Imaging Mass Spectrometry in Papillary Thyroid Carcinoma for the Identification and Validation of Biomarker Proteins.
10.3346/jkms.2014.29.7.934
- Author:
Kyueng Whan MIN
1
;
Joo Young BANG
;
Kwang Pyo KIM
;
Wan Seop KIM
;
Sang Hwa LEE
;
Selina Rahman SHANTA
;
Jeong Hwa LEE
;
Ji Hye HONG
;
So Dug LIM
;
Young Bum YOO
;
Chan Hyun NA
Author Information
1. Department of Pathology, Konkuk University School of Medicine, Seoul, Korea. wskim@kuh.ac.kr
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
Pathology;
Proteins;
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization;
Thyroid Gland;
Neoplasms
- MeSH:
Aged;
Amino Acid Sequence;
Biological Markers/*analysis;
Carcinoma/*diagnosis/metabolism/pathology;
Chromatography, High Pressure Liquid;
Cluster Analysis;
Female;
Humans;
Image Processing, Computer-Assisted;
Male;
Middle Aged;
Molecular Sequence Data;
Molecular Weight;
Phosphoproteins/analysis/metabolism;
Proteome/analysis;
Proteomics;
Reproducibility of Results;
Ribosomal Proteins/analysis/metabolism;
*Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization;
*Tandem Mass Spectrometry;
Thyroid Gland/metabolism/pathology;
Thyroid Neoplasms/*diagnosis/metabolism/pathology
- From:Journal of Korean Medical Science
2014;29(7):934-940
- CountryRepublic of Korea
- Language:English
-
Abstract:
Direct tissue imaging mass spectrometry (IMS) by matrix-assisted laser desorption ionization and time-of-flight (MALDI-TOF) mass spectrometry has become increasingly important in biology and medicine, because this technology can detect the relative abundance and spatial distribution of interesting proteins in tissues. Five thyroid cancer samples, along with normal tissue, were sliced and transferred onto conductive glass slides. After laser scanning by MALDI-TOF equipped with a smart beam laser, images were created for individual masses and proteins were classified at 200-microm spatial resolution. Based on the spatial distribution, region-specific proteins on a tumor lesion could be identified by protein extraction from tumor tissue and analysis using liquid chromatography with tandem mass spectrometry (LC-MS/MS). Using all the spectral data at each spot, various intensities of a specific peak were detected in the tumor and normal regions of the thyroid. Differences in the molecular weights of expressed proteins between tumor and normal regions were analyzed using unsupervised and supervised clustering. To verify the presence of discovered proteins through IMS, we identified ribosomal protein P2, which is specific for cancer. We have demonstrated the feasibility of IMS as a useful tool for the analysis of tissue sections, and identified the tumor-specific protein ribosomal protein P2.
