Pure and Applied Chemistry

Laser ablation inductively coupled plasma mass spectrometry (LA-ICP-MS) has become established as a very efficient and sensitive trace, ultratrace, and surface analytical technique in the life sciences. We have developed a new analytical imaging technique using LA-ICP-MS to study element distribution in biological tissues. Nowadays, LA imaging ICP-MS using double-focusing sector field (LA-ICP-SFMS) or quadrupole-based mass spectrometers (LA-ICP-QMS) can be applied as an exciting tool providing new information on the pathophysiology, pharmacology, and toxicology of elements of interest in biological systems. The quantitative determination of elements (e.g., Cu, Fe, Zn, Se, and others) in biological tissues is of growing interest especially in brain research (e.g., for studying neurodegenerative diseases such as Alzheimer's or Parkinson's disease). LA-ICP-SFMS was employed to produce images of detailed regionally specific element distributions in thin tissue sections of different sizes (such as control human or rat brain tissues or tumor regions). In addition, imaging MS using LA-ICP-QMS was applied to study the uptake and transport of nutrient and toxic elements in plant tissues.

Besides the quantitative imaging of essential and toxic elements in tissues, powerful analytical techniques are also required for the determination and characterization of phosphoproteins and metal-containing proteins within a large pool of proteins, after electrophoretic separation (e.g., blue native, BN and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, SDS-PAGE) into 1D and 2D gels. LA-ICP-MS was used to detect metalloproteins in protein bands of 1D gels or protein spots separated after 2D gel electrophoresis (2D-GE). In addition to elemental determination by LA-ICP-MS, matrix-assisted laser desorption/ionization (MALDI)-MS was employed to identify metal-containing proteins. Recent progress will be discussed in applying LA-ICP-MS in the life sciences, including the imaging of thin slices of tissue and applications in proteome analysis in combination with MALDI-MS to investigate phosphoproteins and metal-containing proteins.