Category Archives: Biochemistry

BUFFALO, N.Y A new study by University at Buffalo researchers has revealed that the absence of a single interaction within a brain receptor reduces its activity. The discovery advances the understanding of how certain brain diseases arise, and could lead to developing precision medicines for treating them.

The study was published Dec. 31 in Proceedings of the National Academy of Sciences by senior authors Gabriela K. Popescu, PhD, professor of biochemistry in the Jacobs School of Medicine and Biomedical Sciences at UB, and Wenjun Zheng, PhD, UB professor of physics in the College of Arts and Sciences; first authors are Gary Iacobucci, PhD, a postdoctoral fellow in Popescus lab, and Han Wen, a doctoral candidate in Zhengs lab.

The research builds on more than a decade of work by Popescu, who studies the brains NMDA (N-methyl-D-aspartate) receptors. Mutations in this protein, which is critical to learning and memory, can result in neuropsychiatric diseases, from epilepsy to schizophrenia. Such mutations are rare and have only been discovered in the past 10 years.

Popescus work focuses on how subtle changes in these key receptors cause them to produce altered electrical signals, which in turn, affect how well the brain functions.

The work describes for the first time an open form of the NMDA receptor and identifies a direct interaction between two amino acid residues. This interaction forms only in the open receptor and helps it stay open for longer, a finding that has clinical implications.

Cycling repeatedly through its open and closed forms is the main business of NMDA receptors, explained Popescu, and the amount of time that the receptors stay open or closed determines the strength and duration of the electrical signal they produce when stimulated.

Excitability levels

The electricity generated by the opening and closing of the receptors, in turn, determines a neurons level of excitability, which has direct clinical consequences. Too much excitability can mean epilepsy, seizures or neurodegeneration, whereas too little can result in schizophrenia and other cognitive disorders, she said.

Until now, the structure of an open form of the NMDA receptor was unknown. To date, the literature has reported only atomic structures for juvenile NMDA receptors, present in young mammals or young neurons, and these are believed to represent a closed form of the receptor.

In previous work, Popescu collaborated with UB co-authors Wen and Zheng to develop a model of how the predominant NMDA receptor protein in the adult brain might look.

In the current paper, the two teams built upon that work and used molecular dynamics simulation to force the closed adult receptor to open. This was accomplished with the use of supercomputing power through UB's Center for Computational Research and mathematical algorithms developed in the Zheng lab.

First clue

This simulated open structure is the first clue to how the internal organization of these receptors may change when they open, said Popescu.

When they compared the positions of atoms between the closed and open NMDA receptor structures, the researchers were able to identify several locations where two amino acid residues had moved closer together, suggesting that they were engaging in a new interaction.

When people have receptors that cannot form this interaction, their receptors and synapses are more sluggish, not as active, said Popescu. The observations in this paper are consistent with symptoms observed in patients whose receptors lack this interaction due to spontaneous mutation of one of the residues we identified here as important.

She noted that precision medicine for NMDA receptors is still in its infancy and the U.S. Food and Drug Administration has only approved a few drugs that work on these receptors.

Functional studies like this will help us better understand how the various mutations affect receptor function and which therapy to try, said Popescu.

Next steps

The researchers will continue to collaborate to better understand not just open and closed NMDA receptors, but also their intermediary conformations. Large genome sequencing studies will also be crucial in identifying the spectrum of mutations in people and revealing how specific mutations lead to characteristic symptoms.

By marrying advances in structure determination with new discoveries on the clinical significance of mutations, we will be able to more easily accomplish what we did in this paper: explain how a single, subtle change in a protein changes its function, Popescu concluded. Based on this information, other experts can ask more directed questions as to what are the consequences of this protein dysfunction for cellular and brain physiology, and ultimately for human behaviors, and finally, what pharmacologic approaches can one take to restore function?

Co-authors are Beiying Liu, PhD, research scientist in the Department of Biochemistry and Matthew Helou, a UB undergraduate biochemistry major.

The research was funded by the National Institutes of Health.

Continued here:
Discovery of a new form of a brain protein has clinical implications - UB News Center

Newswise TAMPA, Fla. The hallmarks of cancer include rapid cell reproduction and metabolic activity. But these processes also lead to increased cellular stress and oxidation, and the risk of cell death. To circumvent these negative consequences of supercharged growth, cancer cells stimulate pathways to reduce oxidative stress and avoid cell death. In an article published in Cell Metabolism, Moffitt Cancer Center researchers report on a newly discovered biochemical pathway that protects cells from a type of cell death called ferroptosis.

Ferroptosis is a specialized type of cell death that is caused by imbalances in oxidation within cells. Ferroptosis results in changes to molecules in the cell membrane called lipids and can be caused by cysteine starvation. Cysteine is a type of amino acid that is one of the building blocks of proteins and is also used by the body for numerous important physiological processes, including cell survival, regulation of oxidative-reduction reactions and energy transfer. Because of its critical role in normal processes, cysteine is highly regulated to prevent excess or insufficient amounts of the amino acid.

Several different types of cancer overexpress molecules that play an important role in cysteine regulation. This suggests that reducing cysteine levels may negatively affect cancer growth. In fact, studies have shown that cancer cells can be induced to undergo cell death by either inhibiting cysteine uptake or starving cells of cysteine. However, the downstream processes that are stimulated by cysteine starvation are unclear. Moffitt researchers performed a series of laboratory investigations to learn what molecules become activated after cysteine deprivation and how this impacts cells.

The researchers discovered that cancer cells can activate signaling pathways to protect themselves against cell death due to cysteine starvation. When the team starved non-small cell lung carcinoma cells of cysteine, the cells began to undergo ferroptosis. However, cysteine starvation also resulted in an unexpected accumulation of small molecules called -glutamyl-peptides, which protected the cells against ferroptosis. The researchers found that the peptides were synthesized through the activity of the protein GCLC. Under normal conditions, GCLC is involved in the first step of the synthesis of the antioxidant glutathione from the amino acids cysteine and glutamate. However, this newly discovered activity of GCLC occurred in the absence of cysteine and was important to limit both glutamate accumulation and oxidant production.

The researchers further analyzed signaling mechanisms controlling GCLC-mediated peptide synthesis and discovered that GCLC was regulated by the protein NRF2. They found that under normal conditions, NRF2 regulated GCLC to produce glutathione, but under cysteine-starved conditions, NRF2 regulated GGLC to produce -glutamyl-peptides.

NRF2 is known to play an important role in the protection against cellular oxidation and is often deregulated in lung cancer, said lead author Gina DeNicola, Ph.D., assistant member of the Cancer Physiology Department at Moffitt. The ability of NRF2 to protect against ferroptosis has important implications for cancer, particularly lung cancers that commonly have NRF2 activation via mutations in KEAP1 and NRF2.

This work was supported the National Institutes of Health (R37 CA230042, R01 DK123738, R01 CA189623, P30 CA076292), the AACR-Takeda Oncology Lung Cancer Research Fellowship (19-40-38-KANG ), the National Pancreas Foundation, a Florida Bankhead-Coley grant, and a Miles for Moffitt award and additional funding from the Moffitt Foundation.

About Moffitt Cancer Center Moffitt is dedicated to one lifesaving mission: to contribute to the prevention and cure of cancer. The Tampa-based facility is one of only 51 National Cancer Institute-designated Comprehensive Cancer Centers, a distinction that recognizes Moffitts scientific excellence, multidisciplinary research, and robust training and education. Moffitt is the No. 11 cancer hospital and has been nationally ranked by U.S. News & World Report since 1999. Moffitts expert nursing staff is recognized by the American Nurses Credentialing Center with Magnet status, its highest distinction. With more than 7,000 team members, Moffitt has an economic impact in the state of $2.4 billion. For more information, call 1-888-MOFFITT (1-888-663-3488), visit MOFFITT.org, and follow the momentum on Facebook, Twitter, Instagram and YouTube.

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Continue reading here:
Moffitt Researchers Discover Biochemical Pathway That Protects Cells from Ferroptosis Cell Death - Newswise

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Automatic Biochemistry Analyzers Market Size By Analysis, Key Vendors, Regions, Type and Application, and Forecasts to 2027 - NeighborWebSJ

A new study by UB researchers has revealed that the absence of a single interaction within a brain receptor reduces its activity. The discovery advances understanding of how certain brain diseases arise, and could lead to developing precision medicines for treating them.

The study was published Dec. 31 in Proceedings of the National Academy of Sciences by senior authors Gabriela K. Popescu, professor of biochemistry in the Jacobs School of Medicine and Biomedical Sciences at UB, and Wenjun Zheng, professor of physics in the College of Arts and Sciences; first authors are Gary Iacobucci, a postdoctoral fellow in Popescus lab, and Han Wen, a doctoral candidate in Zhengs lab.

The research builds on more than a decade of work by Popescu, who studies the brains NMDA (N-methyl-D-aspartate) receptors. Mutations in this protein, which is critical to learning and memory, can result in neuropsychiatric diseases, from epilepsy to schizophrenia. Such mutations are rare and have only been discovered in the past 10 years.

Popescus work focuses on how subtle changes in these key receptors cause them to produce altered electrical signals, which in turn, affect how well the brain functions.

The work describes for the first time an open form of the NMDA receptor and identifies a direct interaction between two amino acid residues. This interaction forms only in the open receptor and helps it stay open for longer, a finding that has clinical implications.

Cycling repeatedly through its open and closed forms is the main business of NMDA receptors, Popescu explains, and the amount of time that the receptors stay open or closed determines the strength and duration of the electrical signal they produce when stimulated.

The electricity generated by the opening and closing of the receptors, in turn, determines a neurons level of excitability, which has direct clinical consequences. Too much excitability can mean epilepsy, seizures or neurodegeneration, whereas too little can result in schizophrenia and other cognitive disorders, she says.

Until now, the structure of an open form of the NMDA receptor was unknown. To date, the literature has reported only atomic structures for juvenile NMDA receptors, present in young mammals or young neurons, and these are believed to represent a closed form of the receptor.

In previous work, Popescu collaborated with UB co-authors Wen and Zheng to develop a model of how the predominant NMDA receptor protein in the adult brain might look.

In the current paper, the two teams built upon that work and used molecular dynamics simulation to force the closed adult receptor to open. This was accomplished with the use of supercomputing power through UBs Center for Computational Research and mathematical algorithms developed in the Zheng lab.

This simulated open structure is the first clue to how the internal organization of these receptors may change when they open, Popescu says.

When they compared the positions of atoms between the closed and open NMDA receptor structures, the researchers were able to identify several locations where two amino acid residues had moved closer together, suggesting that they were engaging in a new interaction.

When people have receptors that cannot form this interaction, their receptors and synapses are more sluggish, not as active, Popescu says. The observations in this paper are consistent with symptoms observed in patients whose receptors lack this interaction due to spontaneous mutation of one of the residues we identified here as important.

She notes that precision medicine for NMDA receptors is still in its infancy and the U.S. Food and Drug Administration has only approved a few drugs that work on these receptors.

Functional studies like this will help us better understand how the various mutations affect receptor function and which therapy to try, she says.

The researchers will continue to collaborate to better understand not just open and closed NMDA receptors, but also their intermediary conformations. Large genome sequencing studies will also be crucial in identifying the spectrum of mutations in people and revealing how specific mutations lead to characteristic symptoms.

By marrying advances in structure determination with new discoveries on the clinical significance of mutations, we will be able to more easily accomplish what we did in this paper: explain how a single, subtle change in a protein changes its function, Popescu concludes. Based on this information, other experts can ask more directed questions as to what are the consequences of this protein dysfunction for cellular and brain physiology, and ultimately for human behaviors, and finally, what pharmacologic approaches can one take to restore function?

Co-authors are Beiying Liu, research scientist in the Department of Biochemistry, and Matthew Helou, a UB undergraduate biochemistry major.

The research was funded by the National Institutes of Health.

Continued here:
Discovery of new form of brain protein has clinical implications - UB Now: News and views for UB faculty and staff - University at Buffalo Reporter

Newswise DALLAS Jan. 13, 2020 Benjamin Tu, Ph.D., a professor of biochemistry at UT Southwestern whose basic science research into cellular function could lead to greater understanding of diseases including cancer, has been named a recipient of the 2021 Edith and Peter ODonnell Award in Science, presented by The Academy of Medicine, Engineering and Science of Texas (TAMEST).

TAMEST presents the annual awards to recognize the achievements of early career Texas investigators in the fields of science, medicine, engineering, and technology innovation. This years awards were announced today during the final day of its annual conference, which was held virtually. The awards come with a $25,000 honorarium and an invitation to make a presentation before TAMEST members. Tu will make his virtual presentation Feb. 24.

Tu is the 15th scientist at UT Southwestern to receive the award since TAMEST initiated the ODonnell Awards in 2006.

Its an honor to be selected, Tu says of the prize. It was certainly welcome news during very challenging times.

The Edith and Peter ODonnell Awards are given to scientists for their contributions addressing the essential role that science and technology play in society, and whose work meets the highest standards of exemplary professional performance, creativity and resourcefulness, according to TAMEST.

We believe Dr. Tus research will lead to future therapeutic advancements for diseases, saysDavid E. Daniel, Ph.D. (NAE), 2021TAMESTboard president.As a pioneer in his field, we are honored to recognize him as the recipient of our 2021 ODonnell Award in Science and are grateful for the discoveries he is making here in Texas that will impact the rest of the world.

Margaret Phillips, Ph.D., professor and chair of biochemistry, nominated Tu for the award. Ben is an incredibly talented scientist, Phillips says. You could almost see him as a detective. He digs into the nuts and bolts of how cells are functioning and regulating themselves.

Tus research focuses on how metabolism regulates cellular functions. Two of his recent areas of investigation have obvious potential for future advances in clinical treatment.

In two 2019 studies, both published inCell, Tu reported that ataxin-2, a protein with a known link to ALS, or Lou Gehrigs disease, is necessary for cells to do the work of clearing out damaged or unneeded parts in a process known as autophagy. Without the protein, cells are more likely to die, he said

In a2011 study published in Molecular Cell, Tu described how the metabolite acetyl-CoA plays a key role in turning on the genes necessary for cell growth.

At the time, few scientists accepted the idea that a metabolite could have such an important role in regulating gene expression, says Tu. Historically, the field had thought that transcription factors (proteins involved in transcribing the genetic information contained in DNA) dictate what genes are turned on.

This new understanding of the importance of acetyl-CoA led to further research by Tu and a 2014Cellpaper that reported how the metabolite might be important for the survival and growth of liver cancer cells. His current research in mice will investigate if chemicals that inhibit acetyl-CoA might slow the growth of pancreatic cancer cells.

Tu came to UT Southwestern in 2004 after receiving masters and bachelors degrees in chemistry from Harvard University and a Ph.D. in biochemistry and biophysics from the University of California, San Francisco. He worked as a postdoctoral fellow under Steven McKnight, Ph.D., professor of biochemistry, before joining the UTSW faculty as an assistant professor of biochemistry in 2007. Tu holds the Martha Steiner Professorship in Medical Research, and is a W.W. Caruth, Jr. Scholar in Biomedical Research.

His previous honors include the Norman Hackerman Award in Chemical Research from The Welch Foundation in 2014 and recognition as a three-time finalist for the prestigious Blavatnik Awards for Young Scientists in 2017, 2018, and 2019. He is also a UT Southwestern Presidential Scholar.

TAMEST, founded in 2004 by then-U.S. Sen. Kay Bailey Hutchison and two Texas Nobel Laureates Michael Brown, M.D., of UT Southwestern, and Richard E. Smalley, Ph.D., of Rice University strives to bring together the states brightest minds. Members include the Texas-based members of the National Academies of Medicine, Engineering, and Sciences; the Royal Society; and Texas 11 Nobel Laureates.

About UTSouthwestern Medical Center

UTSouthwestern, one of the premier academic medical centers in the nation, integrates pioneering biomedical research with exceptional clinical care and education. The institutions faculty has received six Nobel Prizes, and includes 23 members of the National Academy of Sciences, 17 members of the National Academy of Medicine, and 13 Howard Hughes Medical Institute Investigators. The full-time faculty of more than 2,500 is responsible for groundbreaking medical advances and is committed to translating science-driven research quickly to new clinical treatments. UTSouthwestern physicians provide care in about 80 specialties to more than 105,000 hospitalized patients, nearly 370,000 emergency room cases, and oversee approximately 3 million outpatient visits a year.

Continued here:
Biochemist Benjamin Tu Honored With ODonnell Award From TAMEST - Newswise

Illinois State sophomore Gavin Long has always had an inner-Dr. Alan Grant.

Jurassic Park was the first movie he remembered watching as a child, andas he put itdinosaurs were always in his brain. The Steven Spielberg film uncovered his love for science.

It never really went away, Long said.

Growing up in Lincoln Woods, Long wanted to go into sciencegeology in particularbut wasnt sure how his path would look. If pursuing a college education was an option, hed have to dedicate quite a bit of time to part-time work for financial support. And that would significantly eat into the time it would take to become deeply invested in scientific study.

Illinois State University has an answer for students like Long.

In 2018as part of a working partnership with Heartland Community College and Illinois Wesleyan University, the four-year NexSTEM scholarship became available to students who were Pell Grant eligible. That allowed them to pursue community-based research opportunities in science and mathematics with much of the financial burden lifted.

The National Science Foundation awarded a $4.6 million grant to the three-school consortium on a five-year timeline. Nearly $2.8 million went to scholarships, and the other $1.8 million involved research projects for students who may not have the means to find such opportunities within the field.

If you look at the STEM population across the U.S., they are not people who come from a low socio-economic background, said Dr. Sheri Glowinski, director of the NexSTEM program since 2019. There is still a lot of work to do, and the original team wanted to make STEM accessible to people regardless of what their backgrounds are.

There are currently 39 students18 from Illinois Statewho are NexSTEM scholars. Recipients get up to $10,000 per year to help cover the costs of higher education. The program is intended to diversify and grow the pool of STEM professionals.

Its helped me greatly, said freshman Amy Le, a biochemistry major from Peoria. Her research project explores the effects of antibiotics on UV radiation. It covers most of my college tuition, which is why I decided to go to Illinois State, and it made the process of going to college a lot easier because I dont have to also worry about my financial situation.

Student applicants must complete a trio of essays explaining their interests in the field, a STEM project they found particularly challenging and their growth from that, and a little bit about themselves. The selection committee is especially interested in students overcoming obstacles. Glowinski said that answer is a strong indicator of problem-solving skills and determination, two vital components in the STEM field.

I want this to state something. This is going to last longer than my four years.

Recipients are then paired with faculty mentors and sometimes other peers to conduct research opportunities that are based on benefiting the community while advancing scientific knowledge. The opportunity also gives students a significant leg up to be able complete research so early on in their college careers. Glowinski said very few schools in the U.S. provide that to incoming students in an authentic way.

Long has been working with Dr. David Malone to try and find rare elements in car batteries. He noted how important it is to find domestic sources since more than 90 percent of those elements are imported from China.

Its just a great opportunity to get something under my belt, Long said. Any experience is good experience and learning things about geology, maybe Ill find something I prefer to do and potentially help more people.

NexSTEM scholars take great pride in being the first recipients of the program. They not only work to advance their own interests and careers, but also to pay it forward for others who faced the same challenges.

Sophomore actuarial sciences major Tyler Deters and Othniel Carr have been looking into trends of the annuity market. Just seeing the math behind business is kind of cool, and Im appreciative of that aspect of that project, Deters explained. Aside from his own project, Deters and a few of his peers have set up tutoring sessions for fellow student mathematicians.

He knows he will forever have NexSTEM scholar attached to his name. He aspires to continue pushing boundaries by not only making the most of his opportunity, but to inspire students behind him.

I want this to state something, said Deters, who is from Teutopolis. This is going to last longer than my four years.

The NexSTEM committee will ask for an extension of the grant, and Glowinski expects to have 10 more students per school in the upcoming year. COVID-19 has challenged some of the recruiting efforts, but she hopes the program can continue to provide more and more Central Illinois students an opportunity to chase their own visionswhether they are inspired by fictitious dinosaur excursions or something else.

Shes seen remarkable work from the recipients so far and looks forward to watching them grow.

It is incredibly inspiring to see them embrace this, she said. They are embracing all of the course work they are taking and other extra-curriculars. They are doing all of this and still learning in the process. To me, thats amazing.

To see research presentations on video, visit NexSTEMs website.

Check out more scholarship opportunities at Illinois State.

Read more:
Building the future: NexSTEM program aims to diversify math, science, and technology fields - Illinois State University News