Introduction to Proteomics

Delfina C Domínguez; Rosana Lopes; M Lorraine Torres

doi:10.29074/ascls.20.4.234

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Delfina C Domínguez, PhD⇑
1. is associate professor of the Clinical Laboratory Science Program, The University of Texas at El Paso, College of Health Sciences, El Paso TX
Rosana Lopes, PhD
1. is assistant research professor of the Clinical Laboratory Science Program, The University of Texas at El Paso, College of Health Sciences, El Paso TX
M Lorraine Torres, MS
1. is faculty and program director of the Clinical Laboratory Science Program, The University of Texas at El Paso, College of Health Sciences, El Paso TX

Address for correspondence: Delfina C Domínguez PhD, University of Texas at El Paso, Clinical Laboratory Science, College of Health Sciences.1101 N. Campbell Street. El Paso TX, 79902-4238. (915) 747-7238, (915) 747-7207 (fax). Delfina{at}utep.edu.

Compare and contrast gene expression versus protein expression.
Discuss the purpose and goals of proteomics.
Identify the steps followed in a proteomic analysis.
Describe the main techniques used in proteomics.

Extract

Technological advances in the field of genomics have given rise to the development of a new area called proteomics. Proteomics involves the analysis of all proteins expressed in a genome and uses a combination of sophisticated technologies such as two-dimensional electrophoresis, mass spectrometry and bioinformatics to identify and characterize proteins. This new area offers the potential to discover new biomarkers, improve diagnosis, and improve the prognosis of disease processes. This article presents an overview of proteomics importance and related technologies.

The sequencing of the human genome, which unveiled the total genetic content in eukaryotes and advanced technology, has lead to the development of a new field called proteomics. Proteomics encompasses the analysis of all proteins expressed in a cell.¹ Two dimensional electrophoresis (2-DE) and mass spectrometry (MS) are the main techniques used in proteomics. Documenting protein expression of an organism by 2-DE analysis is not a new concept. In 1970, Kaltschmidt and Wittmann² separated ribosomal proteins from Escherichia coli by two-dimensional electrophoresis. A few years later, Klose,³ O'Farrel,⁴ and Scheele⁵ described 2-DE as the main technique used for the separation of complex protein mixtures into distinct protein spots. The direct study of protein expression began with Anderson and Anderson in 1977 who for the first time analyzed human plasma proteins and anticipated the possibility of identifying all proteins present in the human body.⁶ For the past 20 years, 2-DE has been considered the standard technique for analyzing the proteins expressed by cells, tissues and fluids.⁷

Before the genomics revolution, proteins…

ABREVIATIONS: 2-DE = two-dimensional electrophoresis; IPG = immobilized pH gradient; MALDI-TOF = matrix assisted laser desorption ionization time-of-flight; mRNA = messenger ribonucleic acid; pI = isoelectric point.