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DTSTART;TZID=Europe/Madrid:20240301T100000
DTEND;TZID=Europe/Madrid:20240301T110000
DTSTAMP:20260430T165838
CREATED:20240219T144047Z
LAST-MODIFIED:20240222T105448Z
UID:115601-1709287200-1709290800@ibecbarcelona.eu
SUMMARY:PhD Discussions: Alba Herrero y Clement Hallopeau
DESCRIPTION:Molecular imaging to unveil the pathophysiology of metabolic associated fatty liver disease\nAlba Herrero\, Molecular Imaging for Precision Medicine group \nMetabolic-associated fatty liver disease (MAFLD)\, a progressive liver condition rapidly rising to lead to chronic liver disease worldwide\, manifests as metabolic dysregulation\, leading to steatosis\, fibrosis\, and cirrhosis if left untreated. Beyond the liver\, it induces high BMI\, insulin resistance\, and elevated plasma glucose amongst others. Age\, genetics\, and sex influence its clinical presentation\, hindering biomarker detection. Currently\, real-time metabolic monitoring is not readily available in clinical settings. Hyperpolarized Magnetic Resonance Spectroscopic Imaging (HP-MRSI) boosts MR signals\, allowing for real-time metabolic tracking of 13C-labelled substrates\, such as pyruvate\, posing as a solution to this problem.\nWe delineated 6 study groups to evaluate the effects on liver metabolism of specific MAFLD risk factors\, these being diet\, sex\, and genetics. Subjects were monitored throughout the experiment for signs of insulin resistance\, increased plasma glucose\, and BMI levels as MAFLD indicators. Analyzed with a 3T preclinical MRI scanner\, and after injection of hyperpolarized [1-13C]-pyruvate\, the metabolism of pyruvate was tracked in situ\, probing downstream metabolic products such as lactate and alanine.\nMetabolic imaging has the potential to be used in clinical settings to diagnose and track metabolic dysfunctions. Real-time monitoring of pyruvate metabolism using HP-MRSI has revealed alterations across various metabolic conditions\, displaying its clinical potential. \n\nMechanisms of mechanical compartmentalisation in intestinal organoids\nClement Hallopeau\, Integrative Cell and Tissue Dynamics group \nMonolayers of intestinal organoids recapitulate the functional compartmentalisation seen in-vivo.\nCrypt-like regions host stem cells\, Paneth cells and transit amplifying cells\, whereas villus-like regions contain differentiated cells. Measurements of traction forces in these organoids have\nestablished that stem cells push the underlying substrate while the transit-amplifying cells pull it\, defining clear mechanical and functional compartments (Pérez-González\, Ceada et al\, Nat Cell Bio\, 2021). Crypt-villus compartmentalisation is attributed to opposed gradients in Eph/ephrin signaling\, but how these gradients are linked to the mechanical pattern is unknown. To address this question\, we studied the mechanical and functional compartmentalisation in organoids derived from mice lacking EphB2 and EphB3 (EphB2-/-\, EphB3-/-). We found that\, unlike in wild type organoids (WT)\, crypts of EphB2-/-EphB3-/- organoids (KO) expand at the expense of the villuslike region. This phenotype is associated to an increased proliferation of the KO crypts and a decreased expression of the stemness marker olfm4. In mechanical terms\, the 3D traction pattern of the KO crypts is qualitatively similar to the WT\, but forces have a decreased amplitude\, suggesting a decreased tension around the KO crypts. Taken together\, these data establish a link between the mechanical features and the size homeostasis of the functional compartments of the intestinal organoid\, governed by Eph/ephrin signaling.
URL:https://ibecbarcelona.eu/es/event/phd-discussions-alba-herrero-y-clement-hallopeau/
LOCATION:Sala Dolors Aleu\, Cluster II\, IBEC\, Baldiri i Reixac\, Barcelona
CATEGORIES:PhD Discussions Session
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DTSTART;TZID=Europe/Madrid:20240308T100000
DTEND;TZID=Europe/Madrid:20240308T110000
DTSTAMP:20260430T165838
CREATED:20240222T115452Z
LAST-MODIFIED:20240222T115452Z
UID:115629-1709892000-1709895600@ibecbarcelona.eu
SUMMARY:IBEC Seminar: Agathe Chaigne
DESCRIPTION:Molecular and mechanical regulation of abscission in stem cells\nAgathe Chaigne\, PhD.\, Group leader. Cell Biology\, Neurobiology and Biophysics department\, Utrecht University\, The Netherlands \nAbscission is the last step of cell division leading to the complete separation of the two sister cells and consists in the cutting of a cytoplasmic bridge. Abscission is mediated by the membrane remodelling machinery ESCRT which also triggers the severing of a thick bundle of microtubules that needs to be cleared prior to abscission. Here\, we use mouse embryonic stem cells\, which transition from slow to fast abscission during exit from naïve pluripotency to investigate the molecular mechanism for abscission dynamics. We identify a feedback loop between the activity of Aurora B\, mechanics\, and microtubule stability as a main regulator of abscission speed.  
URL:https://ibecbarcelona.eu/es/event/ibec-seminar-agathe-chaigne/
LOCATION:Sala Dolors Aleu\, Cluster II\, IBEC\, Baldiri i Reixac\, Barcelona
CATEGORIES:IBEC Seminar
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DTSTART;TZID=Europe/Madrid:20240314T090000
DTEND;TZID=Europe/Madrid:20240314T170000
DTSTAMP:20260430T165838
CREATED:20240312T151616Z
LAST-MODIFIED:20240313T155224Z
UID:115981-1710406800-1710435600@ibecbarcelona.eu
SUMMARY:ICMS-IBEC Symposium
DESCRIPTION:Dear all\, \n  \nIt is our pleasure to invite you to the ICMS-IBEC symposium on 14 March from 13.00 – 17.00 (Ceres 0.31\, coffee starts at 12.45). Colleagues from both IBEC and ICMS will pitch their research domains with the intent to get better acquainted with each other’s science. We have fostered a successful collaboration for more than 4 years and we hope that this event will stimulate additional bottom-up connections between researchers from both organizations. \nYou can find the full programme here. \nYou can join the symposium online (no need to register)\, by using this link. \n 
URL:https://ibecbarcelona.eu/es/event/breaking-boundaries-in-science-icms-annual-symposium-2024/
LOCATION:Online
CATEGORIES:Joint seminar / workshop / symposium
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BEGIN:VEVENT
DTSTART;TZID=Europe/Madrid:20240322T120000
DTEND;TZID=Europe/Madrid:20240322T130000
DTSTAMP:20260430T165838
CREATED:20240319T141525Z
LAST-MODIFIED:20240319T141525Z
UID:116181-1711108800-1711112400@ibecbarcelona.eu
SUMMARY:IBEC Seminar: Emilio Parisini
DESCRIPTION:Engineering enzymes for biomedical and biotechnological applications\nEmilio Parisini\, Latvian Institute of Organic Synthesis (Riga\, Latvia)\, University of Bologna (Italy) \nEnzyme engineering has the potential to improve the activity\, the stability and the substrate recognition of enzymes. As such\, it paves the way for the design of novel enzymes with improved performances for a wide range of applications. This rational approach can accelerate the production and the use of biocatalysts in different biotechnological sectors\, thus in turn allowing the improvement of chemical processes through the application of green chemistry concepts.  In this talk\, two examples from our current research will be discussed: \nFructosyl Peptide Oxidases (FPOX) are deglycating enzymes that find application as key enzymatic components in diabetes monitoring devices. Indeed\, their use with blood samples can provide a measurement of the concentration of glycated hemoglobin and glycated albumin\, two well-known diabetes markers. However\, the FPOX currently employed in enzymatic assays cannot directly detect whole glycated proteins\, making it necessary to perform a preliminary proteolytic treatment of the target protein to generate small glycated peptides that can act as viable substrates for the enzyme. This is a costly and time consuming step. The rapidly growing demand for cheap\, efficient and rapid diabetes monitoring tests could be met by developing enzymatic assays for glycated hemoglobin and albumin that do not require a preliminary digestion of the proteins. In our lab\, we used an in silico protein engineering approach to enhance the overall thermal stability of the enzyme and widen it active site to improve its catalytic activity toward large substrates. \nThe fast and uncontrolled accumulation of plastic waste in the environment has long begun to impact on the natural ecosystems and to pose an existential threat to all forms of life on our planet. Advanced technical solutions to the plastic waste management problem are therefore in urgent demand. To this end\, enzymatic approaches to plastic degradation hold great promises as novel and more efficient enzymes are constantly being developed. Leaf-branch Compost Cutinase (LCC)\, a naturally occurring PETase\, has been reported to outperform all other known PET-degrading enzymes and to present a melting temperature (Tm) of 84.7°C. This enzyme has been noticeably engineered in 2020\, leading to the so-called ICCG variant (Tm = 94.0°C)\, the current gold standard. In our lab\, we engineered a LCC that features significantly enhanced PETase activity and thermal stability relative to the gold standard ICCG.
URL:https://ibecbarcelona.eu/es/event/ibec-seminar-emilio-parisini/
LOCATION:Sala Dolors Aleu\, Cluster II\, IBEC\, Baldiri i Reixac\, Barcelona
CATEGORIES:IBEC Seminar
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