Back to the future: The human protein index (HPI) and the agenda for post-proteomic biology

Abstract

The effort to produce an index of all human proteins (the human protein index, or HPI) began twenty years ago, before the initiation of the human genome program. Because DNA sequencing technology is inherently simpler and more scalable than protein analytical technology, and because the finiteness of genomes invited a spirit of rapid conquest, the notion of genome sequencing has displaced that of protein databases in the minds of most molecular biologists for the last decade. However, now that the human genome sequence is nearing completion, a major realignment is under way that brings proteins back to the center of biological thinking. Using an influx of new and improved protein technologies--from mass spectrometry to re-engineered two-dimensional (2-D) gel systems, the original objectives of the HPI have been expanded and the time frame for its execution radically shortened. Several additional large scale technology efforts flowing from the HPI are also described.

Isolation and Isotope Labeling of Cysteine- and Methionine-containing Tryptic Peptides

“…density (1). Proteomic analyses using 2D-PAGE can be automated, but only at significant expense requiring automated gel staining and destaining devices, imaging equipment, imaging software, spot cutting robotics, automated in-gel digestion, robotic matrix-assisted laser desorption/ionization (MALDI) plate spotting, and mass spectrometry.…”

Effect of Zinc and DHA on Expression Levels and Post-Translational Modifications of Histones H3 and H4 in Human Neuronal Cells

“…Unlike the genome that is relatively static, the proteome is extremely dynamic and constantly adjusted in response to changing internal (e.g aging) and external events (e.g toxic exposure, drugs). Proteins are composed of a variety of combinations of amino acids, and are subject to co-as well as post-translational modification, such as deletion of amino acid sequences and chemical modification of specific amino acids (e.g oxidation and phosphorylation) (Anderson, Matheson et al 2001). These modifications will influence the activity state, function and interactions of proteins.…”

A path or a new road in laboratory diagnostics? Biological mass spectrometry: Facts and perspectives

“…This was already a goal even before the completion of the human genome mapping (Human Protein Index), but no methodology was available to carry it out. 1 Biological mass spectrometric methods represent a breakthrough exactly in this field. Proteomics research obtains information with modern analytical methods and aims to connect these data to gene functions.…”