Professor Thomas Chiles of the Biology Department, and colleagues at Boston University Medical Center, have been awarded a five-year, multimillion-dollar program project grant from the National Institutes of Allergy and Infectious Disease of the National Institutes of Health (NIH).
Their research will focus on understanding the growth and differentiation of a small subset of white blood cells called B-1a lymphocytes (B-1a cells). B-1a cells, which are found in the peritoneal cavity, and B-2 cells, which are located in the spleen and lymph nodes, help destroy pathogens that enter the body, and then help the body acquire immunity against those particular pathogens, protecting the body from future invasion. However, an over-production of B-1a cells can lead to autoimmune diseases and leukemias.
Thomas Chiles's group at Boston College, working with Dr. Thomas Rothstein of Boston University's Department of Medicine, previously demonstrated that the rules that govern cell cycle control and differentiation to immunoglobulin-secreting plasma cells are different in B-1a cells than in B-2 cells.
As part of the new NIH-funded program project, research carried out at Boston College will seek to better understand the molecular mechanisms that control when B-1a cells enter the cell cycle and proliferate. Insights from these studies will help us understand the molecular basis of several human lymphoproliferative disorders associated with B-1a cells, including a form of cancer called chronic lymphocytic leukemia.
Chronic lymphocytic leukemia, which involves overproduction of white blood cells by the bone marrow, is the most common type of leukemia in adults.
To learn more about research going on in the Chiles Laboratory, please visit:
bc/schools/cas/biology/facadmin/chiles/
BY JOHN P. ROCHE
Maintained: Biology Department
URL: bc/schools/cas/biology/news/chiles/
© 2004 The Trustees of Boston College
понедельник, 24 октября 2011 г.
пятница, 21 октября 2011 г.
New Book Uses ABCs To Teach Children Microbiology
A new children's book from ASM Press uses the familiar genre of the ABC book to introduce readers to the not-so-familiar world of microbes. The Invisible ABCs will delight readers of all ages with its colorful presentation and spectacular selection of illustrations. Intended for school-age children and younger, this unique new book will stimulate parents, teachers, librarians, and even older students to discover the fascinating world of microorganisms.
"We are immersed in microbes. They live in our bodies, in our food, and in everything that surrounds us; we cannot live without them. The Invisible ABCs presents answers to questions that we all have an interest in, such as 'Why can cows use grass for food but humans can't?' and 'Why do we get gas after we eat beans?'" says author Rodney Anderson, a microbiologist and professor at Ohio Northern University, who presents photos he has collected of microorganisms shaped like letters of the alphabet to illustrate the significant role microbes play in our daily lives.
This intriguing book contains a glossary of important terms, as well as endpapers illustrating the relative size of organisms from viruses to whales. Age-appropriate vocabulary and examples are used to communicate important scientific principles and concepts throughout the vibrant pages of The Invisible ABCs. A companion website provides deeper understanding for those who seek to learn more about microorganisms.
The Invisible ABCs can be purchased through ASM Press online at estore.asm/ or through other online retailers.
ASM Press is the book publishing arm of the American Society for Microbiology (ASM), the oldest and largest single life science membership organization in the world. The ASM's mission is to promote research in the microbiological sciences and to assist communication between scientists, policy makers, and the public to improve health and foster economic well-being.
Contact: Jim Sliwa
American Society for Microbiology
"We are immersed in microbes. They live in our bodies, in our food, and in everything that surrounds us; we cannot live without them. The Invisible ABCs presents answers to questions that we all have an interest in, such as 'Why can cows use grass for food but humans can't?' and 'Why do we get gas after we eat beans?'" says author Rodney Anderson, a microbiologist and professor at Ohio Northern University, who presents photos he has collected of microorganisms shaped like letters of the alphabet to illustrate the significant role microbes play in our daily lives.
This intriguing book contains a glossary of important terms, as well as endpapers illustrating the relative size of organisms from viruses to whales. Age-appropriate vocabulary and examples are used to communicate important scientific principles and concepts throughout the vibrant pages of The Invisible ABCs. A companion website provides deeper understanding for those who seek to learn more about microorganisms.
The Invisible ABCs can be purchased through ASM Press online at estore.asm/ or through other online retailers.
ASM Press is the book publishing arm of the American Society for Microbiology (ASM), the oldest and largest single life science membership organization in the world. The ASM's mission is to promote research in the microbiological sciences and to assist communication between scientists, policy makers, and the public to improve health and foster economic well-being.
Contact: Jim Sliwa
American Society for Microbiology
вторник, 18 октября 2011 г.
Worldwide Research Archive Doubles In Size Since 2004
The Protein Data Bank this month reached a significant milestone in its 37-year history as the 50,000th molecule structure was released into its archive, joining other structures vital to pharmacology, bioinformatics, and education.
With its origins in a handwritten petition circulated at a scientific meeting, the PDB is the single worldwide repository for the three-dimensional structures of large molecules and nucleic acids. This freely available online library allows biological researchers and students to study, store and share molecular information on a global scale. Officially founded in 1971 with seven structures at Brookhaven National Laboratory, the archive is currently managed by a consortium called the worldwide Protein Data Bank (wwPDB).
Today, the PDB archive receives approximately 25 new experimentally-determined structures from scientists each day - and more than 5 million files are downloaded from the PDB archive every month. Users include structural biologists, computational biologists, biochemists, and molecular biologists in academia, government, and industry as well as educators and students.
Notable examples include recent structures of the adrenergic receptor, which will revolutionize the discovery of drugs to fight heart disease, allergies, and numerous other diseases, and the many structures of enzymes from HIV, which have been pivotal in the design of new therapies to fight AIDS.
"Advances in science and technology have helped the archive grow by leaps and bounds in the last 10 years," said Dr. Helen M. Berman, director of the RCSB PDB and Board of Governors professor of chemistry and chemical biology, noting that the size of the PDB has doubled in just the last three-and-a-half years.
"We are estimating that the PDB will not only double, but triple to 150,000 structures by 2014," said Dr. Philip E. Bourne, Associate Director of the RCSB PDB and professor of pharmacology at the UCSD Skaggs School of Pharmacy and Pharmaceutical Sciences.
The RCSB PDB is based at Rutgers University in New Jersey, and the San Diego Supercomputer Center (SDSC) and Skaggs School of Pharmacy and Pharmaceutical Sciences at the University of California at San Diego. Bourne, a distinguished scientist with SDSC, has been leveraging the resources of the supercomputer center to create a highly uniform and robust process for archiving and providing access to the molecular structures.
The RCSB PDB is responsible for releasing PDB entries into the archive after they have been reviewed and annotated. At Rutgers, RCSB PDB members annotate structures and develop the sophisticated infrastructure needed to handle these complex data. The primary PDB FTP site is based at SDSC, which serves as the distribution point for PDB users. In addition to the SDSC site, there are failover sites at both the UCSD Skaggs School and Rutgers University to ensure constant access.
In addition to a comprehensive website and database that lets users search, analyze, and visualize the structures of biological macromolecules and their relationships to sequence, function, and disease, the RCSB PDB features a Molecule of the Month series, which recently published its 100th installment. Proteins, one of the main building blocks for living organisms, come in a variety of shapes, with the form of a protein corresponding to its function. The structures housed in the PDB demonstrate great diversity in size, complexity, and function, including:
Insulin, the protein deficient in diabetic patients
p53 tumor suppressor, a protein often implicated in cancer
Anthrax toxin, the disease-causing protein made by anthrax
Amyloid peptide, a protein implicated in Alzheimer's disease
The RCSB PDB is supported by funds from the National Science Foundation, the National Institute of General Medical Sciences, the Office of Science, the Department of Energy, the National Library of Medicine, the National Cancer Institute, the National Center for Research Resources, the National Institute of Biomedical Imaging and Bioengineering, the National Institute of Neurological Disorders and Stroke, and the National Institute of Diabetes & Digestive & Kidney Diseases.
Source: Jan Zverina
University of California - San Diego
With its origins in a handwritten petition circulated at a scientific meeting, the PDB is the single worldwide repository for the three-dimensional structures of large molecules and nucleic acids. This freely available online library allows biological researchers and students to study, store and share molecular information on a global scale. Officially founded in 1971 with seven structures at Brookhaven National Laboratory, the archive is currently managed by a consortium called the worldwide Protein Data Bank (wwPDB).
Today, the PDB archive receives approximately 25 new experimentally-determined structures from scientists each day - and more than 5 million files are downloaded from the PDB archive every month. Users include structural biologists, computational biologists, biochemists, and molecular biologists in academia, government, and industry as well as educators and students.
Notable examples include recent structures of the adrenergic receptor, which will revolutionize the discovery of drugs to fight heart disease, allergies, and numerous other diseases, and the many structures of enzymes from HIV, which have been pivotal in the design of new therapies to fight AIDS.
"Advances in science and technology have helped the archive grow by leaps and bounds in the last 10 years," said Dr. Helen M. Berman, director of the RCSB PDB and Board of Governors professor of chemistry and chemical biology, noting that the size of the PDB has doubled in just the last three-and-a-half years.
"We are estimating that the PDB will not only double, but triple to 150,000 structures by 2014," said Dr. Philip E. Bourne, Associate Director of the RCSB PDB and professor of pharmacology at the UCSD Skaggs School of Pharmacy and Pharmaceutical Sciences.
The RCSB PDB is based at Rutgers University in New Jersey, and the San Diego Supercomputer Center (SDSC) and Skaggs School of Pharmacy and Pharmaceutical Sciences at the University of California at San Diego. Bourne, a distinguished scientist with SDSC, has been leveraging the resources of the supercomputer center to create a highly uniform and robust process for archiving and providing access to the molecular structures.
The RCSB PDB is responsible for releasing PDB entries into the archive after they have been reviewed and annotated. At Rutgers, RCSB PDB members annotate structures and develop the sophisticated infrastructure needed to handle these complex data. The primary PDB FTP site is based at SDSC, which serves as the distribution point for PDB users. In addition to the SDSC site, there are failover sites at both the UCSD Skaggs School and Rutgers University to ensure constant access.
In addition to a comprehensive website and database that lets users search, analyze, and visualize the structures of biological macromolecules and their relationships to sequence, function, and disease, the RCSB PDB features a Molecule of the Month series, which recently published its 100th installment. Proteins, one of the main building blocks for living organisms, come in a variety of shapes, with the form of a protein corresponding to its function. The structures housed in the PDB demonstrate great diversity in size, complexity, and function, including:
Insulin, the protein deficient in diabetic patients
p53 tumor suppressor, a protein often implicated in cancer
Anthrax toxin, the disease-causing protein made by anthrax
Amyloid peptide, a protein implicated in Alzheimer's disease
The RCSB PDB is supported by funds from the National Science Foundation, the National Institute of General Medical Sciences, the Office of Science, the Department of Energy, the National Library of Medicine, the National Cancer Institute, the National Center for Research Resources, the National Institute of Biomedical Imaging and Bioengineering, the National Institute of Neurological Disorders and Stroke, and the National Institute of Diabetes & Digestive & Kidney Diseases.
Source: Jan Zverina
University of California - San Diego
суббота, 15 октября 2011 г.
Study Identifies New Mechanism Linking Activation Of Key Heart Enzyme And Oxidative Stress
A study, led by University of Iowa researchers, reveals a new dimension for a key heart enzyme and sheds light on an important biological pathway involved in cell death in heart disease. The study, published in the May 2 issue of Cell, has implications for understanding, and potentially for diagnosing and treating, heart failure and arrhythmias.
The UI researchers and colleagues from Vanderbilt University in Nashville, Tenn., focused on calmodulin kinase II, or CaM kinase II, a well-studied enzyme critical to many fundamental processes including heartbeat and thought.
Scientists know that CaM kinase's activity is sustained by adding a phosphate group -- a process known as phosphorylation. The new study proves that oxidation -- adding oxygen -- also can sustain the enzyme's activity, and like phosphorylation, the mechanism can be reversed to inactivate the kinase.
"Our results suggest that oxidation of CaM kinase is a dynamic and reversible process that may direct cell signaling in health and disease," said Mark Anderson, M.D., Ph.D., UI professor of internal medicine and molecular physiology and biophysics and senior study author. "Because CaM kinase activity is involved in arrhythmias, hypertrophy and heart cell death, this work also provides new insights into a disease pathway in heart that may lead to development of new drugs to treat heart disease."
In patients with heart failure, the level of angiotensin II -- a signaling molecule that promotes oxidation and cell death -- is elevated. Using a specially created antibody, the researchers found that angiotensin II also increases the amount of oxidized CaM kinase.
In addition, by replacing the cell's normal CaM kinase with a CaM kinase unable to be oxidized, the scientists were able to block angiotensin-induced cell death. Scientists hope this discovery might lead to therapies that prevent cell death by blocking CaM kinase oxidation.
Currently, "angiotensin-blockers" are a mainstay for treating patients with sick hearts, but they work indirectly by targeting receptors on the cell surface. Anderson, who also is the Potter-Lambert Chair in Cardiology and director of the UI Division of Cardiovascular Medicine, suggested that by understanding the signaling mechanisms that occur inside the cell, it might be possible to inhibit the angiotensin pathway more directly. This approach may also preserve some of the good effects mediated by the cell surface receptor.
Using a wide range of scientific techniques and experimental methods, the team, led by Anderson and Jeffrey Erickson, Ph.D., a UI postdoctoral fellow, pinned down the details of the internal signaling mechanism.
Specifically, they showed that oxidation of two neighboring methionines -- sulfur-containing amino acids -- can sustain CaM kinase activity. Loss of these two methionines prevents activation by oxidation. They also found that they could return CaM kinase to its inactive state and inhibit heart cell death and dysfunction by using an enzyme called methionine sulfoxide reductase A (msrA), which reverses the methionine oxidation. Studies in worms, fruit flies and mice have shown that msrA increases lifespan, but, until now, the enzyme's targets in heart were unknown.
The UI team compared mice without the msrA enzyme to normal mice when the animals underwent disease stresses, including excess angiotensin or induced heart attacks. The mice without msrA were more likely to die than normal mice under these circumstances, and the levels of oxidized CaM kinase were much higher in mice that lacked the enzyme.
Anderson speculated that the findings could implicate msrA as a susceptibility gene for patients - potentially, variations in the gene might help explain why some people do so badly after a heart attack where others do well.
The study demonstrates a direct link between CaM kinase activation and oxidative stress, two processes that are implicated in a wide variety of physiological and disease states. These findings will likely have broad implications and applications in basic research, diagnostics and new therapeutic approaches and represent an example of translation science of the type supported and encouraged by the new Institute for Clinical and Translational Science at the UI.
"This study also is a great example of collaborative science," added Anderson. "We had to apply expertise from several different labs to tackle this problem. So, the ease with which we can collaborate across disciplines at the UI and between institutions was enormously beneficial."
The work involved researchers from the UI Roy J. and Lucille A. Carver College of Medicine's Departments of Internal Medicine, Radiation Oncology and Biochemistry; and Vanderbilt University.
In addition to Anderson and Erickson, the UI researchers included Peter Mohler, Ph.D., assistant professor of internal medicine; Douglas Spitz, Ph.D., professor of radiation oncology in the Free Radical and Radiation Biology Graduate Program; Robert Weiss, M.D., professor of internal medicine; Madeline Shea, Ph.D., professor of biochemistry; Mei-ling Joiner, Xiaoqun Guan, Ph.D.; William Kutschke; Jinying Yang; John Lowe; Susan O'Donnell; Nukhet Aykin-Burns, Ph.D.; Matthew Zimmerman, Ph.D.; and Kathy Zimmerman.
The researchers from Vanderbilt University included, Carmine Oddis, M.D.; Ryan Bartlett, Ph.D.; Amy-Joan Ham, Ph.D.; and Roger Colbran, Ph.D.
The study was funded in part by the National Institutes of Health, the Pew Charitable Trust and the UI Research Foundation.
Source:
University of Iowa Health Science Relations, 5135 Westlawn, Iowa City, Iowa 52242-1178
Jennifer Brown
University of Iowa
The UI researchers and colleagues from Vanderbilt University in Nashville, Tenn., focused on calmodulin kinase II, or CaM kinase II, a well-studied enzyme critical to many fundamental processes including heartbeat and thought.
Scientists know that CaM kinase's activity is sustained by adding a phosphate group -- a process known as phosphorylation. The new study proves that oxidation -- adding oxygen -- also can sustain the enzyme's activity, and like phosphorylation, the mechanism can be reversed to inactivate the kinase.
"Our results suggest that oxidation of CaM kinase is a dynamic and reversible process that may direct cell signaling in health and disease," said Mark Anderson, M.D., Ph.D., UI professor of internal medicine and molecular physiology and biophysics and senior study author. "Because CaM kinase activity is involved in arrhythmias, hypertrophy and heart cell death, this work also provides new insights into a disease pathway in heart that may lead to development of new drugs to treat heart disease."
In patients with heart failure, the level of angiotensin II -- a signaling molecule that promotes oxidation and cell death -- is elevated. Using a specially created antibody, the researchers found that angiotensin II also increases the amount of oxidized CaM kinase.
In addition, by replacing the cell's normal CaM kinase with a CaM kinase unable to be oxidized, the scientists were able to block angiotensin-induced cell death. Scientists hope this discovery might lead to therapies that prevent cell death by blocking CaM kinase oxidation.
Currently, "angiotensin-blockers" are a mainstay for treating patients with sick hearts, but they work indirectly by targeting receptors on the cell surface. Anderson, who also is the Potter-Lambert Chair in Cardiology and director of the UI Division of Cardiovascular Medicine, suggested that by understanding the signaling mechanisms that occur inside the cell, it might be possible to inhibit the angiotensin pathway more directly. This approach may also preserve some of the good effects mediated by the cell surface receptor.
Using a wide range of scientific techniques and experimental methods, the team, led by Anderson and Jeffrey Erickson, Ph.D., a UI postdoctoral fellow, pinned down the details of the internal signaling mechanism.
Specifically, they showed that oxidation of two neighboring methionines -- sulfur-containing amino acids -- can sustain CaM kinase activity. Loss of these two methionines prevents activation by oxidation. They also found that they could return CaM kinase to its inactive state and inhibit heart cell death and dysfunction by using an enzyme called methionine sulfoxide reductase A (msrA), which reverses the methionine oxidation. Studies in worms, fruit flies and mice have shown that msrA increases lifespan, but, until now, the enzyme's targets in heart were unknown.
The UI team compared mice without the msrA enzyme to normal mice when the animals underwent disease stresses, including excess angiotensin or induced heart attacks. The mice without msrA were more likely to die than normal mice under these circumstances, and the levels of oxidized CaM kinase were much higher in mice that lacked the enzyme.
Anderson speculated that the findings could implicate msrA as a susceptibility gene for patients - potentially, variations in the gene might help explain why some people do so badly after a heart attack where others do well.
The study demonstrates a direct link between CaM kinase activation and oxidative stress, two processes that are implicated in a wide variety of physiological and disease states. These findings will likely have broad implications and applications in basic research, diagnostics and new therapeutic approaches and represent an example of translation science of the type supported and encouraged by the new Institute for Clinical and Translational Science at the UI.
"This study also is a great example of collaborative science," added Anderson. "We had to apply expertise from several different labs to tackle this problem. So, the ease with which we can collaborate across disciplines at the UI and between institutions was enormously beneficial."
The work involved researchers from the UI Roy J. and Lucille A. Carver College of Medicine's Departments of Internal Medicine, Radiation Oncology and Biochemistry; and Vanderbilt University.
In addition to Anderson and Erickson, the UI researchers included Peter Mohler, Ph.D., assistant professor of internal medicine; Douglas Spitz, Ph.D., professor of radiation oncology in the Free Radical and Radiation Biology Graduate Program; Robert Weiss, M.D., professor of internal medicine; Madeline Shea, Ph.D., professor of biochemistry; Mei-ling Joiner, Xiaoqun Guan, Ph.D.; William Kutschke; Jinying Yang; John Lowe; Susan O'Donnell; Nukhet Aykin-Burns, Ph.D.; Matthew Zimmerman, Ph.D.; and Kathy Zimmerman.
The researchers from Vanderbilt University included, Carmine Oddis, M.D.; Ryan Bartlett, Ph.D.; Amy-Joan Ham, Ph.D.; and Roger Colbran, Ph.D.
The study was funded in part by the National Institutes of Health, the Pew Charitable Trust and the UI Research Foundation.
Source:
University of Iowa Health Science Relations, 5135 Westlawn, Iowa City, Iowa 52242-1178
Jennifer Brown
University of Iowa
среда, 12 октября 2011 г.
Identification Of Stem Cells That Repair Injured Muscles Has Important Implications For Muscular Dystrophy
A University of Colorado at Boulder research team has identified a type of skeletal muscle stem cell that contributes to the repair of damaged muscles in mice, which could have important implications in the treatment of injured, diseased or aging muscle tissue in humans, including the ravages of muscular dystrophy.
The newly identified stem cells are found within populations of satellite cells located between muscle fibers and the surrounding connective tissue that are responsible for the repair and maintenance of skeletal muscles, said Professor Bradley Olwin of CU-Boulder's molecular, cellular and developmental biology department.
When muscle fibers are stressed or traumatized, satellite cells divide to make more specialized muscle cells and repair the muscle, said Olwin. The stem cell population identified by the CU team within the satellite cells -- dubbed "satellite-SP" cells -- were shown to renew the satellite cell population after injection into injured muscle cells, contributing to recovery of muscle tissue in the laboratory mice.
"This research shows how satellite cells can maintain their populations within injured tissues," said Olwin. "The hope is this new method will allow us to repair damaged or diseased skeletal muscle tissue."
A paper on the subject was published in the March 5 issue of the journal Cell Stem Cell. Co-authors on the study included the MCD biology department's Kathleen Tanaka, John Hall and Andrew Troy, as well as Dawn Cornelison from the University of Missouri and Susan Majka from the University of Colorado Denver.
Stem cells are distinguished by their ability to renew themselves through cell division and differentiate into specialized cell types. In healthy skeletal muscle tissue, the population of satellite cells is constantly maintained, leading the CU-Boulder team to believe that at least some of the satellite cell population in the mouse study included stem cells.
For the study, the researchers injected 2,500 satellite-SP cells into a population of satellite cells within injured mouse muscle tissue. They found that 75 percent of the satellite cells that reproduced were derived from the previous satellite-SP cells injected into the tissue. The results demonstrated the injected satellite-SP cells were renewing the satellite cell pool, Olwin said.
"The key point here is we are not just repairing the tissue," said Olwin. "We injected a permanent, self-renewing population of stem cells. One advantage of using this technology is that we can use a relatively small number of stem cells and do the job with a small number of injections -- in this case, only one."
The research has implications for a number of human diseases, he said. In muscular dystrophy, the loss of a protein called dystrophin causes the muscle to literally tear itself apart, a process that cannot be repaired without cell-based intervention. Although injected cells will repair the muscle fibers, maintaining the muscle fibers requires additional cell injections.
The research was funded in part by the National Institutes of Health and the Muscular Dystrophy Association. Olwin is now collaborating with a group at the University of Washington and the Fred Hutchinson Cancer Research Center in Seattle to extend the research.
Source: Bradley Olwin
University of Colorado at Boulder
The newly identified stem cells are found within populations of satellite cells located between muscle fibers and the surrounding connective tissue that are responsible for the repair and maintenance of skeletal muscles, said Professor Bradley Olwin of CU-Boulder's molecular, cellular and developmental biology department.
When muscle fibers are stressed or traumatized, satellite cells divide to make more specialized muscle cells and repair the muscle, said Olwin. The stem cell population identified by the CU team within the satellite cells -- dubbed "satellite-SP" cells -- were shown to renew the satellite cell population after injection into injured muscle cells, contributing to recovery of muscle tissue in the laboratory mice.
"This research shows how satellite cells can maintain their populations within injured tissues," said Olwin. "The hope is this new method will allow us to repair damaged or diseased skeletal muscle tissue."
A paper on the subject was published in the March 5 issue of the journal Cell Stem Cell. Co-authors on the study included the MCD biology department's Kathleen Tanaka, John Hall and Andrew Troy, as well as Dawn Cornelison from the University of Missouri and Susan Majka from the University of Colorado Denver.
Stem cells are distinguished by their ability to renew themselves through cell division and differentiate into specialized cell types. In healthy skeletal muscle tissue, the population of satellite cells is constantly maintained, leading the CU-Boulder team to believe that at least some of the satellite cell population in the mouse study included stem cells.
For the study, the researchers injected 2,500 satellite-SP cells into a population of satellite cells within injured mouse muscle tissue. They found that 75 percent of the satellite cells that reproduced were derived from the previous satellite-SP cells injected into the tissue. The results demonstrated the injected satellite-SP cells were renewing the satellite cell pool, Olwin said.
"The key point here is we are not just repairing the tissue," said Olwin. "We injected a permanent, self-renewing population of stem cells. One advantage of using this technology is that we can use a relatively small number of stem cells and do the job with a small number of injections -- in this case, only one."
The research has implications for a number of human diseases, he said. In muscular dystrophy, the loss of a protein called dystrophin causes the muscle to literally tear itself apart, a process that cannot be repaired without cell-based intervention. Although injected cells will repair the muscle fibers, maintaining the muscle fibers requires additional cell injections.
The research was funded in part by the National Institutes of Health and the Muscular Dystrophy Association. Olwin is now collaborating with a group at the University of Washington and the Fred Hutchinson Cancer Research Center in Seattle to extend the research.
Source: Bradley Olwin
University of Colorado at Boulder
воскресенье, 9 октября 2011 г.
Deadly Fungus Decimating Bat Populations Cannot Be Controlled By Culling
Culling will not stop the spread of a deadly fungus that is threatening to wipe out hibernating bats in North America, according to a new mathematical model.
White-nose syndrome, which is estimated to have killed over a million bats in a three year period, is probably caused by a newly discovered cold-adapted fungus, Geomyces destructans. The new model examines how WNS is passed from bat to bat and concludes that culling would not work because of the complexity of bat life history and because the fungal pathogen occurs in the caves and mines where the bats live.
"Because the disease is highly virulent, our model results support the hypothesis that transmission occurs in all contact areas," write the paper's authors, Tom Hallam and Gary McCracken, both of the University of Tennessee. "Our simulations indicated culling will not control WNS in bats primarily because contact rates are high among colonial bats, contact occurs in multiple arenas, and periodic movement between arenas occurs."
Ground work on the model was initiated in a 2009 modeling workshop on white-nose syndrome held at the National Institute for Mathematical and Biological Synthesis (NIMBioS) in Knoxville, Tennessee. At the interdisciplinary workshop, experts in the fields of bat physiology, fungal ecology, ecotoxicology, and epidemiology discussed ways in which mathematical modeling could be applied to predict and control the spread of WNS.
"NIMBioS' support for the workshop that initiated this project was crucial in helping formulate models that could be useful in looking at white-nose syndrome," Hallam said.
Culling of bats in areas where the disease is present is one of several options that have been considered by state and federal agencies as a way to control the disease. However, a review of management options for controlling WNS in the paper indicates that culling is ineffective for disease control in wild animals and in some cases, can exacerbate the spread.
White-nose syndrome first appeared in a cave in upstate New York in 2006, and has since spread to 14 states and as far north as Canada. Regional extinctions of the most common bat species, the little brown bat, are predicted within two decades due to WNS.
Eating up to two-thirds of their body weight in insects every night, bats help suppress insect populations ultimately reducing crop damage and the quantities of insecticides used on crops. Bats also play an important ecological role in plant pollination and seed dissemination.
Citations: Hallam TG, McCracken GF. 2011. Management of the panzootic white-nose syndrome through culling of bats. Conservation Biology 25(1): 189-194.
Source:
Catherine Crawley
National Institute for Mathematical and Biological Synthesis (NIMBioS)
White-nose syndrome, which is estimated to have killed over a million bats in a three year period, is probably caused by a newly discovered cold-adapted fungus, Geomyces destructans. The new model examines how WNS is passed from bat to bat and concludes that culling would not work because of the complexity of bat life history and because the fungal pathogen occurs in the caves and mines where the bats live.
"Because the disease is highly virulent, our model results support the hypothesis that transmission occurs in all contact areas," write the paper's authors, Tom Hallam and Gary McCracken, both of the University of Tennessee. "Our simulations indicated culling will not control WNS in bats primarily because contact rates are high among colonial bats, contact occurs in multiple arenas, and periodic movement between arenas occurs."
Ground work on the model was initiated in a 2009 modeling workshop on white-nose syndrome held at the National Institute for Mathematical and Biological Synthesis (NIMBioS) in Knoxville, Tennessee. At the interdisciplinary workshop, experts in the fields of bat physiology, fungal ecology, ecotoxicology, and epidemiology discussed ways in which mathematical modeling could be applied to predict and control the spread of WNS.
"NIMBioS' support for the workshop that initiated this project was crucial in helping formulate models that could be useful in looking at white-nose syndrome," Hallam said.
Culling of bats in areas where the disease is present is one of several options that have been considered by state and federal agencies as a way to control the disease. However, a review of management options for controlling WNS in the paper indicates that culling is ineffective for disease control in wild animals and in some cases, can exacerbate the spread.
White-nose syndrome first appeared in a cave in upstate New York in 2006, and has since spread to 14 states and as far north as Canada. Regional extinctions of the most common bat species, the little brown bat, are predicted within two decades due to WNS.
Eating up to two-thirds of their body weight in insects every night, bats help suppress insect populations ultimately reducing crop damage and the quantities of insecticides used on crops. Bats also play an important ecological role in plant pollination and seed dissemination.
Citations: Hallam TG, McCracken GF. 2011. Management of the panzootic white-nose syndrome through culling of bats. Conservation Biology 25(1): 189-194.
Source:
Catherine Crawley
National Institute for Mathematical and Biological Synthesis (NIMBioS)
четверг, 6 октября 2011 г.
New $1.16 Million Study Investigates How Dietary Iron Is Used By Cells
A four-year study on iron metabolism within cells, an essential process that impacts both iron deficiency and iron toxicity, conditions responsible for a multitude of human diseases, is underway at the University at Buffalo funded by a $1.16 million grant from the National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK).
Daniel Kosman, Ph.D., professor of biochemistry in the UB School of Medicine and Biomedical Sciences, is lead researcher on the study.
"The concern about how iron is managed in our cells has never been more acute," said Kosman. "The reasons for this are three-fold. First is the endemic problem of iron deficiency that the World Health Organization estimates afflicts 80 percent of the world's population, or more than 5 billion people.
"Iron deficiency is not confined to developing nations. In the U.S., 5 percent of newborns and 7 percent of new mothers have clinical symptoms of iron deficiency. Reducing the incidence of this nutritional deficit is one of the objectives of the U.S. Department of Health and Human Services' Healthy People 2010 program.
"Second is the broad recognition that the 'corrosive chemistry' associated with iron and oxygen interactions is a major factor in a multitude of human diseases."
Too much iron in tissues, called iron-loading, is thought to increase the risk of tumor development, infection, cardiomyopathy, joint disorders and several endocrine and neurodegenerative disorders.
"And third, we now have an increasingly sophisticated knowledge and understanding of iron metabolic pathways, the proteins involved in these pathways and how these pathways are regulated in all organisms, making this issue ripe for investigation," he said.
Kosman proposes that a general mechanism of cellular iron metabolism requires that iron-handling proteins involved in sequential steps in the pathway must be "architecturally arranged" contiguously in the cell's membranes, at the interfaces between membranes and soluble compartments or within soluble compartments.
The researchers will test this form-function model of ionic iron metabolism by focusing on three steps critical to maintaining the proper balance of iron in cells: 1) the reduction of ferric to ferrous iron and the subsequent transport of ferrous iron into a cell; 2) the "hand-off" of this ferrous iron from a membrane protein to iron chaperones in the cell's cytoplasm; and 3) the utilization of this ionic iron for the activation of essential iron-containing enzymes.
"These three components of cellular iron metabolism are relatively under-investigated," said Kosman, "yet they represent the essence of cell iron metabolism in all organisms."
Understanding the intermediary metabolism of iron is one of the primary objectives of a program announcement from NIH titled "Metals In Medicine," he noted. This announcement encourages studies that lead to the "identification and characterization of the macromolecular players and vesicular compartments involved in metal ion homeostasis and metal trafficking."
Arvinder Singh, Ph.D., a post-doctoral research associate in Kosman's lab; and William E. Wiltsie, a doctoral candidate in biochemistry, also will be involved in the research.
The University at Buffalo is a premier research-intensive public university, the largest and most comprehensive campus in the State University of New York. The School of Medicine and Biomedical Sciences is one of five schools that constitute UB's Academic Health Center. UB's more than 27,000 students pursue their academic interests through more than 300 undergraduate, graduate and professional degree programs.
Contact: Lois Baker
University at Buffalo
Daniel Kosman, Ph.D., professor of biochemistry in the UB School of Medicine and Biomedical Sciences, is lead researcher on the study.
"The concern about how iron is managed in our cells has never been more acute," said Kosman. "The reasons for this are three-fold. First is the endemic problem of iron deficiency that the World Health Organization estimates afflicts 80 percent of the world's population, or more than 5 billion people.
"Iron deficiency is not confined to developing nations. In the U.S., 5 percent of newborns and 7 percent of new mothers have clinical symptoms of iron deficiency. Reducing the incidence of this nutritional deficit is one of the objectives of the U.S. Department of Health and Human Services' Healthy People 2010 program.
"Second is the broad recognition that the 'corrosive chemistry' associated with iron and oxygen interactions is a major factor in a multitude of human diseases."
Too much iron in tissues, called iron-loading, is thought to increase the risk of tumor development, infection, cardiomyopathy, joint disorders and several endocrine and neurodegenerative disorders.
"And third, we now have an increasingly sophisticated knowledge and understanding of iron metabolic pathways, the proteins involved in these pathways and how these pathways are regulated in all organisms, making this issue ripe for investigation," he said.
Kosman proposes that a general mechanism of cellular iron metabolism requires that iron-handling proteins involved in sequential steps in the pathway must be "architecturally arranged" contiguously in the cell's membranes, at the interfaces between membranes and soluble compartments or within soluble compartments.
The researchers will test this form-function model of ionic iron metabolism by focusing on three steps critical to maintaining the proper balance of iron in cells: 1) the reduction of ferric to ferrous iron and the subsequent transport of ferrous iron into a cell; 2) the "hand-off" of this ferrous iron from a membrane protein to iron chaperones in the cell's cytoplasm; and 3) the utilization of this ionic iron for the activation of essential iron-containing enzymes.
"These three components of cellular iron metabolism are relatively under-investigated," said Kosman, "yet they represent the essence of cell iron metabolism in all organisms."
Understanding the intermediary metabolism of iron is one of the primary objectives of a program announcement from NIH titled "Metals In Medicine," he noted. This announcement encourages studies that lead to the "identification and characterization of the macromolecular players and vesicular compartments involved in metal ion homeostasis and metal trafficking."
Arvinder Singh, Ph.D., a post-doctoral research associate in Kosman's lab; and William E. Wiltsie, a doctoral candidate in biochemistry, also will be involved in the research.
The University at Buffalo is a premier research-intensive public university, the largest and most comprehensive campus in the State University of New York. The School of Medicine and Biomedical Sciences is one of five schools that constitute UB's Academic Health Center. UB's more than 27,000 students pursue their academic interests through more than 300 undergraduate, graduate and professional degree programs.
Contact: Lois Baker
University at Buffalo
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