Abstract
The purpose of this research was to perform a preliminary assessment of protein patterns in primary brain tumors using a direct-tissue mass spectrometric technique to profile and map biomolecules. We examined 20 prospectively collected, snap-frozen normal brain and brain tumor specimens using matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS), and compared peptide and protein expression in primary brain tumor and nontumor brain tissues. MS can be used to identify protein expression patterns in human brain tissue and tumor specimens. The mass spectral patterns can reliably identify glial neoplasms of similar histological grade and differentiate them from tumors of different histological grades as well as from nontumor brain tissues. Initial bioinformatics cluster analysis algorithms classified tumor and nontumor tissues into similar groups comparable with their histological grade. We describe a novel tool for the analysis of protein expression patterns in human glial neoplasms. Initial results demonstrate that MALDI-MS technology can significantly aid in the process of unraveling and understanding the molecular complexities of gliomas. MALDI-MS accurately and reliably identified normal and neoplastic tissues, and could be used to discriminate between tumors of increasing grades.
Highlights
Primary brain tumors are a heterogeneous group of neoplasms, each with its own set of genetic and physiological changes that appear to underlie individual patterns of growth, invasion, response to therapy, and prognosis [1, 2]
Whereas the completion of the human genome project has provided a great deal of insight into the genetic aberrations underlying cancer in general, and brain neoplasms in particular, it is becoming more apparent that having the complete sequence of the human genome and its alteration in tumors is not sufficient to elucidate biological function (4 – 8)
matrix-assisted laser desorption/ionization (MALDI)-mass spectrometry (MS) can be used to detect the molecular weight of peptides and proteins over Mr 100,000 directly from a variety of in vitro and in vivo samples including protein solutions, fresh-frozen tissue sections, microdissected fresh tissues, or from cells derived in culture (10 –17)
Summary
Primary brain tumors are a heterogeneous group of neoplasms, each with its own set of genetic and physiological changes that appear to underlie individual patterns of growth, invasion, response to therapy, and prognosis [1, 2]. MALDI-MS can be used to detect the molecular weight of peptides and proteins over Mr 100,000 directly from a variety of in vitro and in vivo samples including protein solutions, fresh-frozen tissue sections, microdissected fresh tissues, or from cells derived in culture (10 –17) In this method, a sample is deposited or mounted on a metal plate, U-desorbing matrix is deposited on the sample, and each matrix droplet is analyzed. These charged molecules are accelerated down a flight tube and detected, and the m/z ratio of each molecule is determined (10 –17)
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