Assessing protein patterns in disease using imaging mass spectrometry.
Direct tissue profiling and imaging mass spectrometry (MS) provides a detailed assessment of the complex protein pattern within a tissue sample. MALDI MS analysis of thin tissue sections results in over of 500 individual protein signals in the mass range of 2 to 70 kDa that directly correlate with protein composition within a specific region of the tissue sample. To date, profiling and imaging MS has been applied to multiple diseased tissues, including human gliomas and nonsmall cell lung cancer. Interrogation of the resulting complex MS data sets has resulted in identification of both disease-state and patient-prognosis specific protein patterns. These results suggest the future usefulness of proteomic information in assessing disease progression, prognosis, and drug efficacy.
Chaurand
Pierre
P
Mass Spectrometry Research Center, Department of Biochemistry, Vanderbilt University, Nashville, Tennessee 37232-8575, USA.
Schwartz
Sarah A
SA
Caprioli
Richard M
RM
D000818:Animals; D001932:Brain Neoplasms / Q000378:metabolism; D002289:Carcinoma, Non-Small-Cell Lung / Q000378:metabolism; D005910:Glioma / Q000378:metabolism; D006801:Humans; D008175:Lung Neoplasms / Q000378:metabolism; D013058:Mass Spectrometry / Q000379:methods*; D051379:Mice; D009369:Neoplasms / Q000378:metabolism; D010455:Peptides / Q000737:chemistry*; D011379:Prognosis; D011506:Proteins / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D013997:Time Factors
D010455:Peptides; D011506:Proteins