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International research teams led by Goethe University Frankfurt and Jena University Hospital find mechanisms involved in regulation of structure and function of endoplasmic reticulum
Our cells are crisscrossed by a system of membrane tubes and pockets called the endoplasmic reticulum (ER). It is crucial for the production of biomolecules and is continuously built up and degraded. Degradation, known as ER-phagy, is promoted by the protein ubiquitin, which controls many processes in the cell. If the proteins involved in ER-phagy are defective, neurodegenerative diseases result. This has been discovered by an international research team led by Goethe University Frankfurt (as part of the EMTHERA research cluster) and Jena University Hospital and published in two papers in the renowned journal Nature.
FRANKFURT. A tangle of pockets, tubes and sac-like membrane structures runs through the cells of humans, animals, plants and fungi: the endoplasmic reticulum, or ER for short. In the ER, proteins are manufactured, folded into their three-dimensional structure and modified, lipids and hormones are produced and calcium concentrations in the cell are controlled. In addition, the ER forms the basis for the cellular transport system, feeds misfolded proteins to intracellular disposal and renders toxins that have entered the cell harmless.
In view of its multiple tasks, the ER is constantly being remodeled. A process called ER-phagy (roughly “self-digestion of the ER") is responsible for ER degradation. Involved is a group of signal-receiving proteins – receptors – that are responsible for the membrane curvatures of the ER and thus for its multiple forms in the cell. In ER-phagy, the receptors accumulate at specific sites on the ER and increase membrane curvature to such an extent that, as a consequence, part of the ER is strangulated and broken down into its component parts by cellular recycling structures (autophagosomes).
In cell culture experiments, biochemical and molecular biological studies, and by computer simulations, the scientific team led by Professor Ivan Đikić of Goethe University Frankfurt first tested the membrane curvature receptor FAM134B and demonstrated that ubiquitin promotes and stabilizes the formation of clusters of FAM134B protein in the ER membrane. Thus, ubiquitin drives ER-phagy. Đikić explains: “Ubiquitin causes the FAM134B clusters to become more stable and the ER to bulge out more at these sites. The stronger membrane curvature then leads to further stabilization of the clusters and, moreover, attracts additional membrane curvature proteins. So the effect of ubiquitin is self-reinforcing." The researchers were also able to detect cluster formation using super-high resolution microscopy.
Đikić continues: “To fulfill this function, ubiquitin changes the shape of part of the FAM134B protein. This is another facet of ubiquitin that performs an almost unbelievable array of tasks to keep all different cell functions working."
The importance of ER-phagy is demonstrated by diseases resulting from a defective FAM134B protein. A team led by Professor Christian Hübner from Jena University Hospital previously identified mutations in the FAM134B gene causing a very rare hereditary sensory and autonomic neuropathy (HSAN), in which sensory nerves die. As a result, patients are unable to perceive pain and temperature correctly, which can lead to incorrect stresses or injuries going unnoticed and developing into chronic wounds. In a long-standing collaboration between Jena University Hospital and Goethe University Frankfurt FAM134B was identified as the first receptor for ER-phagy.
Mutations in another membrane curvature protein called ARL6IP1 cause a similar neurodegenerative disorder which combines sensory defects with muscle hardening (spasticity) in the legs. The scientific team led by Christian Hübner and Ivan Đikić has now identified that ARL6IP1 belongs to the ER-phagy machinery as well and is also ubiquitinated during ER-phagy.
Christian Hübner explains: “In mice that do not possess the ARL6IP1 protein, we can see that the ER virtually expands and degenerates as the cells age. This leads to an accumulation of misfolded proteins or protein clumps, which are no longer disposed of in the cell. As a result, nerve cells in particular, which do not renew as quickly as other body cells, die, causing the clinical symptoms in affected patients and genetically modified mice. We hypothesize from our data that the two membrane curvature receptors FAM134B and ARL6IP1 form mixed clusters during ER-phagy and depend on each other to control normal size and function of ER. Additional work will be required to fully acknowledge the role of ER-phagy in neurons as well as in other cell types."
Overall, however, the research teams have taken a decisive step toward understanding ER-phagy, Đikić is convinced: “We now understand better how cells control their functions and thus create something we call cellular homeostasis. In biology, this knowledge allows fascinating insights into the incredible achievements of our cells, and for medicine it is essential for understanding diseases, diagnosing them on time and helping patients by developing new therapies. "
Scientists from the following institutions were involved in the work:
Background information:
EMTHERA research cluster: Emerging strategies against infections, inflammation, and impaired immune mechanisms https://www.emthera.de/
Collaborative Research Center (SFB 1177) "Molecular and functional characterization of selective autophagy". http://www.sfb1177.de/
Frankfurt scientists discover new molecular mechanisms that eliminate intracellular damages – Mutations in this pathway trigger neurodegenerative diseases (2015) https://www.goethe-university-frankfurt.de/74984432/Controller_in_the_Cell
Publications:
1) Alexis González, Adriana Covarrubias-Pinto, Ramachandra M. Bhaskara, Marius Glogger, Santosh K. Kuncha, Audrey Xavier, Eric Seemann, Mohit Misra, Marina E. Hoffmann, Bastian Bräuning, Ashwin Balakrishnan, Britta Qualmann, Volker Dötsch, Brenda A. Schulman, Michael M. Kessels, Christian A. Hübner, Mike Heilemann, Gerhard Hummer, Ivan Dikic: Ubiquitination regulates ER-phagy and remodeling of endoplasmic reticulum. Nature (2023) https://doi.org/10.1038/s41586-023-06089-2
2) Hector Foronda, Yangxue Fu, Adriana Covarrubias-Pinto, Hartmut T. Bocker, Alexis González, Eric Seemann, Patricia Franzka, Andrea Bock, Ramachandra M. Bhaskara, Lutz Liebmann, Marina E. Hoffmann, Istvan Katona, Nicole Koch, Joachim Weis, Ingo Kurth, Joseph G. Gleeson, Fulvio Reggiori, Gerhard Hummer, Michael M. Kessels, Britta Qualmann, Muriel Mari, Ivan Dikić, Christian A. Hübner: Heteromeric 1 clusters of ubiquitinated ER-shaping proteins drive ER-phagy. Nature (2023) https://doi.org/10.1038/s41586-023-06090-9
Images for download:
1) https://www.uni-frankfurt.de/137667495
ER-Phagy: Part of the ER is strangulated and broken down into its component parts by autophagosomes
Researchers in Frankfurt and Jena have now deciphered how the disturbed recycling chain of the endoplasmic reticulum can cause neurodegenerative diseases. Graphics: Manja Schiefer
2) https://www.uni-frankfurt.de/137667230
Membrane curvature proteines cluster in ER membrane
A super-high resolution microscopy technique reveals how FAM134B proteins assemble into clusters after stimulation of ER-phagy in the endoplasmic reticulum. Photos: Gonzáles et al., Nature (2023) https://doi.org/10.1038/s41586-023-06089-2
Further information
Prof. Dr. Ivan Ðikić
Institute of Biochemistry II,Goethe University Frankfurt
and Buchmann Institute for Molecular Life Sciences
Tel: +49 (0) 69 6301-5964
dikic@biochem2.uni-frankfurt.de
Twitter: @iDikic2 @goetheuni
Prof. Dr. Christian Hübner
Institute of Human Genetics
and Center for Rare Diseases
University Hospital Jena
Tel. +49 3641 9-396800
Christian.Huebner@med.uni-jena.de
Twitter: @UKJ_Jena
Extension for the looted property project at Frankfurt University Library: 349 looted volumes identified to date
The exhibition "StolperSeiten – NS-Raubgut in der Universitätsbibliothek Frankfurt am Main" (“Stumbling Pages – NS looted property in the Frankfurt University Library") will be made available online as a virtual 360° tour on Provenance Research Day, which falls on April 12, 2023 this year. The exhibit is based on a project funded by the German Lost Art Foundation (Deutsches Zentrum Kulturgutverluste) as part of which the library is researching books in its inventory that can be attributed to persecutees of the Nazi era. The extension is the direct result of comparatively frequent finds, with the project now running until November 2024. There have already been several restitutions to Jewish and other organizations.
"StolperSeiten" (Stumbling Pages) was the title of a much-noticed 2022 exhibition at the library on Nazi looted property at the Frankfurt University Library (“NS-Raubgut in der Universitätsbibliothek Frankfurt am Main"). This exhibition is now open again, but in the form of a virtual 360° tour. It spans the historical framework that led to the looting of hundreds of thousands of cultural assets in Germany and Europe from 1933 onwards. With its focus on the city of Frankfurt, and the city's libraries in particular, the exhibit addresses the role libraries played in the organized looting and how they profited from it, pointing out many concrete cases of injustice. In addition, the use of partially interactive elements also makes the work of contemporary provenance researchers more accessible. http://stolperseiten.studiumdigitale.uni-frankfurt.de/
The online exhibit was designed as part of a project run by “fuels – Future Learning Spaces". Funded by the Hessian Ministry of Higher Education, Research, Science and the Arts, the joint project of Goethe University, Darmstadt Technical University and Darmstadt University of Applied Sciences aims to bring innovative technologies such as 360°, augmented and virtual reality into the university landscape. For more information, visit: https://futurelearning.space/
Project to identify looted National Socialist property
In November 2020, Frankfurt University Library's (UB JCS) Provenance Research team started a project to identify looted National Socialist property in a first sub-collection comprising around 80,000 volumes. The search focuses on so-called "cultural property seized as a result of persecution", i.e. books that were looted or extorted from persecuted persons or institutions during the Nazi era. Commenting on the motives for researching Nazi looted property in the library, UB JCS director Daniela Poth says: "We consider it a moral obligation to uncover the injustice committed during the Nazi era and to document it in public, even if this does not make up for it. That is something university management, library management and project management all agree on." The project at Goethe University's UB JCS is sponsored by the German Lost Art Foundation. In addition, given the fact that many of the affected books are on permanent loan at the UB JCS but historically belong to the municipality, the city of Frankfurt is also providing a subsidy for the project costs.
Following the approval for an extension – itself based on the comparatively high number of finds – the project will now run until November 2024, and therefore already passed its halftime mark a few months ago. Time for an interim assessment. To date, almost 40,000 volumes have been individually checked on the shelf for any references to previous owners. This has turned out to be the case in an unusually high percentage of about 39%. As a result, more than 15,000 volumes have had to be examined more closely to clarify whether the suspicion of looted property is merited. Such an initial suspicion exists for over 3,800 books. Another 200 books have met with strong suspicion, whereas 349 books have been confirmed as cases of looted property. However, the project team's work does not end with the investigation into actual numbers or with the documentation of these cases on UB JCS' freely accessible search portal. For all confirmed cases of looted property, the project staff also researches the existence of descendants or successor institutions. If this search, which can be very complex, is successful, the library contacts the potential restitution recipients and clarifies whether they desire a return, or would prefer another "fair and just solution".
The fact that it took some time after the start of the project before the first restitutions could be both prepared and carried out illustrates just how time-consuming research and coordination are. Within the last six months, three books were restituted to the Jewish Community of Munich and Upper Bavaria, one book to the Jewish Religious Community of Baden and eight volumes to the Minerva Lodge of the Three Palms in Leipzig. Corresponding references to these volumes are available in the library's search portal – as virtual "StolperSeiten". Further restitutions are in the preparatory stage and expected to be completed during the course of the year.
Further information: Dr. Mathias Jehn, Head of the Department "Curating Subject Information Mediation", J. C. Senckenberg University Library, Bockenheimer Landstraße 134-138, 60325 Frankfurt, Tel: +49 (69) 798 39007, Mail: m.jehn@ub.uni-frankfurt.de
Contact for general press inquiries: Bernhard Wirth, Staff Development and Public Relations of the Library, Tel. +49 (69) 798 39223; Mail: pr-team@ub.uni-frankfurt.de
Editor: Dr. Dirk Frank, Press Officer, PR & Communication Office, Theodor-W.-Adorno-Platz 1, 60323 Frankfurt am Main, Tel: +49 (0) 69 798-13753, frank@pvw.uni-frankfurt.de
International research team from Germany, Austria, Canada, the Netherlands and the USA applies new carbonate analysis method to eggshells from Troodon, reptiles and birds
An international research team led by Goethe University Frankfurt, Germany, determined that Troodon, a dinosaur very close to modern birds, was a warm-blooded animal (an endotherm), but had a reproductive system similar to that of modern reptiles. The scientists applied a new method which allowed for accurate determination of the temperature when the egg's carbonate shell was formed. Furthermore, the researchers showed that Troodon laid 4 to 6 eggs per clutch. As nests with up to 24 Troodon eggs had been found, the scientists conclude that several Troodon females laid their eggs in communal nests.
FRANKFURT. In millions of years and with a long sequence of
small changes, evolution has shaped a particular group of dinosaurs, the theropods,
into the birds we watch fly around the planet today. In fact, birds are the
only descendants of dinosaurs which survived the catastrophic extinction 66
million years ago that ended the Cretaceous period.
Troodon was such a theropod. The carnivorous
dinosaur was about two meters long and populated the vast semi-arid landscapes of
North America about 75 million years ago. Like some of its dinosaur relatives, Troodon
presented some bird-like features like hollow and light bones. Troodon walked
on two legs and had fully developed feathery wings, but its relatively large size
precluded it from flying. Instead, it probably ran quite fast and caught its
prey using its strong claws. Troodon
females laid eggs more similar to the asymmetric eggs of modern birds than to
round ones of reptiles, the oldest relatives of all dinosaurs. These eggs were coloured
and have been found half buried into the ground, probably allowing Troodon to sit and brood them.
An international team of scientists led by
Mattia Tagliavento and Jens Fiebig from Goethe University Frankfurt, Germany, has
now examined the calcium carbonate of some well-preserved Troodon eggshells.
The researchers used a method developed by Fiebig's group in 2019 called “dual
clumped isotope thermometry". By using this method, they could measure the
extent to which heavier varieties (isotopes) of oxygen and carbon clump
together in carbonate minerals. The prevalence of isotopic clumping, which is
temperature-dependent, made it possible for scientists to determine the
temperature at which the carbonates crystallized.
When analyzing Troodon eggshells, the
research team was able to determine that the eggshells were produced at temperatures
of 42 and 30 degrees Celsius. Mattia Tagliavento, leading author of the study,
explains: “The isotopic composition of Troodon
eggshells provides evidence that these extinct animals had a body temperature
of 42°C, and that they were able to reduce it to about 30°C, like modern
birds."
The scientists then compared isotopic
compositions of eggshells of reptiles (crocodile, alligator, and various
species of turtle) and modern birds (chicken, sparrow, wren, emu, kiwi,
cassowary and ostrich) to understand if Troodon was closer to either
birds or reptiles. They revealed two different isotopic patterns: reptile eggshells
have isotopic compositions matching the temperature of the surrounding
environment. This is in line with these animals being cold-blooded and forming
their eggs slowly. Birds, however, leave a recognizable so-called non-thermal
signature in the isotopic composition, which indicates that eggshell formation
happens very fast. Tagliavento: “We think this very high production rate is connected to the fact that
birds, unlike reptiles, have a single ovary. Since they can produce just one
egg at the time, birds have to do it more rapidly."
When comparing these results to Troodon
eggshells, the researchers did not detect the isotopic composition which is typical
for birds. Tagliavento is convinced: “This demonstrates that Troodon formed its eggs in a way more
comparable to modern reptiles, and it implies that its reproductive system was
still constituted of two ovaries."
The researchers finally combined their
results with existing information concerning body and eggshell weight, deducing
that Troodon produced only 4 to 6 eggs per reproductive phase. “This
observation is particularly interesting because Troodon nests are usually large, containing up to 24 eggs",
Tagliavento explains. “We think this is a strong suggestion that Troodon
females laid their eggs in communal nests, a behaviour that we observe today
among modern ostriches."
These are extremely exciting findings, Jens
Fiebig comments: “Originally, we developed the dual clumped isotope method to accurately
reconstruct Earth's surface temperatures of past geological eras. This study
demonstrates that our method is not limited to temperature reconstruction, it
also presents the opportunity to study how carbonate biomineralization evolved
throughout Earth's history."
Publication: Mattia Tagliavento, Amelia J. Davies, Miguel Bernecker, Philip T. Staudigel, Robin R. Dawson, Martin Dietzel, Katja Goetschl, Weifu Guo, Anne S. Schulp, François Therrien, Darla K. Zelenitsky, Axel Gerdes, Wolfgang Müller, Jens Fiebig: Evidence for heterothermic endothermy and reptile-like eggshell mineralization in Troodon, a non-avian maniraptoran theropod. PNAS (2023) https://www.pnas.org/cgi/doi/10.1073/pnas.2213987120
Images
for download: https://www.uni-frankfurt.de/134845598
Caption:
Artist's impression of two Troodons with a
common nest. Illustration: Alex Boersma/PNAS
Participating
partners:
Institute of Geosciences, Goethe
University Frankfurt, Germany.
Frankfurt Isotope and Element Research Center (FIERCE), Goethe University
Frankfurt, Germany.
Institute of Applied Geosciences, Graz University of Technology, Austria.
Royal Tyrrell Museum of Palaeontology, Drumheller, Canada.
Department of Geoscience, University of Calgary, Canada.
Naturalis Biodiversity Center, Leiden, the Netherlands.
Deptartment of Earth Sciences, Universiteit Utrecht, the Netherlands
Department of Geosciences, University of Massachusetts, USA.
Morrill Science Center, Amherst, USA
Department of Geology and Geophysics, Woods Hole Oceanographic Institution, USA
Background:
Thermometers for Earth history: "Dual
clumped isotope" method for carbonate analysis (2020).
https://aktuelles.uni-frankfurt.de/english/geosciences-exact-climate-data-from-the-past/
Further
information:
Goethe
University Frankfurt
Institute for Geosciences
Dr. Mattia Tagliavento
Phone. +49 176 64735849
Tagliavento@geo.uni-frankfurt.de
Professor Jens Fiebig
Phone: +49 (0) 69 798 40182
Jens.Fiebig@em.uni-frankfurt.de
Naturalis
Biodiversity Center
and Utrecht University, Leiden/Utrecht, The Netherlands
Professor Anne S. Schulp (English, German,
Dutch)
Phone: +31 6 51229317
anne.schulp@naturalis.nl
/ a.s.schulp@uu.nl
Twitter-Handles: @goetheuni @UUGeo @UMass
@UniGraz @WHOI @Naturalis_Sci @RoyalTyrrell @UCalgarySWC
@anneschulp @Naturalis_Sci
@museumnaturalis
Editor: Dr. Markus Bernards, Science Editor, PR
& Communication Office, Tel: -49 (0) 69 798-12498, Fax: +49 (0) 69 798-763 12531, bernards@em.uni-frankfurt.de.
International team from Goethe University and the University of Kent identifies nitroxoline as a potential drug
Mpox – previously known as "monkeypox" – is currently spreading worldwide. An international research team from Goethe University and the University of Kent has now identified a compound that could help fight the disease. Their study has been published in the “Journal of Medical Virology".
Nitroxoline is the name of the new drug candidate that could potentially be used to treat mpox. It was identified by scientists at Goethe University and the University of Kent as part of a multi-site study. The results of their research will now allow clinical trials to begin soon.
The current mpox outbreak is the first of this size to occur outside of Africa and also the first mpox outbreak caused by human-to-human transmission. People with immunodeficiencies are particularly at risk from the disease. Although antiviral agents have already been shown to inhibit the replication of the mpox virus in experimental models, the efficacy of these substances has not yet been confirmed in humans and some may have significant side effects. In addition, there are insufficient stocks to treat all mpox patients. Moreover, resistance formation against tecovirimat, the most promising mpox drug candidate to date, has already been reported.
In the present study, the international team led by Professor Jindrich Cinatl (of Goethe University Frankfurt and the Dr. Petra Joh-Research Institute) and Professor Martin Michaelis (School of Biosciences, University of Kent) has identified nitroxoline, a well-tolerated antibiotic, as a potential treatment alternative for the mpox virus based on experiments using cell culture and skin explant models.
Nitroxoline is also effective against a tecovirimat-resistant strain of the mpox virus, as well as other bacterial and viral pathogens that are frequently co-transmitted with mpox viruses, meaning it simultaneously suppresses multiple pathogens that are often involved in severe courses of mpox. Since nitroxoline is a well-tolerated antibiotic that has long been used to treat humans, it can be tested directly against mpox in clinical trials.
"The emergence of resistant virus strains is a cause of great concern," says Professor Jindrich Cinatl of Goethe University and the Dr. Petra Joh-Research Institute. "It is very reassuring that nitroxoline is effective against a tecovirimat-resistant virus."
Professor Martin Michaelis of the University of Kent adds: "The more different drugs become available to treat viral diseases, the better. We hope that nitroxoline will turn out to be an effective treatment for mpox patients."
Publication: Denisa Bojkova, Nadja Zöller, Manuela Tietgen, Katja Steinhorst, Marco Bechtel, Tamara Rothenburger, Joshua Kandler, Sandra Ciesek, Holger Rabenau, Jindrich Cinatl (Goethe University Frankfurt); Mark Wass, Martin Michaelis (University of Kent); Julia Schneider, Victor Corman (Charité Berlin), Repurposing of the antibiotic nitroxoline for the treatment of mpox. In: Journal of Medical Virology
DOI: https://doi.org/10.1002/jmv.28652
Further information
Prof. Jindrich Cinatl
Working Group Head
Institute for Medical Virology
Goethe University
Tel.: +49 (0)69 6301-6409
E-Mail Cinatl@em.uni-frankfurt.de
https://www.kgu.de/einrichtungen/institute/zentrum-der-hygiene/medizinische-virologie/forschung/research-group-cinatl/
Editor: Dr. Anke Sauter, Science Editor, PR & Communication Office, Tel: +49 (0)69 798-13066, Fax: +49 (0) 69 798-763 12531, sauter@pvw.uni-frankfurt.de
Award ceremony in Frankfurt’s Paulskirche – Acknowledgement of Frederick W. Alt and David G. Schatz, winners of the main prize, and of Leif S. Ludwig, winner of the Early Career Award
The 2023 Paul Ehrlich and Ludwig Darmstaedter Prize, worth €120,000, will today be awarded to immunologists Frederick W. Alt and David G. Schatz in Frankfurt's Paulskirche for their discovery of molecules and mechanisms that enable our immune system to perform the astonishing feat of recognizing billions of different bacterial, viral and other antigens on first contact. The Early Career Award goes to Leif S. Ludwig, biochemist and physician, for a method he has devised to analyze the origin and development of human blood cells, which also include the cells of the immune system.
Unlike more primitive organisms, jawed vertebrates like we humans not only have an innate immune system but also an adaptive one that is capable of preparing itself for all kinds of invaders. This is because – at some point in the course of evolution – one of our ancestors apparently succeeded in taming a DNA parasite that had implanted itself in his genome. This is how the parasite became the gene for an enzyme that advanced to become the command center of immunological diversity. This enzyme, RAG1/2, excises fragments from the DNA of certain chromosomes in maturing immune cells (lymphocytes) and recombines them to form functional genes in a random process. This somatic recombination multiplies the variability of antibodies and T cell receptors. It is a prerequisite for our body's ability to build around ten billion different antibodies, although it only has about 20,000 protein blueprints in the form of genes. David G. Schatz discovered the RAG1/2 enzyme, Frederick W. Alt the enzymes that repair the DNA excised by it. “In decades of research, Alt and Schatz have shed light on the previously hidden evolution of our adaptive immunity, and in so doing they have raised our knowledge of the development of the immune system to a new level," says Professor Thomas Boehm, Chairman of the Scientific Council of the Paul Ehrlich Foundation, commending the achievements of the two winners of the main prize.
The RAG1/2 enzyme is the motor for somatic recombination. Without it, neither functional B and T cells nor effective adaptive immunity can develop. Many cases of severe immunodeficiency are caused by mutations of the RAG genes, and some lymphomas and leukemias are associated with malfunctions of the enzymes encoded by these genes. This makes understanding not only the molecular mechanism but also their evolutionary origin and how they behave in the living cell nucleus even more important. According to Schatz's findings, RAG1/2 originates from a gene that began jumping at will through the genome of our very early ancestors millions of years ago, like a kind of selfish parasite. In structural biology studies, Schatz has traced these jumps (transposons) over several stages of evolution. He has shown which biochemical tricks we vertebrates used to fix the jumping RAG1/2 gene at a certain position and harness it for the immune system.
As they migrate through the cell nucleus of immature lymphocytes, RAG enzymes draw together chromatin clusters, in which the DNA is coiled up in a space-saving way, temporarily and again and again to form recombination centers. There, they perform chromatin scanning, which Alt has described for the first time. They draw a chromatin thread, which can be over a million DNA letters long, through the recombination center like a loop. The result is that gene segments previously far apart are suddenly opposite each other and can be joined firmly together.
The B and T lymphocytes, on which acquired immunity rests, are components of our blood, in which at least 500 billion old cells per day are replaced by new ones in a healthy person. They originate from hematopoietic stem cells in the bone marrow and then mature on divergent developmental trajectories over several stages, like all other blood cells. Determining the resulting lineages and relationships is highly interesting for medicine, for example for identifying at which branch point a leukemia cell forms. Leif S. Ludwig, the winner of this year's Early Career Award, has devised a method that opens up the possibility for the first time for medicine to do this relatively inexpensively, quickly and reliably. Ludwig's method, which has already been tested on individual patients, combines the analysis of mutations in mitochondria with the latest technologies for the gene sequencing of individual cells.
2023 Paul Ehrlich and Ludwig Darmstaedter Prize
https://www.uni-frankfurt.de/124912621/2023_Alt_Schatz
Dr. Frederick W. Alt is Charles A. Janeway Professor of Pediatrics and Director of the Program in Cellular and Molecular Medicine at Boston Children's Hospital, a Howard Hughes Medical Institute Investigator, and Professor of Genetics at Harvard Medical School.
https://www.childrenshospital.org/research/labs/alt-laboratory-research
Dr. David G. Schatz is Professor of Molecular Biophysics and Biochemistry at Yale University and Chairperson of the Department of Immunobiology at Yale School of Medicine.
https://medicine.yale.edu/profile/david-schatz/
2023 Paul Ehrlich and Ludwig Darmstaedter Early Career Award
https://www.uni-frankfurt.de/131228185/2023_Ludwig
Dr. Leif S. Ludwig is the leader of the Emmy Noether Junior Research Group “Stem Cell Dynamics and Mitochondrial Genomics" at the Berlin Institute of Health at Charité and the Max Delbrück Center. https://www.mdc-berlin.de/de/ludwig
Further information:
Press Office Paul Ehrlich Foundation
Joachim Pietzsch
Tel.: +49 (0)69 36007188
j.pietzsch@wissenswort.com
www.paul-ehrlich-stiftung.de
Editors: Joachim Pietzsch / Dr Markus Bernards, Science Editor, PR & Communication Department, Tel: +49 (0) 69 798-12498, Fax: +49 (0) 69 798-763 12531, bernards@em.uni-frankfurt.de.