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Goveas, L.

Publications and source records attributed to Goveas, L..

4 recordsLinked to original sources

Insights into gadolinium uptake and release dynamics of a macrocyclic contrast agent in blood cells

BackgroundGadolinium-based contrast agents (GBCAs) are routinely used in magnetic resonance imaging (MRI). Although macrocyclic GBCAs were initially considered biologically inert, it is now known that a fraction of patients retains gadolinium (Gd) for prolonged periods in tissues such as blood, bone, and brain. Because the first cellular interactions of GBCAs occur in the bloodstream, this study aimed to elucidate the uptake mechanism but also the intracellular persistence and release dynamics of gadoterate meglumine, one of the most widely used macrocyclic agents, in white blood cells (WBCs). Methodology and principal findingsWBCs and K562 cells were incubated with gadoterate meglumine under different conditions to investigate its cellular entry mechanisms. Uptake of the contrast agent was quantified by measuring intracellular Gd using single-cell inductively coupled plasma mass spectrometry (SC-ICP-MS). Time and concentration-dependent incubation of K562 cells revealed saturable uptake kinetics consistent with a Michaelis-Menten model which is independent of the phase of the cell cycle. Gadoterate meglumine uptake in both WBCs and K562 cells was shown to be an active process, as uptake was strongly reduced or abolished at low temperature (16{degrees}C and 4{degrees}C) and in the presence of metabolic inhibitors (sodium azide and 2-deoxyglucose). Co-incubation with multiple endocytosis inhibitors (Dyngo 4a, Dynole 2-24 and chlorpromazine) did not significantly decrease intracellular Gd levels in K562 cells and caused only a slight reduction in WBCs, indicating that endocytosis is not the main entry pathway for gadoterate meglumine in these cells. Furthermore, we assessed the retention time of the Gd inside the cells, showing that only after 24 hours post incubation 80% percent of the intracellular Gd was released through an active process. Finally, we demonstrate that one of the mechanisms of Gd release from WBCs involves extracellular vesicles, which may substantially increase its potential for downstream accumulation in different tissues, including immunoprivileged tissues like brain. SignificanceThe observed time-dependent accumulation, temperature and energy dependence of gadoterate meglumine uptake demonstrate that active cellular mechanisms are primarily responsible for GBCA internalization. Furthermore, our results indicate that macropinocytosis, phagocytosis, and clathrin-mediated endocytosis are not the primary routes of gadoterate meglumine entry. Hereby, we also describe that Gd externalization is an active process involving extracellular vesicles which may influence the Gd distribution in different tissues and its consequent long-term retention. Further studies are required to explore strategies to block this process in order to mitigate potential long-term gadolinium retention.

cell biology↗

The phosphorylation status of LRRK2 at the S910/S935 cluster determines its sensitivity to activation by RAB29

Leucine-Rich Repeat Kinase 2 (LRRK2) is a signaling molecule involved in Parkinsons disease pathomechanisms. In disease, the LRRK2 protein displays both a toxic gain of kinase function and a loss of phosphorylation at heterophosphosites found in an extended loop of the LRR domain. RAB GTPases, such as RAB29, have been identified as upstream activators of LRRK2. Indeed, co-expression of LRRK2 with RAB29 induces a hyperactivation of LRRK2 kinase activity, however the role of the LRRK2 heterologous phosphorylation status in its activation remains unknown. Here, our aim was to determine the role of LRRK2 heterologous phosphorylation on its activation by RAB29. Using single and compound phosphodead or phosphomimetic mutants of LRRK2 we show differential sensitivity of LRRK2 phosphomutants to activation by RAB29, with phosphodead mutants being more susceptible to be activated than phosphomimetic mutants. Interestingly, we find that the single phosphodead S910A LRRK2 mutant displays an activation of LRRK2 kinase activity similar to that observed for the compound phosphodead 6xS>A LRRK2 mutant (S860A/S910A/S935A/S955A/S973A/S976A). Time-course analysis revealed that phosphodead mutants displayed higher but also faster activation by RAB29. In addition, both physical interaction between LRRK2 and RAB29 as well as RAB29-induced recruitment of LRRK2 to the trans-Golgi network (TGN) was enhanced by phosphodead compared to phosphomimetic mutants. To confirm effects on native LRRK2, we tested a panel of ten nanobodies targeting LRRK2 that stabilized LRRK2 phosphorylation at varying levels. Nanobodies stabilizing LRRK2 at low S935 phosphorylation levels showed enhanced RAB29-induced activation compared to nanobodies not affecting pS935 LRRK2. Finally, we tested whether LRRK2 heterologous phosphorylation could affect centrosome cohesion deficits, a phenotype that has been linked to LRRK2 hyperactivation, and found that both the phosphodead LRRK2 as well as a nanobody stabilizing dephosphorylated LRRK2 enhanced the centrosome cohesion deficit. Our findings indicate that hyperactivability of LRRK2 is directly related to its heterologous phosphorylation status, with dephosphorylation leading to strong hyperactivation of LRRK2 by upstream activating RABs, and phosphorylated LRRK2 showing the opposite. This implies that strategies favoring LRRK2 phosphorylation will have therapeutic benefit.

neuroscience↗

Multi-cohort, cross-species urinary proteomics reveals signatures of LRRK2 dysfunction in Parkinsons disease

Pathogenic mutations in Leucine-rich repeat kinase 2 (LRRK2) are the predominant genetic cause of Parkinsons disease (PD) and often increase kinase activity, making LRRK2 inhibitors promising treatment options. Although LRRK2 kinase inhibitors are advancing clinically, non-invasive readouts of LRRK2-linked pathway modulation remain limited. Profiling urinary proteomes from 1,215 individuals across three cohorts and integrating whole-genome sequencing from >500 participants to map genotype-proteome associations, we identified 177 urinary proteins associated with pathogenic LRRK2, enriched for lysosomal/glycosphingolipid, immune, and membrane-trafficking pathways. Machine learning narrowed the features to a cohort-agnostic 30-protein panel that classified G2019S carriers with a mean ROC AUC of 0.91 across independent tests. To evaluate translation, we performed multi-organ and urinary proteomics in rat gain- and loss-of-function models (BAC-LRRK2G2019S and Lrrk2KO) and after Lrrk2 inhibition (MLi-2 and PF-475), revealing tissue-specific responses--strongest in kidney--and cross-species overlap, including 24 brain proteins detectable in human urine. Rat-derived perturbations predicted LRRK2 mutation status in patients (AUC 0.75) and reversed with Lrrk2 inhibition, supporting their pharmacodynamic utility. Together, our findings establish urine as a scalable, non-invasive matrix that captures systemic and brain-relevant consequences of LRRK2 dysfunction and nominate candidate pharmacodynamic markers set to support LRRK2-directed trials.

systems biology↗

Functional analyses of two novel LRRK2 pathogenic variants in familial Parkinson's disease

BackgroundPathogenic variants in the LRRK2 gene are a common monogenic cause of Parkinsons disease. However, only seven variants have been confirmed to be pathogenic. ObjectivesWe identified two novel LRRK2 variants (H230R and A1440P) and performed functional testing. MethodsWe transiently expressed wildtype, the two new variants, or two known pathogenic mutants (G2019S and R1441G), in HEK-293T cells, with or without LRRK2 kinase inhibitor treatment. We characterized the phosphorylation and kinase activity of the mutants by western blotting. Thermal shift assays were performed to determine the folding and stability of the LRRK2 proteins. ResultsThe two variants were found in two large families and segregate with the disease. They display altered LRRK2 phosphorylation and kinase activity. ConclusionsWe identified two novel LRRK2 variants which segregate with the disease. The results of functional testing lead us to propose these two variants as novel causative mutations for familial Parkinsons disease.

genetics↗