<p><strong>In closed communities such as the Amish in North America, rare genetic disorders occur more frequently. In children from this community, a condition has been described that affects the development of the nervous system and manifests, for example, as muscle weakness or epileptic seizures. The disorder is linked to a small change in a single protein, but for a long time it was unclear which cellular process this change disrupts. This question has now been answered by researchers from CEITEC Masaryk University, who show that the disease is caused by a disruption of a key mechanism required for the proper processing of genetic information in the cell.</strong></p><p>Every cell must first transcribe genetic information and then modify it before it can be used. From the original “working transcript,” unnecessary parts are removed and the remaining pieces are precisely joined together. This process, known as RNA splicing, consists of many consecutive steps and is tightly regulated. If the process does not proceed correctly or stops at any point, the cell cannot properly convert the copied genetic information into a usable form and therefore cannot function as it should.</p><p>Researchers from CEITEC Masaryk University have now described one of the key steps in this process – <strong>a specific signal inside the cell</strong>. This signal acts as a checkpoint: only once it is fulfilled, the entire mechanism is activated and the process can continue.</p><p><i>“We showed that during RNA splicing, a chemical modification of the protein SF3B1 is required at a precisely timed step. This modification allows another protein, SNIP1, to bind. If this signal is not transmitted correctly, the cell cannot proceed with the splicing process,”</i> explains first author<strong> </strong><a target="_blank" rel="noopener noreferrer" href="https://www.ceitec.eu/pavla-gajduskova-ph-d/u26136?page=publication"><strong>Pavla Gajdušková</strong></a>.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_4_79e003984a.jpeg" alt="CEITEC: A Rare Genetic Disorder in the Amish Community Helped Confirm a Key Cellular Mechanism: Pavla Gajdušková" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_4_79e003984a.jpeg 235w," sizes="100vw" width="1600" height="1067"></p><p>This is where the research connects to patients in the Amish community. In affected children, a <strong>small genetic change in the SNIP1 protein </strong>disrupts its ability to respond properly to the signal mediated by the modified SF3B1 protein, <strong>making RNA splicing less efficient than in healthy individuals</strong>. As a result, errors occur during RNA splicing that the cell cannot correct, impairing its function – especially in the nervous system.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_44a7e2ef17.jpg" alt="CEITEC/Blažek Lab: A Rare Genetic Disorder in the Amish Community Helped Confirm a Key Cellular Mechanism: Interaction between SF3B1 and SNIP1 proteins." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_44a7e2ef17.jpg 156w," sizes="100vw" width="1600" height="1600"><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_2_85826d711e.jpg" alt="CEITEC/Blažek Lab: A Rare Genetic Disorder in the Amish Community Helped Confirm a Key Cellular Mechanism: The effect of mutations in SNIP1 on cell proliferation." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_2_85826d711e.jpg 235w," sizes="100vw" width="1600" height="1067"></p><p>The researchers were thus able to clarify the cause of this rare neurodevelopmental disorder. <i>“Additionally, the cause of this disease also confirms the correctness of the checkpoint we described. It shows that even a small change in one of the proteins involved can disrupt the RNA splicing mechanism on which the cell depends,”</i> adds group leader <a target="_blank" rel="noopener noreferrer" href="https://www.ceitec.eu/dalibor-blazek-ph-d/u25918"><strong>Dalibor Blažek</strong></a>.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_3_f95cfd68eb.jpeg" alt="CEITEC/Martin Indruch: A Rare Genetic Disorder in the Amish Community Helped Confirm a Key Cellular Mechanism: Dalibor Blažek." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vzacna_geneticka_porucha_z_amisske_komunity_pomohla_potvrdit_klicovy_mechanismus_v_bunce_3_f95cfd68eb.jpeg 235w," sizes="100vw" width="1600" height="1067"></p><p>Although the study focuses on basic research, its implications are broader. It suggests that the same mechanism may also play a role in regulating cell division – a process that is often disrupted in cancer.</p><blockquote><p>The research was carried out by scientists from <strong>CEITEC Masaryk University </strong>in collaboration with researchers from Spain and Germany. The study was published in the journal <a target="_blank" rel="noopener noreferrer" href="https://www.nature.com/articles/s41467-026-71119-2">Nature Communications</a>.</p></blockquote>

A Rare Genetic Disorder in the Amish Community Helped Confirm a Key Cellular Mechanism

<p><strong>This study investigates the pathogenesis of neurosyphilis through cerebrospinal fluid proteomics using LC–MS/MS and ELISA validation. Comparative analysis identified 234 differentially expressed proteins, with major alterations linked to lysosomal dysfunction, axon guidance, and neurodegeneration pathways.</strong></p><p>Key lysosomal proteins, including PSAP and DNASE2, together with the axonal protein EPHA4, were significantly downregulated in neurosyphilis patients. These proteins showed potential as biomarkers for neurodegeneration and may provide new insights into disease mechanisms, diagnostics, and therapeutic targets.</p><blockquote><h4><strong>The original article</strong></h4><h4><a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689"><strong>Cerebrospinal Fluid Proteome Reveals Dysregulation of Lysosomal and Axonal Proteins in Neurosyphilis</strong></a></h4><p>Huayang Tang*, Junjie Hu, Yifan Wu, Jinping Gao, Wenjun Wang, Xiaodong Zheng, Ran Zhang, Bo Liang, Fusheng Zhou, Ze Guo*</p><p>J. Proteome Res. 2026, 25, 2, 713–722</p><p><a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1021/acs.jproteome.5c00689">https://doi.org/10.1021/acs.jproteome.5c00689</a></p><h6>licensed under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/"><strong>CC-BY 4.0</strong></a></h6></blockquote><p><strong>Selected sections from the article follow. Formats and hyperlinks were adapted from the original.</strong></p><div><p>Neurosyphilis (NS) is a group of clinical syndromes characterized by neuroinflammation caused by <i>Treponema pallidum</i> (<i>T. pallidum</i>), which occurs in all stages of syphilis. <a href="javascript:void(0);">(1,2)</a> NS is classified based on clinical presentation as either asymptomatic (ANS) or symptomatic (SNS), and based on disease stage as either early (occurring 1–2 years after primary infection) or late. <a href="javascript:void(0);">(1)</a> <i>T. pallidum</i> can cause local nonspecific and central nervous system (CNS) inflammation, leading to possible degenerative changes. <a href="javascript:void(0);">(3)</a> The immune response of CNS in neurosyphilis is comparable to that observed in other neuroinflammatory diseases. Consequently, the presence of neurological symptoms may not reliably indicate active CNS inflammation in syphilis patients. <a href="javascript:void(0);">(3)</a> A cerebrospinal fluid (CSF) proteomic study identified three biomarkers (SEMA7A, SERPINA3, and ITIH4) that contribute to NS and have potential implications for diagnosis and therapeutic strategies. <a href="javascript:void(0);">(4)</a> Through integrated proteomics and single-cell transcriptomics analyses, Toll-like/NF-κB signaling was identified as the key pathway involved in CNS damage caused by <i>T. pallidum</i>. <a href="javascript:void(0);">(5)</a> Despite an increasing understanding of the biomarkers and possible neuroinflammatory damage mechanisms of neurosyphilis, the mechanisms of neurodegeneration caused by <i>T. pallidum</i> infection remain elusive. <a href="javascript:void(0);">(6)</a></p><p>Patients with neurosyphilis exhibit stage-specific profiles of soluble factors in their CSF, which are linked to both immune status and the extent of neuronal damage. <a href="javascript:void(0);">(7)</a> In this study, we analyzed differentially expressed proteins (DEPs) in the CSF proteomes from 28 individuals, including neurosyphilis (NS), suspected neurosyphilis (spNS) and non-neurosyphilis (nNS) individuals, by LC–MS/MS and analyzed a public data set of the neurosyphilis CSF proteome. Validation was then performed by ELISA in an independent group comprising 110 samples. The results revealed that neuroinflammation by <i>T. pallidum</i> infection results in dysregulation of the key proteins in lysosomal and axonal pathway, which suggesting a potential contribution to neurodegeneration in neurosyphilis.</p><h4><strong>Materials and Methods</strong></h4><h5><strong>LC–MS/MS</strong></h5><p>The tryptic peptides were dissolved in 0.1% formic acid (solvent A) and loaded onto a custom-made reversed-phase column (15 cm × 75 μm). Using an <strong>EASY-nLC 1000 UPLC system</strong>, a gradient was run at 400 nL/min as follows: 6% to 23% solvent B (0.1% formic acid in 98% acetonitrile) over 26 min, 23% to 35% in 8 min, up to 80% in 3 min, and held at 80% for 3 min. Peptides were ionized via an NSI source at 2.0 kV and analyzed online by a <a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/products/559"><strong>Q Exactive Plus mass spectrometer</strong></a><strong>.</strong> Full scans (<i>m</i>/<i>z</i> 350–1800) were acquired in the Orbitrap at 70,000 resolution. The top precursors were selected for MS/MS with an NCE of 28, and fragments were detected at 17,500 resolution. A data-dependent method cycled between one MS scan and 20 MS/MS scans with a 15.0 s dynamic exclusion. AGC was set at 5E4. MS/MS data were processed with MaxQuant (v.1.5.2.8) using Trypsin/P as the enzyme (up to 2 missed cleavages). Precursor mass tolerance was 20 ppm (first search) and 5 ppm (main search); fragment mass tolerance was 0.02 Da. Fixed modification: carbamidomethyl (C); variable modification: oxidation (M). The FDR threshold was &lt;1%, and the minimum peptide score was &gt;40.</p><h5><strong>ELISA</strong></h5><p>CSF levels of host proteins were quantified using commercial ELISA kits according to the manufacturers’ protocols. Proteins analyzed included PSAP (OKEH07124, Aviva, USA), CTSL (abx150963, Abbexa, UK), NPC2 (A-QEK07857, Biogradetech, USA), and DNASE2 (abx386953, Abbexa, UK). Briefly, 100 μL of CSF was added to precoated plates and incubated at 37 °C for 2 h. After washing, 100 μL of detection antibody was added to each well and incubated at 37 °C for another 2 h. Following a wash, 100 μL of streptavidin-HRP working solution was added and incubated at room temperature for 20 min in the dark. The reaction was stopped with 50 μL of stop solution, and the optical density was measured at 450 nm.</p><h4><strong>Results</strong></h4><h5><strong>Downregulation of Key Lysosomal Proteins in CSF from Patients With Neurosyphilis</strong></h5><p>By analyzing the DEPs in NS vs nNS, we observed a significant enrichment of downregulated proteins in the lysosome pathway (<i>P</i> = 0.007) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>A), with 9 lysosomal proteins showing significant downregulation (<i>P</i><sub>adj</sub> &lt; 0.05) in the NS group (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S4</a>). To validate this finding, we examined the public CSF proteomics data set of neurosyphilis (PXD033034) and identified 18 proteins in the lysosomal pathway that were significantly downregulated in patients with NS (<i>P</i><sub>adj</sub> &lt; 0.05) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S4</a>). PPI network analysis determined the top 10 hub genes within the lysosome pathway (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>B). A Venn diagram revealed 3 proteins (PSAP, CTSL, and NPC2) shared across our current data, the public data set (PXD033034) and the top 10 hub genes (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>C). The mass spectrometry results indicated that the levels of PSAP (<i>P</i><sub>adj</sub> = 0.043), CTSL (<i>P</i><sub>adj</sub> = 0.028) and NPC2 (<i>P</i><sub>adj</sub> = 0.013) were significantly lower in the NS group compared to the nNS group (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>D). The PXD033034 data set revealed consistent changes in the PSAP, CTSL, and NPC2 levels in the NS group (<i>P</i><sub>adj</sub> &lt; 0.05) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Figure S1 and Table S4</a>). In addition, associations between the lysosomal protein DNASE2 and NS were observed in both the present study (<i>P</i><sub>adj</sub> = 0.003) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>D) and the PXD033034 data set (<i>P</i><sub>adj</sub> &lt; 0.05) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Figure S1 and Table S4</a>), with subgroup analysis revealing a significantly lower expression level of DNASE2 in the SNS group compared to the ANS group (<i>P</i> = 0.035) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>D and <a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S3</a>). Further validation by ELISA (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S5</a>) in an independent group (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#tbl1">Table 1</a>) confirmed significantly downregulated CSF levels of PSAP (<i>P</i> &lt; 0.0001), CTSL (<i>P</i> &lt; 0.0001), NPC2 (<i>P</i> = 0.0024) and DNASE2 (<i>P</i> &lt; 0.0001) in patients with NS (n = 21) than in nNS individuals (n = 56) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>E) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S6</a>), as well as decreased in the SNS subgroup (<i>P</i> &lt; 0.05) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Figure S2 and Table S6</a>). Receiver operating characteristic (ROC) curve analysis supported PSAP (AUC = 0.91, 95% CI: 0.83–0.99) and DNASE2 (AUC = 0.95, 95% CI: 0.91–0.99) for distinguishing NS from nNS and as potential biomarkers for assessing neurodegeneration in NS (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>F). These results indicate that <i>T. pallidum</i> infection may lead to lysosomal dysfunction in CNS.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/J_Proteome_Res_2026_25_2_713_722_Figure_2_Downregulation_of_key_lysosomal_proteins_in_the_cerebrospinal_fluid_of_neurosyphilis_patients_bbccd95f44.jpg" alt="J. Proteome Res. 2026, 25, 2, 713–722: Figure 2. Downregulation of key lysosomal proteins in the cerebrospinal fluid of neurosyphilis patients. (a) KEGG pathway analysis demonstrated that downregulated proteins in patients with NS were significantly enriched in the lysosome pathway, as well as in axon guidance and neurodegeneration. (b) The top 10 hub genes involved in the lysosome pathway were identified using the STRING network data set and PPI analysis. (c) A Venn diagram revealed 3 proteins (PSAP, CTSL, and NPC2) shared across our current data, the public data set (PXD033034) and the top 10 hub genes. (d) The CSF levels of PSAP (Padj = 0.043), CTSL (Padj = 0.028), DNASE2 (Padj = 0.003) and NPC2 (Padj = 0.013) were significantly decreased in the NS group than in the nNS group. Subgroup analysis found a significantly lower expression level of DNASE2 in the SNS group than in the ANS group (P = 0.035). (e) PSAP, DNASE2, CTSL and NPC2 levels in CSF were tested by ELISA in the nNS (n = 56) and NS (n = 21) groups. Compared with those in the nNS group, significantly lower PSAP (P &lt; 0.0001), CTSL (P &lt; 0.0001), DNASE2 (P &lt; 0.0001) and NPC2 (P = 0.0024) levels were detected in the NS group. (f) ROC curve analysis for NS revealed that PSAP had an AUC = 0.91 (95% CI: 0.83–0.99), DNASE2 had an AUC = 0.95 (95% CI: 0.91–0.99), CTSL had an AUC = 0.85 (95% CI: 0.76–0.95), and NPC2 had an AUC = 0.72 (95% CI: 0.59–0.85). NS: neurosyphilis; nNS: non-neurosyphilis; ANS: asymptomatic neurosyphilis; SNS: symptomatic neurosyphilis. ROC: receiver operating characteristic; AUC: area under the curve. * P &lt; 0.05, ** P &lt; 0.01, ****P &lt; 0.0001." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_J_Proteome_Res_2026_25_2_713_722_Figure_2_Downregulation_of_key_lysosomal_proteins_in_the_cerebrospinal_fluid_of_neurosyphilis_patients_bbccd95f44.jpg 140w," sizes="100vw" width="2100" height="2339"></p><h5><strong>Downregulation of Key Axonal Proteins Correlated with Lysosomal Protein Reduction in Neurosyphilis CSF</strong></h5><p>Lysosomes play crucial roles in neuronal health by maintaining axonostasis. <a href="javascript:void(0);">(10)</a> The enrichment analysis indicated that the downregulated proteins in NS were implicated in the biological processes of axonostasis (such as axon development and axonogenesis) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig1">Figure 1</a>F) and the pathway of axon guidance (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig2">Figure 2</a>A). Our proteomic data revealed a total of 24 downregulated (<i>P</i><sub>adj</sub> &lt; 0.05) axonal proteins and 1 upregulated (<i>P</i><sub>adj</sub> &lt; 0.05) axonal protein in the CSF of patients with NS (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S9</a>). Furthermore, the PXD033034 data set revealed 55 downregulated (<i>P</i><sub>adj</sub> &lt; 0.05) and 4 upregulated (<i>P</i><sub>adj</sub> &lt; 0.05) axonal proteins in NS (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/suppl/10.1021/acs.jproteome.5c00689/suppl_file/pr5c00689_si_001.zip">Table S9</a>). The top 10 hub genes involved in the biological processes of axon development and axonogenesis were identified by PPI network analysis (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig4">Figure 4</a>A). Considering the overlap of our current data, the PXD033034 data set and the top 10 hub genes (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig4">Figure 4</a>B), one key protein, EPHA4, was identified across 3 data sets, with significant downregulation in our current data (<i>P<sub>adj</sub></i> = 0.011) and in the PXD033034 data set (<i>P<sub>adj</sub></i> = 0.028) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig4">Figure 4</a>C). Correlation analysis further revealed a positive correlation between the levels of PSAP and EPHA4 (<i>r</i> = i 0.83, <i>P</i> &lt; 0.05) (<a target="_blank" rel="noopener noreferrer" href="https://pubs.acs.org/doi/10.1021/acs.jproteome.5c00689#fig4">Figure 4</a>D). Reduced levels of PSAP and EPHA4 in CSF have been implicated in neurodegenerative diseases, including Alzheimer’s disease (AD) and Parkinson’s disease (PD). <a href="javascript:void(0);">(11,12)</a> Our findings suggest that coordinated dysregulation of lysosomal and axonal proteins may contribute to neurodegeneration in NS.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/J_Proteome_Res_2026_25_2_713_722_Figure_4_Key_axonal_protein_downregulated_in_CSF_from_patients_with_neurosyphilis_66f5533e94.jpg" alt="J. Proteome Res. 2026, 25, 2, 713–722: Figure 4. Key axonal protein downregulated in CSF from patients with neurosyphilis. (a) The top 10 hub genes involved in axonostasis were identified by the STRING network data set and PPI analysis. (b) A Venn diagram revealed 1 protein (EPHA4) shared across DEPs related to axonostasis in our current data and in the public data set (PXD033034) and the top 10 hub genes. (c) EPHA4 was significantly downregulated both in our present study (Padj = 0.011) and in the PXD033034 data set (Padj = 0.028). (d) Correlation analysis demonstrated that the EPHA4 level was significantly positively correlated (P &lt; 0.05) with the levels of PSAP (r = 0.83), CTSL (r = 0.6), NPC2 (r = 0.69), DNASE2 (r = 0.61) and SEMA7A (r = 0.83). NS: neurosyphilis; nNS: non-neurosyphilis. * P &lt; 0.05." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_J_Proteome_Res_2026_25_2_713_722_Figure_4_Key_axonal_protein_downregulated_in_CSF_from_patients_with_neurosyphilis_66f5533e94.jpg 178w," sizes="100vw" width="1250" height="1096"></p><h4><strong>Conclusions</strong></h4><p>The present study reveals the associations of dysregulated proteins in lysosomal and axonal pathways with neurosyphilis, and potential evidence of shared pathophysiological mechanisms between neuroinflammation caused by <i>T. pallidum</i> infection and neurodegenerative diseases.</p><p>However, this study has certain limitations. First, the use of ELISA to validate a limited number of proteins has certain limitations, such as the inherent cross-reactivity of ELISA. In the future, we can optimize the validation experiments by adding techniques such as Western blotting for verification. Second, this study uses a cross-sectional sampling method for research, which limits our ability to infer disease progression and treatment responses. In the future, we will conduct follow-up on the subjects, continue collecting cerebrospinal fluid samples after treatment, and observe whether the protein dysregulation is reversible after treatment. For spNS patients, follow-up should also be conducted to determine if they have transformed into NS, which will be very valuable for validating the predictive utility of our biomarkers. Finally, although multiple discovery and validation cohort studies have been conducted, we currently lack direct mechanistic evidence. Future work will investigate whether exposing neural cell coculture models to outer-membrane antigens of <i>T. pallidum</i> reproduces the lysosome and axon alterations observed in CSF, clarifying their role in neural damage of neurosyphilis and potential biomarkers for diagnosis and treatment of neurodegeneration in neurosyphilis.</p></div>

Cerebrospinal Fluid Proteome Reveals Dysregulation of Lysosomal and Axonal Proteins in Neurosyphilis

<p><strong>In the week of May 11, the following webinars await you in the field of liquid phase and especially HPLC and LC/MS.</strong></p><blockquote><h4><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinars"><strong>👉 DETAILS AND REGISTRATION IN THE WEBINARS SECTION</strong></a></h4><p><strong>👉 Search and filter in the largest global database</strong> with over <strong>5 500 GC, LC, MS and spectroscopy webinars</strong>.</p></blockquote><h5><strong>1. Thermo Fisher Scientific: Uncovering Microplastics: Identification, Quantification, and Exposure Assessment</strong></h5><ul><li>Tu, 12.5.2026 08:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6136">Registration</a></li></ul><p>In this webinar, we will explore complementary analytical solutions for comprehensive microplastics characterization.</p><h5><strong>2. Waters Corporation: Size variant analysis of antibodies and ADCs using SEC, SEC-MALS, SEC-MS, and 2D Protein A-SEC Methods</strong></h5><ul><li>Tu, 12.5.2026 17:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6169">Registration</a></li></ul><p>Size-exclusion chromatography (SEC) is essential for analyzing aggregates, monomers, and fragments in biotherapeutic proteins.</p><h5><strong>3. Waters Corporation: Beyond C18 and Phenyl: Expanding Selectivity with Biphenyl Columns Built for UV and pH Robustness</strong></h5><ul><li>We, 13.5.2026 16:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6183">Registration</a></li></ul><p>Discover how modern biphenyl stationary phases improve challenging LC separations with lower UV bleed, broad pH stability, and enhanced recovery of metal-sensitive analytes.</p><h5><strong>4. Milestone: Modern Sample Prep for Organic Contaminants: PAHs, PFAS, MOSH/MOAH in Food</strong></h5><ul><li>We, 13.5.2026 16:00 CET</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/5822">Registration</a></li></ul><p>Learn how microwave-assisted extraction streamlines food analysis of PAHs, PFAS, and MOSH/MOAH, improving recoveries, reducing solvents, and meeting regulatory demands.</p><h5><strong>5. SelectScience: Achieve faster GLP-1 amino acid analysis with rapid UPLC technology</strong></h5><ul><li>We, 13.5.2026 17:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6173">Registration</a></li></ul><p>Accelerate GLP-1 amino acid analysis. Learn how UPLC, microwave hydrolysis and Waters AccQ-Tag solutions speed up drug development and ensure compliance.</p><h5><strong>6. Waters Corporation: Transform Your Daily Lab Operations with Automation - Biomolecules Workflows</strong></h5><ul><li>Th, 14.5.2026 11:00 CEST</li><li><a target="_blank" rel="noopener noreferrer" href="https://lcms.labrulez.com/webinar/6174">Registration</a></li></ul><p>Discover how Andrew+ and OneLab automate complex biomolecule workflows. Learn how labs improve consistency, traceability, and efficiency in oligonucleotide and peptide analysis.</p>

Webinars LabRulezLCMS Week 20/2026

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Since its establishment in 2011, CEITEC has quickly developed into a cutting-edge infrastructure for research which performs highly alongside the best institutes in Europe. Among the main priorities of CEITEC are the promotion of a motivating and dynamic international scientific environment, the provision of state-of-the-art research infrastructure, and the policy of open communication and equal opportunities.

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Phenomenex Axia Preparative LC Columns

Available in over 40 unique achiral and chiral selectivities, Axia advanced preparative column packings and column hardware designs offer several advantages.

<p class="cke-user_style-important"><strong>Guaranteed, Longest Lasting Preparative HPLC and SFC Column</strong></p><p>Available in over 40 unique achiral and chiral selectivities, Axia advanced preparative column packings and column hardware designs offer several advantages. Unlike traditional preparative HPLC column packing methods, the Axia packing method offers increased sorbent bed density for increased performance and eliminates media bed collapse as a source of premature column failure in preparative HPLC/SFC columns.</p><h3><strong>Axia Packed Preparative HPLC Columns</strong></h3><h4><strong>Axia Single Axial Compression Step</strong></h4><p>Axia packed preparative columns involve a single axial compression step, unlike conventional packed preparative columns. The ideal prep HPLC column bed density is custom calculated and automated for each specific media and column size. Computer control of the entire process ensures both proper bed density and column uniformity every time.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Axia_Packing_Technology_1785ff0442.jpg" alt="Phenomenex: Axia Packing Technology" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Axia_Packing_Technology_1785ff0442.jpg 245w," sizes="100vw" width="917" height="560"></p><h4><strong>Unmatched Column Reproducibility</strong></h4><p>The <strong>automated</strong> <strong>Axia™ packing system</strong> provides <strong>feedback control</strong> and <strong>infinite tuning</strong> of packing density for specific media characteristics such as mechanical strength and porosity. An optimum higher bed density can be consistently reproduced column-to-column. This directly translates into consistent efficiency and peak asymmetry measurements and decreases the column variability seen in traditionally packed preparative columns.</p><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Unmatched_Column_Reproducibility_a752be8dd5.jpg" alt="Phenomenex: Unmatched Column Reproducibility" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Unmatched_Column_Reproducibility_a752be8dd5.jpg 245w," sizes="100vw" width="995" height="534"></p><h3><strong>Seamless Scalability to Increase Sample Load</strong></h3><h4><strong>Increase Column Length</strong></h4><p>Increase sample load without increasing your flow rate by using a longer column. With Axia technology, each preparative column is optimized for:</p><ul><li>Analytical-like efficiency</li><li>Long column lifetime</li><li>High sample load with high surface area media such as Kinetex, Aeris, Gemini, Luna, Luna Omega, or Synergi</li></ul><h4><strong>Increase Column ID</strong></h4><p>For maximizing load without increasing the run time, consider scaling up to a larger column ID. Axia packed columns provide the three important benefits you need.</p><ul><li>Reproducible performance across all column diameters</li><li>Increased throughput without sacrificing purity</li><li>High efficiency from analytical to preparative</li></ul><p><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Phenomenex_Increase_Column_ID_a45d7f8aa3.jpg" alt="Phenomenex: Increase Column ID" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_Phenomenex_Increase_Column_ID_a45d7f8aa3.jpg 156w," sizes="100vw" width="908" height="910"></p><h3><strong>Axia Technology Outperforms Traditional Packing Processes!</strong></h3><p>Because of the constant pressure placed on the integrated packing piston, Axia packed columns possess the dynamic capability of maintaining a consistent, homogeneous media bed. This results in superior column performance no matter which media selectivity you choose.</p><h3><strong>How to choose the right column</strong></h3><h5><strong>Acidic Compounds</strong></h5><ul><li>Kinetex XB-C18</li><li>Gemini C18</li></ul><h5><strong>Aromatic</strong></h5><ul><li>Luna Phenyl-Hexyl</li><li>Kinetex Biphenyl</li></ul><h5><strong>Closely Related Compounds</strong></h5><ul><li>Kinetex F5</li><li>Luna PFP(2)</li></ul><h5><strong>Extremely Hydrophobic</strong></h5><ul><li>Kinetex C8</li><li>Luna C8(2)</li></ul><h5><strong>Extremely Polar</strong></h5><ul><li>Luna HILIC(2)</li><li>Kinetex HILIC</li></ul><h5><strong>Hydrophobic Compounds</strong></h5><ul><li>Luna C18(2)</li><li>Kinetex C18</li></ul><h5><strong>Polar Acids</strong></h5><ul><li>Luna Omega Polar C18</li><li>Kinetex Polar C18</li></ul><h5><strong>Polar Bases</strong></h5><ul><li>Luna Omega PS C18</li><li>Kinetex PS C18</li></ul><h5><strong>Sugars</strong></h5><ul><li>Luna NH(2)</li></ul><h5><strong>Chiral</strong></h5><ul><li>Lux i-Amylose-3</li><li>Lux Cellulose-1</li></ul>

Products from category HPLC columns focused on PrepLC from Phenomenex - page 1

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