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New Technique Yields Troves of Information From Nanoscale Bone Samples
Engineering Researchers at Rensselaer
Polytechnic Institute Have Developed New Process for the
Microdissection and In-Depth Biochemical Analysis of Bone
Tissue
A new technique developed at Rensselaer Polytechnic
Institute allows researchers to collect large amounts of
biochemical information from nanoscale bone samples.
Along with adding important new insights into the fight
against osteoporosis, this innovation opens up an entirely new
proteomics-based approach to analyzing bone quality. It could
even aid the archeological and forensic study of human
skeletons.
“We’re able to take very small, nanoscale-sized bone
samples, and determine the protein signatures of the bone,”
said Deepak Vashishth, head of the Department of Biomedical
Engineering at Rensselaer, who led the study. “This is a
relatively quick, easy way for us to determine the history of
the bone – how and when it formed – as well as the quality of
the bone, and its likelihood to fracture.”
Results of the study, titled “Biochemical Characterization
of Major Bone-Matrix Proteins Using Nanoscale-Size Bone Samples
and Proteomics Methodology,” were released online in late May
by the journal Molecular & Cellular
Proteomics. The journal, published by the American
Society for Biochemistry and Molecular Biology, will also
feature the paper in an upcoming print edition. The study may
be viewed online at: http://bit.ly/lAfSfI.
The research, funded by the U.S. National Institutes of
Health, was conducted in the laboratories of the Center for Biotechnology and
Interdisciplinary Studies at Rensselaer.
Bones are primarily composed of mineral, with the remaining
amount comprised of organic material. The vast majority of the
organic material is collagen. The remaining non-collagenous
organic material is a mixture of other proteins, which form an
interlinked matrix. The quality of this matrix varies greatly
with age, nutrition, and disease. Vashishth and his research
group investigate this bone matrix to determine how the
interaction and modification of individual proteins impact the
development, structure, and strength of the overall bone.
In this study, they paired laser-capture microscopy with
several other techniques to create an entirely new method for
analyzing bone matrix. The analysis yields data about the
concentration of different proteins in the bone matrix, which
in turn leads to key information about the bone – such as when
it was formed, how it has been modified, and if it is more or
less prone to fracture.
Vashishth said this is an important step toward augmenting
current osteoporosis diagnosis techniques, which measure bone
loss and the quantity of bone present, with new, minimally
invasive, proteomics-driven techniques for assessing the
quality of the bone.
The young field of proteomics focuses on the structure and
function of proteins, and is ripe for innovation, Vashishth
said. The term “proteomics” echoes the word genomics, the study
of genes. Proteomics seeks to decode the human proteome by
documenting the structure, function, and interactions of
proteins.
“This is kind of a new area, because bone fracture has
always been looked at from a bone calcium perspective, a
mineral perspective, and current osteoporosis treatment methods
are all geared toward that,” he said. “In osteoporosis, very
little attention has been paid to bone proteins. That’s why
we’re very excited about our new proteomics-based method to
read a bone’s protein signature, and assess the quality of the
bone. I think it opens up a new avenue for approaching and
studying osteoporosis.”
Like all tissues in the human body, bones regenerate
themselves over time. Bones regenerate much slower than other
tissues, however, and the skeleton takes about 10 years to
gradually replace itself with new tissue. Different parts of a
bone regenerate at different rates, meaning some areas of a
bone may be older and more susceptible to fracture, while other
areas of the same bone are newer and sturdier. Older and
younger parts of a bone have different protein signatures and
react differently to medical treatments. Vashishth said his new
method is an easy way to help differentiate between different
aged areas of bone, determine their quality, and forecast their
susceptibility to fracture.
Finally, along with pushing forward the emerging field of
bone proteomics and opening up new possibilities for studying
and treating osteoporosis, Vashishth’s findings could prove
useful to researchers in other areas who deal with bone.
Forensics, biology, anthropology, archaeology, and other areas
where bone samples are truly rare, small, and precious would
likely find it useful to analyze bone protein signatures with
minimal damage to the bone sample, he said. This protein
signature information could offer new insight into how bones
were formed, along with the nutrition and diet of those
individuals.
Co-authors of the study are
Wilfredo Colon, professor in the Rensselaer Department of Chemistry
and Biological Chemistry; as well as postdoctoral
researcher Grazyna Sroga and doctoral student Lamya Karim, both
in the Rensselaer Department of Biomedical
Engineering.
For more information on Vashishth and his research at
Rensselaer, visit:
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Published
June 22,
2011 |
Contact: Michael Mullaney
Phone: (518) 276-6161
E-mail: mullam@rpi.edu |
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