Have
you ever googled mass spectrometry? The search returns 23,600,000
hits, underscoring its extensive use world wide in a broad range
of applications and disciplines. The use of mass spectrometry at
the University of Arizona is as equally extensive with a large
range of use by faculty, postdoctoral fellows, employees and students
taking advantage of its impressive power. Due to this extensive
use and the collective expertise that exists at the University
of Arizona in this area, the Mass Spectrometry Consortium was formed
in 2006. The Mass Spectrometry Consortium is co-directed by Drs.
Serrine S. Lau, Professor of Pharmacology and Toxicology, and Vicki
H. Wysocki, Professor of Chemistry. Various mass-spectrometry based
units are part of this consortium infrastructure including Molecular
Mass Spectrometry housed in Old Chemistry, Inorganic Mass Spectrometry
housed in Geo Sciences and the Arizona Proteomics Consortium housed
collectively in the BIO5 Institute, College of Pharmacy, and Old
Chemistry. The Water Contamination Center in Gould Simpson is also
planned to join the Mass Spectrometry Consortium. To view the organizational
structure of the Arizona Mass Spectrometry Consortium click here:
http://massspectrometryconsortium.arizona.edu/.
Of
special importance to many investigators is the use of mass spectrometry
within the context of biologically relevant systems and applications.
As such, proteomics at the University of Arizona has grown exponentially
and with great momentum over the past 6-8 years. The study of "proteomics",
or the protein complement of the cell, is considered the counterpart
to the study of the genetic complement of the cell, or genomics.
Proteomics is a scientific effort to identify, characterize and
assess protein function in living cells. Scientists look for
normal proteins, and when they find them, things are as they
should be. When new or altered proteins are found that are associated
with diseased states, this is a signal/marker for further examination.
Human proteomics research focuses on determining which of the
millions of proteins or combinations of proteins made up by human
cells are involved in the cause or in the persistence of disease.
This
is an exciting field since the human proteome (i.e: the assembly
of proteins in any one cell), is always changing and many opportunities
exist during these stages of change for insight into the differences
between normal and diseased states as well as for therapy. With
that in mind, the Arizona Proteomics Consortium (http://www.arizonaproteomics.org/)
strives to remain current in terms of instrumentation and its
method development capabilities, to better serve the scientific
endeavors of University of Arizona investigators.
Proteomics
relies heavily on analytical and bio-analytical techniques to
probe proteins. The key to proteomics is partial protein sequence
analysis coupled to computer-assisted searching of genomic and
protein sequence databases (see figure above).
Starting
from a sample and following some good old-fashioned biochemical
techniques, individual or assemblies of proteins to be identified
(either normal or aberrant in nature), are cleaved into smaller
pieces known as peptides. These peptides are then introduced
into and analyzed with mass spectrometers that give mass information
and/or structural information about these peptides. Computer
programs then use all of this information to search available
databases for the protein origin of these peptides. With these
tools, scientists can identify specific proteins, and characterize
which proteins interact with each other.
The
Proteomics Core of the University of Arizona, which was started
in 1998, sponsored by the Southwest Environmental Health Sciences
Center (SWEHSC Director, Serrine S. Lau, http://swehsc.pharmacy.arizona.edu/ ) is currently housed in the College of Pharmacy. In January
2006 the core expanded to a centralized Arizona Proteomics Consortium
(Director, George Tsaprailis; Associate Director, Linda Breci)
and is supported by the Arizona Cancer Center, Arizona Research
Laboratories, BIO5, Department of Chemistry and SWEHSC. Due to
rapidly changing research needs, this facility has seen its workload
more than triple in the past few years in addition to expanding
into new exciting areas such as imaging and profiling of proteins
in frozen tissue by MALDI-TOF mass spectrometry. New instrumentation
for proteomics has also been recently added to this facility
through various successful funding opportunities.
In
addition to being targets for drugs, proteins can be targets
for prevention of diseases such as cancer. For instance, if doctors
know a specific gene or protein is associated with cancer and
find it when it first develops, they may be able to block it
before it sends incorrect messages to cells.
Computers
and bioinformatics tools are a tremendous help in this overall
endeavor. They can review thousands and millions of pieces of
data very quickly, and they work day and night. That allows researchers
to identify patterns associated with particular diseases. As
more and more of patterns are identified, newer and better drugs
can be developed to stop faulty genes and proteins, hopefully
without causing the side effects associated with certain current
disease therapies. |