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Abstract

Grant Number: 1P01GM067166-019001
Project Title: Core--Metal Ion Regulation /Transport
PI Information:NameEmailTitle
DAVID, LARRY L. davidl@ohsu.edu ASSOCIATE PROFESSOR

Abstract: The purpose of this core is to provide the instrumentation and technical support to fulfill the goals of this application. The core will provide atomic absorption analysis of metals; equipment and expertise to perform two-dimensional electrophoresis analysis of proteins, an IAsys apparatus for the analysis of protein protein interactions; a mass spectrometry facility for the analysis of proteins and peptides; and a confocal microscope facility for the immunolocalization of proteins in cells and tissues. The atomic absorption instrument will allow sensitive quantitative anlysis of copper, iron, and selenium ions necessary to study the cellular mechanisms regulating their transport and function. The two-dimensional electrophoresis equipment will be used to separate complex mixtures of cellular proteins to identify components of signal transduction pathways that regulate ion transport, and to elucidate mechanisms of metal ion toxicity. The IAsys apparatus will provide a direct way to measure the strength and specificity that ion transport proteins interact with other components in the cell that regulate their trafficking and activity. The mass spectrometer will be used to identify phosphorylation sites in ion transport proteins, identify new proteins regulating ion transport, determine how proteins, such as transferrin, interact to form protein complexes, and confirm the efficiency of incorporation of selenocysteine into proteins prepared for small angle x-ray diffraction experiments. The confocal microscope will allow direct visualization of the subcellular localization of ion transport proteins so that the mechanisms controlling their trafficking in normal and diseased tissue can be understood.

Public Health Relevance:
This Public Health Relevance is not available.

Thesaurus Terms:
biomedical equipment resource, biomedical facility, copper, ion transport, iron, protein protein interaction, protein structure function, selenium
atomic absorption spectrometry, confocal scanning microscopy, mass spectrometry, two dimensional gel electrophoresis

Institution: OREGON HEALTH AND SCIENCE UNIVERSITY
3181 SW Sam Jackson Pk Rd
PORTLAND, OR 972393098
Fiscal Year: 2003
Department:
Project Start: 01-DEC-2002
Project End: 30-NOV-2007
ICD: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
IRG: ZRG1


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