This minimally invasive technique, called Polarization Gating Spectroscopy, will now be tested in a much larger international clinical trial led by the Mayo Clinic researchers. The preliminary study suggests it may be possible, one day, to use a less invasive endoscope to screen patients for early development of pancreatic cancer.

The pancreas is notoriously hard to reach and see due to its very deep location in the abdomen, surrounded by intestines. The study investigators theorized that there may be changes in the nearby “normal appearing” tissue of the small intestine which is much more accessible.

“No one ever thought you could detect pancreatic cancer in an area that is somewhat remote from the pancreas, but this study suggests it may be possible,” says Dr. Michael Wallace, chairman of the Division of Gastroenterology at Mayo Clinic in Florida. “Although results are still preliminary, the concept of detection field effects of nearby cancers holds great promise for possible early detection of pancreatic cancer.”

In this study, the Mayo Clinic physicians tested a light probe developed by their long-time collaborators at Northwestern University.

The light, attached to a small fiber-optic probe known as an endoscope, measures the amount of oxygenated blood as well as the size of blood vessels in tissue near the duct where the pancreas joins the small intestine. Because a growing tumor requires a heightened supply of blood, normal tissue in the vicinity of the cancer reveals evidence of enlarged blood vessels and changes in the amount of oxygen within the blood.

Such “field effects” from cancer can be measured in other areas of the GI tract, says Dr. Wallace. “With this technology, others studies have shown that cancerous polyps can be detected more than 11 inches from the polyp itself. Early studies are evaluating if esophageal cancers can also be detected remotely,” he says.

The probe acts “a bit like a metal detector that beeps faster and louder as you get close to cancer,” he says. The researchers are measuring within six to 10 inches of the pancreas in the small intestine immediately next to the pancreas.

Dr. Wallace and his team tested the probe on 10 patients who were later determined to have pancreatic cancer, and on nine participants who did not have pancreatic cancer.

They found that testing both measures — blood vessel diameter and blood oxygenation — detected all 10 pancreatic cancers. But the probe was less precise (63 percent accurate) in determining which of the healthy volunteers did not have pancreatic cancer.

“There is room for improvement in this instrument, and our group is working on that,” he says. “If the studies confirm the early results, it would make the pancreas accessible to a much simpler upper endoscope and that would be a real advance in the treatment of pancreatic cancer.”

Patients now often undergo an endoscopic examination of the upper intestine to search for the cause of heartburn or stomach pain, Dr. Wallace says. An endoscopic probe could be easily outfitted to explore for evidence of pancreatic cancer in patients at heightened risk, he says.

Mihir Patel, M.D., a gastroenterologist who worked with Dr. Wallace on the study, says that despite of intense research, we haven’t been successful in significantly improving the overall survival associated with pancreatic cancer in the past several decades. That’s because we haven’t been able to detect the cancer early enough. Developing a technique to screen the patients and detect pancreatic cancer at an early stage would be a potential breakthrough. In preliminary data, this technology has shown to hold similar potential.

Ann Decker, Executive Director, Indian River State College (IRSC) Foundation; Dr. Edwin Massey, President, IRSC; Dean Hart, Chief Commercial Officer, NanoInk; Dr. Kevin Cooper, Director of Advanced Technology, IRSC; Jason Fromer, Global Business Development Executive, NanoProfessor,

NanoProfessor® has partnered with Indian River State College (IRSC) in Fort Pierce, Fla. in the naming of the NanoProfessor Advanced Materials Lab within the newly opened Brown Center for Innovation and Entrepreneurship. Indian River State College will be the first college in the Southeastern U.S. to offer students access to the instrumentation and curriculum provided by the NanoProfessor Nanoscience Education Program.

“We are committed to offering Indian River State College students an education that prepares them for hi-tech jobs in the fields of nanotechnology, alternative energy, photonics, nanomaterials, electronics, and more,” said Dr. Edwin Massey, President of IRSC. “In accordance with that commitment, we have partnered with NanoProfessor in the NanoProfessor Advanced Materials Lab. Within this lab, IRSC students will have access to state-of-the-art instruments and an advanced curriculum that has traditionally only been available to graduate students at research universities.”

“We are pleased to be associated with the wonderful work being done at Indian River State College through our partnership in naming the NanoProfessor Advanced Materials Lab,” said Dean Hart, Chief Commercial Officer of NanoInk. “The Brown Center for Innovation and Entrepreneurship is an incredible example of the commitment IRSC has made in preparing a hi-tech workforce for Florida’s Research Coast. Companies will no doubt take notice that IRSC is providing the type of talented human capital needed to grow successful hi-tech businesses in Florida.”

The NanoProfessor Nanoscience Education Program provides IRSC students with access to instrumentation, curriculum, and hands-on labs to expand their knowledge, skills, and real-world experience needed to work in the growing nanotechnology industry. In conducting lab experiments, students learn the fundamentals for building custom-engineered nanoscale structures while working with state-of-the-art  equipment including NanoInk’s NLP 2000 Desktop NanoFabrication System, an atomic force microscope, a nanoparticle characterization instrument, an advanced fluorescence microscope, and various chemical and biological materials used today within current and emerging nanotechnology applications.

At the dedication of the NanoProfessor Advanced Materials Lab, Dean Hart presented Dr. Edwin Massey a unique, framed image of the smallest IRSC logo in existence. Consisting of 6,500 20-nanometer dots, the actual logo was printed with NanoInk’s proprietary Dip Pen Nanolithography® and only measures 10 x 10 microns. The framed image of the micron-sized IRSC logo will hang in the NanoProfessor Advanced Materials Lab and includes a plaque stating that approximately 17,000 copies of the actual printed IRSC logo could be placed on the head of a pin, helping students and visitors to the lab better understand the incredibly small size of nanotechnology.

The Brown Center for Innovation and Entrepreneurship at the IRSC Main Campus in Fort Pierce is a multi-purpose, energy-efficient building containing technologically advanced laboratories designed to develop the skills necessary for hi-tech employment or entrepreneurship. The 65,000-square-foot building was constructed to Silver LEED standards of environmental design with recycled materials.

Lyden possesses an extensive background in biostatistical analysis in pharmaceutical, biotechnical and medical device clinical research. Prior to founding BioStat International, Inc., Lyden served as the Manager of Clinical and Statistical Affairs at Bausch and Lomb Pharmaceutical Division.

“It can be challenging to get young people interested in biostatistics.” said Lyden. “Biostatistics can be a very rewarding career and it is the goal of this panel to impart students contemplating a future in biostatistics with career possibilities, industry challenges and rewards that exist in our field.”

The discussion panel occurred on the first day of the SIBS six-week learning program. Undergraduate students from across the nation interested in pursuing a graduate program in Biostatistics enroll in the program to learn more about graduate studies and gain insight from biostatistics experts. Participants have access to the university’s computing systems and libraries and will also receive hands-on training from top biostaticians, clinicians and epidemiologists.

Following the discussion panel, the students were invited to a reception with the SIBS staff to kick off the six-week program. Upon completion of the program, students may transfer 3 college credits to their home institution.

Assistant Professor Dimitrios Vavylonis and graduate student Tyler Drake joined a University of Miami research team led by Associate Professor Fulvia Verde to learn that protein Cdc42 begins the ballet of proteins that change cell polarity, by oscillating throughout the cellular membrane of new cells. By changing polarity, Cdc42 regulates shape, structure and function in yeast cells. This oscillatory mechanism may be a general strategy among all self-organizing biological systems, not just simple yeast.

Researchers used fluorescent markers to tag each of the many proteins involved, observing the protein oscillate, switching sides about every five minutes. The fluctuations provide an adaptable mechanism for cells to control their size and structure in the fast-changing environment within.

The findings demonstrate just part of the complex process of cell growth and differentiation, but mark how advanced the science of biophysics has become. Only recently has the clear imaging and monitoring of protein activity become possible at the minute sizes and shortened time scales of individual cell maturation.

Now, researchers at Weill Cornell Medical College have made a discovery that once again forces us to revise the textbooks. This time, however, the findings pertain to RNA, which like DNA carries information about our genes and how they are expressed. The researchers have identified a novel base modification in RNA which they say will revolutionize our understanding of gene expression.

Their report, published in the journal Cell as Comprehensive Analysis of mRNA Methylation Reveals Enrichment in 3′ UTRs and near Stop Codons shows that messenger RNA (mRNA), long thought to be a simple blueprint for protein production, is often chemically modified by addition of a methyl group to one of its bases, adenine. Although mRNA was thought to contain only four nucleobases, their discovery shows that a fifth base, N6-methyladenosine (m6A), pervades the transcriptome. The researchers found that up to 20 percent of human mRNA is routinely methylated. Over 5,000 different mRNA molecules contain m6A, which means that this modification is likely to have widespread effects on how genes are expressed.

“This finding rewrites fundamental concepts of the composition of mRNA because, for 50 years, no one thought mRNA contained internal modifications that control function,” says the study’s senior investigator, Dr. Samie R. Jaffrey, an associate professor of pharmacology at Weill Cornell Medical College.

“We know that DNA and proteins are routinely modified by chemical switches that have profound effects on their function in both health and disease. But biologists believed mRNA was simply an intermediate between DNA and protein,” he says. “Now we know mRNA is much more complex, and defects in RNA methylation can lead to disease.”

Indeed, as part of the study, the researchers demonstrated that the obesity risk gene, FTO (fat mass and obesity-associated), encodes an enzyme capable of reversing this modification, converting m6A residues in mRNA back to regular adenosine. Humans with FTO mutations have an overactive FTO enzyme, which results in low levels of m6A and causes abnormalities in food intake and metabolism that lead to obesity.

The researchers uncovered links between m6A and other diseases as well.

“We found that m6A is present in many mRNAs encoded by genes linked to human diseases, including cancer as well as several brain disorders, such as autism, Alzheimer’s disease, and schizophrenia,” says the study’s lead investigator, Dr. Kate Meyer, a postdoctoral researcher in Dr. Jaffrey’s laboratory.

“Methylation in RNA is a reversible modification that appears to be a central step in a wide variety of biological pathways and physiological processes,” she says.

The first time that m6A was detected in mRNA was in 1975, but at the time scientists were unsure whether this finding was a result of contamination by other RNA molecules, Dr. Jaffrey says. Over 90 percent of RNA is either transfer RNA (tRNA) or ribosomal RNA (rRNA), cellular workhorses that are routinely modified.

But Dr. Jaffrey says he has always been interested in the idea that mRNA may be modified — “DNA, proteins, other forms of RNA are modified, so why not mRNA?” he says — so he and investigators in his laboratory developed a technique to help them uncover methylation in mRNA taken from both mouse and human samples.

They used two different antibodies that recognize and bind to m6A in mRNA in order to selectively isolate the mRNAs that contain m6A. By subjecting these mRNAs to next-generation sequencing, they were able to identify the sequence of each individual mRNA they had isolated. Co-authors Dr. Christopher Mason and Dr. Olivier Elemento, assistant professors from the Department of Physiology and Biophysics and Computational Genomics in Computational Biomedicine at Weill Cornell Medical College, then developed computational algorithms to reveal the identity of each of these methylated mRNAs.

The Weill Cornell researchers don’t know how the thousands of m6As they detected in humans work to control the function of mRNAs, but they do note that the m6As are located near “stop codons” in mRNA sequences. These areas signal the end of translation of the mRNA, suggesting that m6A might influence ribosomal function. “But we really don’t know yet,” says Dr. Mason, a co-lead investigator on the study. “It may allow other proteins to bind to mRNA, or subject these mRNAs to a whole new regulatory pathway. Our bioinformatics analyses are providing several hints about the possible impact of methylation on RNA function.”

Indeed, in their study, the investigators have already found that m6A sites frequently occur in regions of mRNA that are highly conserved across several species of vertebrates. “This shows that m6A sites are not just important for humans, but rather are maintained under selection across hundreds of millions of years of evolution, and thus are likely of critical importance for all animals,” Dr. Mason says.

“This is the first demonstration of an epitranscriptomic modification — alterations in RNA function that are not due to changes in the underlying sequence,” he adds.

“These findings are very, very exciting, and amazing, really, when you consider that mRNA has been around for so long and that nobody realized, in all this time, that they were being regulated in this way,” Dr. Jaffrey says. “It was right under our noses.”

In addition to investigating how m6A regulates mRNAs within cells, the researchers are now focused on identifying the enzymes and pathways that control mRNA methylation.

Their study already demonstrates that FTO is capable of reversing adenosine methylation and suggests that it acts on a large proportion of cellular mRNA. “FTO mutations are estimated to occur in one billion people worldwide and are a leading cause of obesity and type 2 diabetes. Our studies link m6A levels in mRNA to these major health problems and identify for the first time the mRNAs which are potentially targeted by FTO,” Dr. Meyer says.

The investigators are currently working to understand how defective regulation of m6A in patients with FTO mutations causes obesity and metabolic disorders, and they are also developing tests to rapidly identify compounds that inhibit FTO activity. These compounds are expected to inhibit the overactive FTO found in humans, potentially leading to novel therapeutics for diabetes and obesity.

Part of the difficulty in creating a vaccine against malaria is that it requires a system that can produce complex, three-dimensional proteins that resemble those made by the parasite, thus eliciting antibodies that disrupt malaria transmission. Most vaccines created by engineered bacteria are relatively simple proteins that stimulate the body’s immune system to produce antibodies against bacterial invaders. More complex proteins can be produced, but this requires an expensive process using mammalian cell cultures, and the proteins those cells produce are coated with sugars due to a chemical process called glycosylation.

“Malaria is caused by a parasite that makes complex proteins, but for whatever reason this parasite doesn’t put sugars on those proteins,” said Stephen Mayfield, a professor of biology at UC San Diego who headed the research effort. “If you have a protein covered with sugars and you inject it into somebody as a vaccine, the tendency is to make antibodies against the sugars, not the amino acid backbone of the protein from the invading organism you want to inhibit. Researchers have made vaccines without these sugars in bacteria and then tried to refold them into the correct three-dimensional configuration, but that’s an expensive proposition and it doesn’t work very well.”

Instead, the biologists looked to produce their proteins with the help of an edible green alga, Chlamydomonas reinhardtii, used widely in research laboratories as a genetic model organism, much like the fruit fly Drosophila and the bacterium E. coli. Two years ago, a UC San Diego team of biologists headed by Mayfield, who is also the director of the San Diego Center for Algae Biotechnology, a research consortium seeking to develop transportation fuels from algae, published a landmark study demonstrating that many complex human therapeutic proteins, such as monoclonal antibodies and growth hormones, could be produced by Chlamydomonas.

That got James Gregory, a postdoctoral researcher in Mayfield’s laboratory, wondering if a complex protein to protect against the malarial parasite could also be produced by Chlamydomonas. Two billion people live in regions where malaria is present, making the delivery of a malarial vaccine a costly and logistically difficult proposition, especially when that vaccine is expensive to produce. So the UC San Diego biologists set out to determine if this alga, an organism that can produce complex proteins very cheaply, could produce malaria proteins that would inhibit infections from malaria.

“It’s too costly to vaccinate two billion people using current technologies,” explained Mayfield. “Realistically, the only way a malaria vaccine will ever be used is if it can be produced at a fraction of the cost of current vaccines.  Algae have this potential because you can grow algae any place on the planet in ponds or even in bathtubs.”

Collaborating with Joseph Vinetz, a professor of medicine at UC San Diego and a leading expert in tropical diseases who has been working on developing vaccines against malaria, the researchers showed that the proteins produced by the algae, when injected into laboratory mice, made antibodies that blocked malaria transmission from mosquitoes.

“It’s hard to say if these proteins are perfect, but the antibodies to our algae-produced protein recognize the native proteins in malaria and, inside the mosquito, block the development of the malaria parasite so that the mosquito can’t transmit the disease,” said Gregory.

“This paper tells us two things: The proteins that we made here are viable vaccine candidates and that we at least have the opportunity to produce enough of this vaccine that we can think about inoculating two billion people,” said Mayfield. “In no other system could you even begin to think about that.”

The scientists, who filed a patent application on their discovery, said the next steps are to see if these algae proteins work to protect humans from malaria and then to determine if they can modifiy the proteins to elicit the same antibody response when the algae are eaten rather than injected.

Other UC San Diego scientists involved in the discovery were Fengwu Li from Vinetz’s laboratory and biologists Lauren Tomosada, Chesa Cox and Aaron Topol from Mayfield’s group. The basic technology that led to the development was supported by the Skaggs family. The research was supported by grants from the National Institute of Allergy and Infectious Diseases and the San Diego Foundation.  The California Energy Commission supported work on recombinant protein production for biofuels use, and this technology helped enabled these studies.

The PLoS ONE article can be accessed at: http://dx.plos.org/10.1371/journal.pone.0037179

“This work has major implications for modulating the fatty-acid profiles in plants, which is terribly important, not only to sustainable food production and nutrition but now also to biorenewable chemicals and fuels,” said Joseph Noel, a professor and director of the Jack H. Skirball Center for Chemical Biology and Proteomics at the Salk Institute.

“Because very high-energy molecules such as fatty acids are created in the plant using the energy of the sun, these types of molecules may ultimately provide the most cost-effective and efficient sources for biorenewable products,” added Eve Syrkin Wurtele, a professor of genetics, development and cell biology at Iowa State.

The analysis of gene activity (by the Iowa group) and determination of protein structures (by the Salk group) independently identified in the model plant thale cress (Arabidopsis thaliana) three related proteins that appear to be involved in fatty-acid metabolism. The Iowa and Salk researchers then joined forces to test this hypothesis, demonstrating a role of these proteins in regulating the amounts and types of fatty acids accumulated in plants. The researchers also showed that the action of the proteins is very sensitive to temperature and that this feature may play an important role in how plants mitigate temperature stress using fatty acids.

Although the researchers now understand that the three proteins – dubbed fatty-acid-binding proteins one, two and three, or FAP1, FAP2 and FAP3 – are involved in fatty-acid accumulation in plant tissues such as leaves and seeds, Wurtele said researchers still don’t understand the physical mechanism these proteins employ at the molecular level. That knowledge will ultimately allow the two collaborating research groups to predictably engineer better functions in plants.

“The proteins appear to be crucial missing links in the metabolism of fatty acids in Arabidopsis, and likely serve a similar function in other plant species since we find the same genes spread throughout the plant kingdom,” said Ryan Philippe, a post-doctoral researcher in Noel’s lab.

“If the researchers can understand precisely what role the proteins play in seed oil production,” said first author Michelle Ngaki, “they might be able to modify the proteins’ activity in new plant strains that produce more oil or higher quality oil than current crops.”

Further, if the three proteins help plants regulate stress, plant scientists might be able to exploit that trait to develop plants that are more resistant to stress, Wurtele said. And that could allow farmers to grow crops for biorenewable fuels and chemicals on marginal land that’s not suited for food crops.

All of this, she said, could point to new directions in biological studies.

“We are entering the age of predictive biology,” Wurtele said. “That means harnessing computational approaches to deduce gene function, model biological processes and predict the consequences of altering a single gene to the complex biological network of an organism.”

The CNIO team, in collaboration with Eduard Ayuso and Fátima Bosch of the Centre of Animal Biotechnology and Gene Therapy at the Universitat Autònoma de Barcelona (UAB), treated adult (one‐year‐old) and aged (two‐year‐old) mice, with the gene therapy delivering a “rejuvenating” effect in both cases, according to the authors.

Mice treated at the age of one lived longer by 24% on average, and those treated at the age of two, by 13%. The therapy, furthermore, produced an appreciable improvement in the animals’ health, delaying the onset of age‐related diseases – like osteoporosis and insulin resistance – and achieving improved readings on aging indicators like neuromuscular coordination.

The gene therapy consisted of treating the animals with a DNA-­modified virus, the viral genes having been replaced by those of the telomerase enzyme, with a key role in aging. Telomerase repairs the extreme ends or tips of chromosomes, known as telomeres, and in doing so slows the cell’s and therefore the body’s biological clock. When the animal is infected, the virus acts as a vehicle depositing the telomerase gene in the cells.

This study “shows that it is possible to develop a telomerase-­based anti-­aging gene therapy without increasing the incidence of cancer,” the authors affirm. “Aged organisms accumulate damage in their DNA due to telomere shortening, [this study] finds that a gene therapy based on telomerase production can repair or delay this kind of damage,” they add.

‘Resetting’ the biological clock

Telomeres are the caps that protect the end of chromosomes, but they cannot do so indefinitely: each time the cell divides the telomeres get shorter, until they are so short that they lose all functionality. The cell, as a result, stops dividing and ages or dies. Telomerase gets around this by preventing telomeres from shortening or even rebuilding them. What it does, in essence, is stop or reset the cell’s biological clock.

But in most cells the telomerase gene is only active before birth; the cells of an adult organism, with few exceptions, have no telomerase. The exceptions in question are adult stem cells and cancer cells, which divide limitlessly and are therefore immortal — in fact several studies have shown that telomerase expression is the key to the immortality of tumour cells.

It is precisely this risk of promoting tumour development that has set back the investigation of telomerase­‐based anti­‐aging therapies.

In 2007, Blasco’s group demonstrated that it was feasible to prolong the lives of transgenic mice, whose genome had been permanently altered at the embryonic stage, by causing their cells to express telomerase and, also, extra copies of cancer­‐resistant genes. These animals live 40% longer than normal and do not develop cancer.

The mice subjected to the gene therapy now under test are likewise free of cancer. Researchers believe this is because the therapy begins when the animals are adult so do not have time to accumulate sufficient number of aberrant divisions for tumors to appear.

Also important is the kind of virus employed to carry the telomerase gene to the cells. The authors selected demonstrably safe viruses that have been successfully used in gene therapy treatment of hemophilia and eye disease. Specifically, they are non-­‐replicating viruses derived from others that are non-­‐pathogenic in humans.

This study is viewed primarily as “a proof-­‐of-­‐principle that telomerase gene therapy is a feasible and generally safe approach to improve healthspan and treat disorders associated with short telomeres,” state Virginia Boccardi (Second University of Naples) and Utz Herbig (New Jersey Medical School-­‐University Hospital Cancer Centre) in a commentary published in the same journal.

Although this therapy may not find application as an anti‐aging treatment in humans, in the short term at least, it could open up a new treatment option for ailments linked with the presence in tissue of abnormally short telomeres, as in some cases of human pulmonary fibrosis.

As Blasco says, “aging is not currently regarded as a disease, but researchers tend increasingly to view it as the common origin of conditions like insulin resistance or cardiovascular disease, whose incidence rises with age. In treating cell aging, we could prevent these diseases.”

With regard to the therapy under testing, Bosch explains: “Because the vector we use expresses the target gene (telomerase) over a long period, we were able to apply a single treatment. This might be the only practical solution for an anti‐aging therapy, since other strategies would require the drug to be administered over the patient’s lifetime, multiplying the risk of adverse effects.”

The device, which could be several hundred times more sensitive than other biosensors, combines the attributes of two distinctly different types of sensors, said Muhammad A. Alam, a Purdue University professor of electrical and computer engineering.

“Individually, both of these types of biosensors have limited sensitivity, but when you combine the two you get something that is better than either,” he said.

Findings are detailed in a paper appearing Monday (May 14) in the Proceedings of the National Academy of Sciences. The paper was written by Purdue graduate student Ankit Jain, Alam and Pradeep R. Nair, a former Purdue doctoral student who is now a faculty member at the Indian Institute of Technology, Bombay.

The device – called a Flexure-FET biosensor – combines a mechanical sensor, which identifies a biomolecule based on its mass or size, with an electrical sensor that identifies molecules based on their electrical charge. The new sensor detects both charged and uncharged biomolecules, allowing a broader range of applications than either type of sensor alone.

The sensor has two potential applications: personalized medicine, in which an inventory of proteins and DNA is recorded for individual patients to make more precise diagnostics and treatment decisions; and the early detection of cancer and other diseases.

In early cancer diagnostics, the sensor makes possible the detection of small quantities of DNA fragments and proteins deformed by cancer long before the disease is visible through imaging or other methods, Alam said.

The sensor’s mechanical part is a vibrating cantilever, a sliver of silicon that resembles a tiny diving board. Located under the cantilever is a transistor, which is the sensor’s electrical part.

In other mechanical biosensors, a laser measures the vibrating frequency or deflection of the cantilever, which changes depending on what type of biomolecule lands on the cantilever. Instead of using a laser, the new sensor uses the transistor to measure the vibration or deflection.

The sensor maximizes sensitivity by putting both the cantilever and transistor in a “bias.” The cantilever is biased using an electric field to pull it downward as though with an invisible string.

“This pre-bending increases the sensitivity significantly,” Jain said.

The transistor is biased by applying a voltage, maximizing its performance as well.

“You can make the device sensitive to almost any molecule as long as you configure the sensor properly,” Alam said.

A key innovation is the elimination of a component called a “reference electrode,” which is required for conventional electrical biosensors but cannot be miniaturized, limiting practical applications.

“Eliminating the need for a reference electrode enables miniaturization and makes it feasible for low-cost, point-of-care applications in doctors’ offices,” Alam said.

The study is the first example of using bone cell progenitors derived from human embryonic stem cells to grow compact bone tissue in quantities large enough to repair centimeter-sized defects. When implanted in mice and studied over time, the implanted bone tissue supported blood vessel ingrowth, and continued development of normal bone structure, without demonstrating any incidence of tumor growth.

Dr. Marolt’s work is a significant step forward in using pluripotent stem cells to repair and replace bone tissue in patients. Bone replacement therapies are relevant in treating patients with a variety of conditions, including wounded military personnel, patients with birth defects, or patients who have suffered other traumatic injury.

Since conducting this work as proof of principle at Columbia University, Dr. Marolt has continued to build upon this research as an Investigator in the NYSCF Laboratory, developing bone grafts from induced pluripotent stem (iPS) cells. iPS cells are similar to embryonic stem cells in that they can also give rise to nearly any type of cell in the body, but iPS cells are produced from adult cells and as such are individualized to each patient. By using iPS cells rather than embryonic stem cells to engineer tissue, Dr. Marolt hopes to develop personalized bone grafts that will avoid immune rejection and other implant complications.