Imaging Mass Spectrometry of Intact Biomolecules in Tissue Sections - Proteomic and Metabolomic Approaches to Biomarker Discovery - page 382

CHAPTER
25

Imaging Mass Spectrometry of Intact
Biomol ecules in Tissue S ections

Erin H. Seeley, Richard M. Caprioli
Mass Spectrometry Research Center, Department of Biochemistry,
Vanderbilt University School of Medicine, Nashville, TN, USA

OUTLINE

Introduction 393 3D Imaging 401

Matrix Application 394 High-Speed Imaging 403

Protein Analysis 396 Conclusions and Perspectives 403

Peptides and Protein Digests 397 Acknowledgments 403

Lipid Analysis 399 References 403

Drug Analysis 400

INTRODUCTION

dehydration, washing with organic solvents or
buffers, and matrix application. Mass spectral
data are then generated using an ionization
probe passed over the tissue surface in a raster
pattern, where each ablated spot or pixel gives
rise to an individual mass spectrum.
Traditional proteomic techniques for the anal-
ysis of molecules from tissue specimens, such as
LC-MS or 2D gel analysis, require that the tissue
be homogenized prior to analysis, eliminating
the spatial localization of analytes. Immunohis-
tochemistry allows for the localization of speci

Imaging mass spectrometry (IMS) technology
enables the in situ analysis of biomolecules
and pharmaceutical compounds directly from
thin tissue sections. 1 e 3 Thin sections (typically
5 e 20

m) are taken from a block of tissue and
collected onto a target in a fashion similar to
that used for histological analysis. After collec-
tion, sections are processed by one of several
methods depending on the class of molecules
to be analyzed. These steps may include

m

c