NDLI: Matrix-assisted laser desorption ionization-imaging mass spectrometry: a new methodology to study human osteoarthritic cartilage.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Cillero-Pastor, Berta Eijkel, Gert B. Kiss, Andras Blanco, Francisco J. Heeren, Ron M. A.
Description	Country affiliation: Netherlands Author Affiliation: Cillero-Pastor B ( FOM Institute AMOLF, Amsterdam, The Netherlands.)
Abstract	OBJECTIVE: Information about the distribution of proteins and the modulation that they undergo in the different phases of rheumatic pathologies is essential to understanding the development of these diseases. We undertook this study to demonstrate the utility of mass spectrometry (MS)-based molecular imaging for studying the spatial distribution of different components in human articular cartilage sections. METHODS: We compared the distribution of peptides and proteins in human control and osteoarthritic (OA) cartilage. Human control and OA cartilage slices were cut and deposited on conductive slides. After tryptic digestion, we performed matrix-assisted laser desorption ionization-imaging MS (MALDI-IMS) experiments in a MALDI-quadrupole time-of-flight mass spectrometer. Protein identification was undertaken with a combination of multivariate statistical methods and Mascot protein database queries. Hematoxylin and eosin staining and immunohistochemistry were performed to validate the results. RESULTS: We created maps of peptide distributions at 150-µm raster size from control and OA human cartilage. Proteins such as biglycan, prolargin, decorin, and aggrecan core protein were identified and localized. Specific protein markers for cartilage oligomeric matrix protein and fibronectin were found exclusively in OA cartilage samples. Their distribution displayed a stronger intensity in the deep area than in the superficial area. New tentative OA markers were found in the deep area of the OA cartilage. CONCLUSION: MALDI-IMS identifies and localizes disease-specific peptides and proteins in cartilage. All the OA-related peptides and proteins detected display a stronger intensity in the deep cartilage. MS-based molecular imaging is demonstrated to be an innovative method for studying OA pathology.
File Format	HTM / HTML
ISSN	00043591
e-ISSN	15290131
Journal	Arthritis & Rheumatism
Issue Number	3
Volume Number	65
Language	English
Publisher	Wiley-Blackwell
Publisher Date	2013-03-01
Publisher Place	United States
Access Restriction	Subscribed
Subject Keyword	Immunohistochemistry Amino Acid Sequence Tissue Banks Research Support, Non-u.s. Gov't Decorin Peptide Fragments Biological Markers Molecular Sequence Data Biglycan Metabolism Spectrometry, Mass, Matrix-assisted Laser Desorption-ionization Reproducibility Of Results Pathology Aggrecans Cartilage, Articular Proteomics Osteoarthritis, Knee Discipline Rheumatic Diseases
Content Type	Text
Resource Type	Article
Subject	Immunology and Allergy Immunology Pharmacology (medical) Rheumatology

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