
Author Contributions
Conflicts of Interest
References
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Lionetto, M.G.; Caricato, R.; Giordano, M.E.; Schettino, T. The Complex Relationship between Metals and Carbonic Anhydrase: New Insights and Perspectives. Int. J. Mol. Sci. 2016, 17, 127. https://doi.org/10.3390/ijms17010127
Lionetto MG, Caricato R, Giordano ME, Schettino T. The Complex Relationship between Metals and Carbonic Anhydrase: New Insights and Perspectives. International Journal of Molecular Sciences. 2016; 17(1):127. https://doi.org/10.3390/ijms17010127
Chicago/Turabian StyleLionetto, Maria Giulia, Roberto Caricato, Maria Elena Giordano, and Trifone Schettino. 2016. "The Complex Relationship between Metals and Carbonic Anhydrase: New Insights and Perspectives" International Journal of Molecular Sciences 17, no. 1: 127. https://doi.org/10.3390/ijms17010127