title: Metalloproteomics in the molecular study of cell physiology and disease.
abstract: 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.
authors: University of Heidelberg, Mannheim, Germany.
authors: Hermann-Josef
authors: HJ
authors: Thierse
authors: Stefanie
authors: S
authors: Helm
authors: Patrick
authors: P
authors: Pankert
mesh_terms: D002846:Chromatography, Affinity; D015180:Electrophoresis, Gel, Two-Dimensional; D013058:Mass Spectrometry; D008667:Metalloproteins / Q000032:analysis* / Q000502:physiology; D040901:Proteomics
chemical_list: D008667:Metalloproteins