Research

Two-dimensional gel proteome reference map of blood monocytes

Ming Jin¹ , Philip T Diaz^2,3 , Tran Bourgeois¹ , Charis Eng^4,5 , Clay B Marsh^2,1,3 and Haifeng M Wu^1,2,3

¹  Department of Pathology, The Ohio State University, Columbus, OH, USA

²  Division of Pulmonary, Critical Care and Sleep Medicine, Department of Internal Medicine, The Ohio State University, Columbus, OH, USA

³  Dorothy M. Davis Heart and Lung Research Institute, The Ohio State University, Columbus, OH, USA

⁴  Genomic Medicine Institute, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH, USA

⁵  Department of Genetics, Case Western Reserve University School of Medicine, Cleveland Clinic Foundation, Cleveland, OH, USA

author email corresponding author email

Proteome Science 2006, 4:16doi:10.1186/1477-5956-4-16

Published:	1 September 2006

Abstract

Background:

Blood monocytes play a central role in regulating host inflammatory processes through chemotaxis, phagocytosis, and cytokine production. However, the molecular details underlying these diverse functions are not completely understood. Understanding the proteomes of blood monocytes will provide new insights into their biological role in health and diseases.

Results:

In this study, monocytes were isolated from five healthy donors. Whole monocyte lysates from each donor were then analyzed by 2D gel electrophoresis, and proteins were detected using Sypro Ruby fluorescence and then examined for phosphoproteomes using ProQ phospho-protein fluorescence dye. Between 1525 and 1769 protein spots on each 2D gel were matched, analyzed, and quantified. Abundant protein spots were then subjected to analysis by mass spectrometry. This report describes the protein identities of 231 monocyte protein spots, which represent 164 distinct proteins and their respective isoforms or subunits. Some of these proteins had not been previously characterized at the protein level in monocytes. Among the 231 protein spots, 19 proteins revealed distinct modification by protein phosphorylation.

Conclusion:

The results of this study offer the most detailed monocyte proteomic database to date and provide new perspectives into the study of monocyte biology.