Summary
Physical and chemical stresses as well as metal-related diseases can disrupt the normal trafficking of metal ions. Moreover, homeostatic imbalance of such metal ions may modulate essential cellular functions (including signal transduction pathways), may catalyze oxidative damage, and may affect the folding of nascent proteins. Here we describe a new qualitative subproteomic method for the detection, isolation, and identification of metal-interacting proteins. Combining both classical immobilized metal ion affinity chromatography (IMAC) and modern proteomic techniques (e.g., two dimensional gel electrophoresis [2-DE]), metal-specific proteins have been successfully isolated and identified to define a metalloproteome. These metal-specific proteomes may give new insights into metal-related pathophysiological processes, such as the allergic reaction to nickel, which represents the most common form of human contact hypersensitivity.
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Acknowledgments
We thank Doris Wild and Stefanie Eikelmeier for excellent technical assistance, and Dr. Ian Haidl, Depts. of Pediatrics, Microbiology and Immunology, Halifax, Canada, for very careful reading of the manuscript. This work was supported in part by the Landesstiftung Baden-Wüerttemberg, Germany, Forschungsprogramm “Allergologie” by grant P-LS-AL/26 (to HJT), and the European Union, as part of the project Novel Testing Strategies for In Vitro Assessment of Allergens (Sens-it-iv), LSHB-CT-2005 – 018681, (www.sens-it-iv.eu).
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Thierse, HJ., Helm, S., Pankert, P. (2008). Metalloproteomics in the Molecular Study of Cell Physiology and Disease. In: Posch, A. (eds) 2D PAGE: Sample Preparation and Fractionation. Methods in Molecular Biology™, vol 425. Humana Press. https://doi.org/10.1007/978-1-60327-210-0_12
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DOI: https://doi.org/10.1007/978-1-60327-210-0_12
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