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Laser Ablation for Analysis of the Composition of Molecules in Tissues

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biophysics".

Deadline for manuscript submissions: closed (31 July 2021) | Viewed by 6589

Special Issue Editor

Institute of Clinical Chemistry and Laboratory Medicine, University Medical Center Hamburg-Eppendorf, Martinistr. 52, 20246 Hamburg, Germany
Interests: pathobiochemistry; proteoforms; glycomics; lipidomics; metabolomics; proteomics; mass spectrometry; liquid chromatography; biomarker

Special Issue Information

Dear Colleagues,

Comprehensive analysis of tissues gives information about the structure and function of organisms as well as about their disorders. Pathologists are getting important information about disease states by investigating images of the morphology of tissue sections using light microscopy of stained tissues. Using this approach, information about the chemical composition is minimal. Since the introduction of mass spectrometric imaging (MSI) approximately two decades ago, this gap is getting smaller and smaller. MALDI-MSI is one branch of MSI of tissue sections. MALDI-MSI can be interpreted as a special form of laser ablation, delivering information about the distribution of abundances of molecules in tissues. Laser ablation has also been combined with electrospray ionization (LAESI) for tissue analysis. A more direct form of laser ablation giving access to the distribution of elements in tissues is MSI performed with inductively coupled plasma mass spectrometry (ICP-MS). With ICP-MS in combination with antibodies labeled with metal ions (e.g. metal-coded affinity tags (MECAT)), even a targeted analysis of the distribution of defined proteins is possible. For untargeted analysis of “omes”, such as proteomes in tissues, laborious and time-consuming procedures, such as laser capture microdissection (LCM), have been used in recent years. Laser ablation as a tool for the sampling of tissues for the analysis of omes, requiring several sample preparation steps prior to MS, was introduced within this decade, e.g., by Isabelle Fournier, Marcel Kwiatkowski, or Kermit Murray, and is now a promising alternative for LCM. The picosecond infrared laser (PIRL), developed by Dwayne Miller, is also promising.

In summary, laser ablation either directly coupled with MS or for sampling has become an important tool in biochemistry and medicine.

The scope of this Special Issue is to highlight the theoretical background and report new results, current developments, and applications of methods that apply different forms of laser ablation for tissue analysis as described above. Reviews are also welcome.

Prof. Dr. Hartmut Schlüter
Guest Editor

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Keywords

  • inductively coupled plasma mass spectrometry (ICP-MS)
  • laser ablation electrospray ionization (LAESI)
  • mass spectrometric imaging (MSI)
  • MALDI-MSI
  • metal-coded affinity tags (MECAT)
  • picosecond infrared laser (PIRL)
  • tissue section
  • tissue sampling
  • glycomics
  • lipidomics
  • metabolomics
  • proteomics

Published Papers (2 papers)

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Research

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15 pages, 6594 KiB  
Article
Tissue Sampling and Homogenization in the Sub-Microliter Scale with a Nanosecond Infrared Laser (NIRL) for Mass Spectrometric Proteomics
by Jan Hahn, Manuela Moritz, Hannah Voß, Penelope Pelczar, Samuel Huber and Hartmut Schlüter
Int. J. Mol. Sci. 2021, 22(19), 10833; https://doi.org/10.3390/ijms221910833 - 07 Oct 2021
Cited by 5 | Viewed by 2070
Abstract
It was recently shown that ultrashort pulse infrared (IR) lasers, operating at the wavelength of the OH vibration stretching band of water, are highly efficient for sampling and homogenizing biological tissue. In this study we utilized a tunable nanosecond infrared laser (NIRL) for [...] Read more.
It was recently shown that ultrashort pulse infrared (IR) lasers, operating at the wavelength of the OH vibration stretching band of water, are highly efficient for sampling and homogenizing biological tissue. In this study we utilized a tunable nanosecond infrared laser (NIRL) for tissue sampling and homogenization with subsequent liquid chromatography tandem mass spectrometry (LC-MS/MS) analysis for mass spectrometric proteomics. For the first time, laser sampling was performed with murine spleen and colon tissue. An ablation volume of 1.1 × 1.1 × 0.4 mm³ (approximately 0.5 µL) was determined with optical coherence tomography (OCT). The results of bottom-up proteomics revealed proteins with significant abundance differences for both tissue types, which are in accordance with the corresponding data of the Human Protein Atlas. The results demonstrate that tissue sampling and homogenization of small tissue volumes less than 1 µL for subsequent mass spectrometric proteomics is feasible with a NIRL. Full article
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Review

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13 pages, 512 KiB  
Review
Mass Spectrometry Imaging as a Potential Tool to Investigate Human Osteoarthritis at the Tissue Level
by Yea-Rin Lee, Matthew T. Briggs, Mark R. Condina, Hamish Puddy, Paul H. Anderson, Peter Hoffmann and Julia S. Kuliwaba
Int. J. Mol. Sci. 2020, 21(17), 6414; https://doi.org/10.3390/ijms21176414 - 03 Sep 2020
Cited by 9 | Viewed by 3955
Abstract
Osteoarthritis (OA) is the most common degenerative joint disease, predicted to increase in incidence year by year due to an ageing population. Due to the biological complexity of the disease, OA remains highly heterogeneous. Although much work has been undertaken in the past [...] Read more.
Osteoarthritis (OA) is the most common degenerative joint disease, predicted to increase in incidence year by year due to an ageing population. Due to the biological complexity of the disease, OA remains highly heterogeneous. Although much work has been undertaken in the past few years, underlying molecular mechanisms leading to joint tissue structural deterioration are not fully understood, with only few validated markers for disease diagnosis and progression being available. Discovery and quantitation of various OA-specific biomarkers is still largely focused on the bodily fluids which does not appear to be reliable and sensitive enough. However, with the advancement of spatial proteomic techniques, several novel peptides and proteins, as well as N-glycans, can be identified and localised in a reliable and sensitive manner. To summarise the important findings from OA biomarker studies, papers published between 2000 and 2020 were searched via Google Scholar and PubMed. Medical subject heading (MeSH) terms ‘osteoarthritis’, ‘biomarker’, ‘synovial fluid’, ‘serum’, ‘urine’, ’matrix-assisted laser desorption/ionisation’, ‘mass spectrometry imaging’, ‘proteomic’, ‘glycomic’, ‘cartilage’, ‘synovium’ AND ‘subchondral bone’ were selectively used. The literature search was restricted to full-text original research articles and written only in English. Two main areas were reviewed for OA biomarker studies: (1) an overview of disease-specific markers detected from different types of OA bio-samples, and (2) an up-to-date summary of the tissue-specific OA studies that have utilised matrix-assisted laser desorption/ionisation mass spectrometry imaging (MALDI-MSI). Overall, these OA biomarkers could provide clinicians with information for better the diagnosis, and prognosis of individual patients, and ultimately help facilitate the development of disease-modifying treatments. Full article
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