Pub Date : 2026-01-06Epub Date: 2025-09-29DOI: 10.1016/j.jprot.2025.105541
Maria Pinheiro Spínola , Dina Rešetar Maslov , Ivana Rubić , Mónica Mendes da Costa , Vladimir Mrljak , Madalena Lordelo , André Martinho de Almeida , José António Mestre Prates
Limnospira platensis (Spirulina) is known for its nutritional and bioactive profile, but its high-level dietary inclusion effects in broilers, particularly post-extrusion and enzyme pre-treatment, remain underexplored. We investigated how 15 % L. platensis raw (MA), extruded (MAE) or extruded with pancreatin (0.20 %) and lysozyme (0.01 %) (MAEM) affects the pectoralis major proteome of Ross 308 broilers. Birds were fed until day 35, then muscle proteins were prepared by filter-aided sample preparation, TMT 6-plex labelling and analysed by LC-MS/MS. Statistical analysis identified 26 differentially abundant proteins (p < 0.05, ≥ 2 peptides). MAEM samples clustered separately, showing increased abundance of NDUFA10 (Complex I; + 1.30-fold), COX5B (Complex IV; + 1.25-fold) and glycogen phosphorylase (+ 1.40-fold). Enrichment analysis revealed up-regulation of ATP synthesis, oxidative phosphorylation and glycogen catabolism in L. platensis groups, whereas control diets featured proteins linked to fatty-acid β-oxidation and myofibrillar assembly. These results indicate that extrusion combined with enzyme treatment enhances nutrient bioavailability and shifts the broiler muscle proteome toward energy-metabolism pathways without compromising performance. Data are available via ProteomeXchange (PXD064230).
Significance
The incorporation of Spirulina (Limnospira platensis) as a sustainable alternative to conventional feed ingredients is gaining attention in poultry nutrition. However, its specific effects on broiler's muscle proteome, as well as the impact of higher Spirulina inclusion levels on animal performance, remain largely unexplored. Herein, we investigated how extruded L. platensis, with and without enzyme supplementation, influences muscle protein expression. Results revealed a metabolic shift toward enhanced mitochondrial ATP production and glycogen metabolism when L. platensis was incorporated into the diets, suggesting improved energy efficiency and nutrient utilisation. These findings provide valuable insight into the biological mechanisms underlying muscle development in broilers fed microalgae-based diets. More broadly, they highlight the potential of combining pre-treated microalga ingredients as a strategy to optimise animal performance and health in the framework of poultry production.
{"title":"Extruded Limnospira platensis with enzyme supplementation shifts the broiler muscle proteome toward enhanced energy metabolism pathways","authors":"Maria Pinheiro Spínola , Dina Rešetar Maslov , Ivana Rubić , Mónica Mendes da Costa , Vladimir Mrljak , Madalena Lordelo , André Martinho de Almeida , José António Mestre Prates","doi":"10.1016/j.jprot.2025.105541","DOIUrl":"10.1016/j.jprot.2025.105541","url":null,"abstract":"<div><div><em>Limnospira platensis</em> (Spirulina) is known for its nutritional and bioactive profile, but its high-level dietary inclusion effects in broilers, particularly post-extrusion and enzyme pre-treatment, remain underexplored. We investigated how 15 % <em>L. platensis</em> raw (MA), extruded (MAE) or extruded with pancreatin (0.20 %) and lysozyme (0.01 %) (MAEM) affects the <em>pectoralis major</em> proteome of Ross 308 broilers. Birds were fed until day 35, then muscle proteins were prepared by filter-aided sample preparation, TMT 6-plex labelling and analysed by LC-MS/MS. Statistical analysis identified 26 differentially abundant proteins (<em>p</em> < 0.05, ≥ 2 peptides). MAEM samples clustered separately, showing increased abundance of NDUFA10 (Complex I; + 1.30-fold), COX5B (Complex IV; + 1.25-fold) and glycogen phosphorylase (+ 1.40-fold). Enrichment analysis revealed up-regulation of ATP synthesis, oxidative phosphorylation and glycogen catabolism in L. <em>platensis</em> groups, whereas control diets featured proteins linked to fatty-acid β-oxidation and myofibrillar assembly. These results indicate that extrusion combined with enzyme treatment enhances nutrient bioavailability and shifts the broiler muscle proteome toward energy-metabolism pathways without compromising performance. Data are available via ProteomeXchange (<span><span>PXD064230</span><svg><path></path></svg></span>).</div></div><div><h3>Significance</h3><div>The incorporation of Spirulina (<em>Limnospira platensis</em>) as a sustainable alternative to conventional feed ingredients is gaining attention in poultry nutrition. However, its specific effects on broiler's muscle proteome, as well as the impact of higher Spirulina inclusion levels on animal performance, remain largely unexplored. Herein, we investigated how extruded L. <em>platensis</em>, with and without enzyme supplementation, influences muscle protein expression. Results revealed a metabolic shift toward enhanced mitochondrial ATP production and glycogen metabolism when L. <em>platensis</em> was incorporated into the diets, suggesting improved energy efficiency and nutrient utilisation. These findings provide valuable insight into the biological mechanisms underlying muscle development in broilers fed microalgae-based diets. More broadly, they highlight the potential of combining pre-treated microalga ingredients as a strategy to optimise animal performance and health in the framework of poultry production.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105541"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145206672","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-06Epub Date: 2025-10-27DOI: 10.1016/j.jprot.2025.105547
Zhigang Xiong , Chaoxi Li , Qiangqiang Han , Yanting Su , Liming Cheng , Hao-Long Zeng
<div><div>Glioblastoma multiforme (GBM) and low-grade astrocytoma (LGA) are diffuse gliomas with distinct biological features and prognoses. However, the molecular mechanisms driving their differences are not fully understood. In this study, we performed a multi-dataset analysis integrating in-house quantitative proteomics data with high-quality external datasets to identify GBM-specific proteomic alterations between tumoral and peritumoral tissues relative to LGA. Our analysis revealed more pronounced proteomic differences between intra- and peritumoral tissues in GBM than in LGA. Proteins specifically dysregulated in GBM were predominantly linked to upregulated RNA splicing and spliceosome signaling. Through multi-dataset integration, we identified 73 GBM-specific upregulated proteins enriched in processes such as transcriptional regulation, hypoxia and necrosis, cytoskeleton organization, extracellular matrix remodeling, and immune response. Conversely, the 129 GBM-specific downregulated proteins were mainly involved in tumor suppression, G-protein signaling, calcium signaling, and neuronal gap junctions. Using these signature proteins, we developed a risk model based on CDK2, HDAC1, IGFBP2, SLC6A1, and TNR, which significantly predicted overall survival in glioma patients. This study delineates the proteomic landscape of GBM in comparison to LGA and offers a valuable resource for future mechanistic and clinical investigations.</div></div><div><h3>Significance</h3><div>Diffuse gliomas are a heterogeneous brain tumor that include both low-grade and high-grade variants, each characterized by distinct morphological and biological features. Glioblastoma multiforme (GBM) is the most common primary high-grade and malignant brain tumor, with a median survival of less than 15 months despite aggressive treatment, including surgery, radiotherapy, and chemotherapy. In contrast, low-grade astrocytoma (LGA) exhibits indolent growth and a less aggressive clinical course, resulting in significantly longer patient survival compared to GBM. The molecular mechanisms underlying the biological differences between LGA and GBM are incompletely understood, and there is an urgent need for new molecular biomarkers to enhance diagnosis and therapeutic options. In this study, we conducted a comprehensive multi-dataset analysis by integrating our in-house quantitative proteomics data with several high-quality external datasets. We analyzed tumor and peritumoral tissue samples from human GBM and LGA, and further identified the GBM-specifically regulated proteomic signatures and signaling pathways, which is crucial for understanding the molecular mechanisms driving the aggressive behavior of GBM and could serve as a foundation for developing novel diagnostic biomarkers and therapeutic targets. Future research should focus on validating these GBM-specific proteins in larger cohorts and exploring their functional roles in GBM progression. Additionally, integrating multi-omic
{"title":"Comparative quantitative proteomics of tumoral and peritumoral tissues for distinguishing human glioblastoma from low-grade astrocytoma","authors":"Zhigang Xiong , Chaoxi Li , Qiangqiang Han , Yanting Su , Liming Cheng , Hao-Long Zeng","doi":"10.1016/j.jprot.2025.105547","DOIUrl":"10.1016/j.jprot.2025.105547","url":null,"abstract":"<div><div>Glioblastoma multiforme (GBM) and low-grade astrocytoma (LGA) are diffuse gliomas with distinct biological features and prognoses. However, the molecular mechanisms driving their differences are not fully understood. In this study, we performed a multi-dataset analysis integrating in-house quantitative proteomics data with high-quality external datasets to identify GBM-specific proteomic alterations between tumoral and peritumoral tissues relative to LGA. Our analysis revealed more pronounced proteomic differences between intra- and peritumoral tissues in GBM than in LGA. Proteins specifically dysregulated in GBM were predominantly linked to upregulated RNA splicing and spliceosome signaling. Through multi-dataset integration, we identified 73 GBM-specific upregulated proteins enriched in processes such as transcriptional regulation, hypoxia and necrosis, cytoskeleton organization, extracellular matrix remodeling, and immune response. Conversely, the 129 GBM-specific downregulated proteins were mainly involved in tumor suppression, G-protein signaling, calcium signaling, and neuronal gap junctions. Using these signature proteins, we developed a risk model based on CDK2, HDAC1, IGFBP2, SLC6A1, and TNR, which significantly predicted overall survival in glioma patients. This study delineates the proteomic landscape of GBM in comparison to LGA and offers a valuable resource for future mechanistic and clinical investigations.</div></div><div><h3>Significance</h3><div>Diffuse gliomas are a heterogeneous brain tumor that include both low-grade and high-grade variants, each characterized by distinct morphological and biological features. Glioblastoma multiforme (GBM) is the most common primary high-grade and malignant brain tumor, with a median survival of less than 15 months despite aggressive treatment, including surgery, radiotherapy, and chemotherapy. In contrast, low-grade astrocytoma (LGA) exhibits indolent growth and a less aggressive clinical course, resulting in significantly longer patient survival compared to GBM. The molecular mechanisms underlying the biological differences between LGA and GBM are incompletely understood, and there is an urgent need for new molecular biomarkers to enhance diagnosis and therapeutic options. In this study, we conducted a comprehensive multi-dataset analysis by integrating our in-house quantitative proteomics data with several high-quality external datasets. We analyzed tumor and peritumoral tissue samples from human GBM and LGA, and further identified the GBM-specifically regulated proteomic signatures and signaling pathways, which is crucial for understanding the molecular mechanisms driving the aggressive behavior of GBM and could serve as a foundation for developing novel diagnostic biomarkers and therapeutic targets. Future research should focus on validating these GBM-specific proteins in larger cohorts and exploring their functional roles in GBM progression. Additionally, integrating multi-omic","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105547"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145401380","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-06Epub Date: 2025-09-16DOI: 10.1016/j.jprot.2025.105536
Michael Santos Silva , Leila S. Coelho-Rato , Navid Delshad , Tatiana Tarkhova , Joakim Edman , Preethy Paul , Annika Meinander , John E. Eriksson
Human papillomavirus (HPV) is a major driver of cervical and other epithelial cancers, with the viral oncoprotein E6 playing a central role in tumorigenesis by promoting degradation of the tumor suppressor p53. While prophylactic vaccines prevent infection, there remains a critical need for therapeutic strategies that eliminate established HPV-positive cells. Here, we identify anisomelic acid (AA), a natural diterpenoid, as a novel pharmacological principle that selectively induces the degradation of HPV16 E6. Using cellular thermal shift assay, we demonstrate that AA directly interacts with E6, likely triggering a conformational change that promotes its ubiquitination. Proteomic analysis of the E6 interactome in AA-treated cells revealed consistent enrichment of E3 ubiquitin ligases, including E6AP, UBR4, CDC20, and TRIP12, as well as proteasomal subunits. To our knowledge, this represents the first comprehensive proteomics framework of the HPV16 E6 interactome under small-molecule treatment conditions. These findings support a model in which AA facilitates proteasome-mediated elimination of E6, and the dataset itself provides a timely and valuable resource for HPV biology and therapeutic development.
{"title":"Anisomelic acid promotes proteasomal degradation of HPV16 E6 via E3 ligase recruitment: A mass spectrometry-based interactome study","authors":"Michael Santos Silva , Leila S. Coelho-Rato , Navid Delshad , Tatiana Tarkhova , Joakim Edman , Preethy Paul , Annika Meinander , John E. Eriksson","doi":"10.1016/j.jprot.2025.105536","DOIUrl":"10.1016/j.jprot.2025.105536","url":null,"abstract":"<div><div>Human papillomavirus (HPV) is a major driver of cervical and other epithelial cancers, with the viral oncoprotein E6 playing a central role in tumorigenesis by promoting degradation of the tumor suppressor p53. While prophylactic vaccines prevent infection, there remains a critical need for therapeutic strategies that eliminate established HPV-positive cells. Here, we identify anisomelic acid (AA), a natural diterpenoid, as a novel pharmacological principle that selectively induces the degradation of HPV16 E6. Using cellular thermal shift assay, we demonstrate that AA directly interacts with E6, likely triggering a conformational change that promotes its ubiquitination. Proteomic analysis of the E6 interactome in AA-treated cells revealed consistent enrichment of E3 ubiquitin ligases, including E6AP, UBR4, CDC20, and TRIP12, as well as proteasomal subunits. To our knowledge, this represents the first comprehensive proteomics framework of the HPV16 E6 interactome under small-molecule treatment conditions. These findings support a model in which AA facilitates proteasome-mediated elimination of E6, and the dataset itself provides a timely and valuable resource for HPV biology and therapeutic development.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105536"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145086449","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-06Epub Date: 2025-10-08DOI: 10.1016/j.jprot.2025.105539
Julio A. González-Noriega , Martín Valenzuela-Melendres , Adrián Hernández-Mendoza , Humberto Astiazarán-García , Thalia Islava-Lagarda , Orlando Tortoledo-Ortiz , Ana L. De La Garza-Hernández , Samaria L. Gutierrez-Pacheco , Andrés Alvarez-Armenta , Emmanuel Ríos-Castro , José A. Huerta-Ocampo , E. Aída Peña-Ramos
The present study evaluated the angiotensin-converting enzyme inhibitory activity (ACEi) of a porcine skin collagen hydrolysate (PSCH) and its peptide fractions before and after a simulation of gastrointestinal digestion and their ability to reduce lipid accumulation in adipocytes (LAA). Before digestion, peptide fractions <1 kDa (PF4) had the highest (p < 0.05) ACEia (85.45 %), followed by PSCH (53.54 %). Post-digestion, PF4 (IC50: 124.49 μg/mL) decreased its activity; thus, DPF4 (digested PF4) had an ACE IC50 of 204.56 μg/mL, while fraction <1 kDa from digested hydrolysate (FDH) showed the lowest activity (IC50: 313.81 μg/mL). Peptides were identified by LC-MS/MS and homology database search and aligned to peptides widely recognized as ACE inhibitors. Nine peptides were identified as potential ACE inhibitors through docking with the active site cavity of this enzyme (mainly GAXGPXGPQ and GPPGPA), and interaction with Zn (II). Subsequently, adding 600 μg/mL of FDH in preadipocytes reduced 71 % LAA, while DPF4 was less effective (45.5 % reduction). The addition of digested peptide fractions into differentiated adipocytes had a similar (p > 0.05) reduction of LAA of 22–39 %. Therefore, regardless of their differences as ACE inhibitors, digested FDH and DPF4 have a similar potential as anti-obesogenic adjuvants.
Significance
In this study, we evaluated the angiotensin-converting enzyme inhibitory activity of a porcine skin collagen hydrolysate and its peptide fractions before and after a simulation of gastrointestinal digestion and their ability to reduce lipid accumulation in adipocytes. Peptides were identified by LC-MS/MS and homology database search and aligned to peptides widely recognized as ACE inhibitors. Nine peptides were identified as potential ACE inhibitors through docking with the active site cavity of this enzyme (mainly GAXGPXGPQ and GPPGPA), and interaction with Zn (II). Subsequently, adding digested peptide fractions into differentiated adipocytes resulted in a reduction of lipid accumulation in adipocytes.
{"title":"Antiobesogenic effect of hydrolysates and peptide fractions of porcine collagen after in vitro gastrointestinal digestion","authors":"Julio A. González-Noriega , Martín Valenzuela-Melendres , Adrián Hernández-Mendoza , Humberto Astiazarán-García , Thalia Islava-Lagarda , Orlando Tortoledo-Ortiz , Ana L. De La Garza-Hernández , Samaria L. Gutierrez-Pacheco , Andrés Alvarez-Armenta , Emmanuel Ríos-Castro , José A. Huerta-Ocampo , E. Aída Peña-Ramos","doi":"10.1016/j.jprot.2025.105539","DOIUrl":"10.1016/j.jprot.2025.105539","url":null,"abstract":"<div><div>The present study evaluated the angiotensin-converting enzyme inhibitory activity (ACEi) of a porcine skin collagen hydrolysate (PSCH) and its peptide fractions before and after a simulation of gastrointestinal digestion and their ability to reduce lipid accumulation in adipocytes (LAA). Before digestion, peptide fractions <1 kDa (PF4) had the highest (<em>p</em> < 0.05) ACEia (85.45 %), followed by PSCH (53.54 %). Post-digestion, PF4 (IC<sub>50</sub>: 124.49 μg/mL) decreased its activity; thus, DPF4 (digested PF4) had an ACE IC<sub>50</sub> of 204.56 μg/mL, while fraction <1 kDa from digested hydrolysate (FDH) showed the lowest activity (IC<sub>50</sub>: 313.81 μg/mL). Peptides were identified by LC-MS/MS and homology database search and aligned to peptides widely recognized as ACE inhibitors. Nine peptides were identified as potential ACE inhibitors through docking with the active site cavity of this enzyme (mainly GAXGPXGPQ and GPPGPA), and interaction with Zn (II). Subsequently, adding 600 μg/mL of FDH in preadipocytes reduced 71 % LAA, while DPF4 was less effective (45.5 % reduction). The addition of digested peptide fractions into differentiated adipocytes had a similar (<em>p</em> > 0.05) reduction of LAA of 22–39 %. Therefore, regardless of their differences as ACE inhibitors, digested FDH and DPF4 have a similar potential as anti-obesogenic adjuvants.</div></div><div><h3>Significance</h3><div>In this study, we evaluated the angiotensin-converting enzyme inhibitory activity of a porcine skin collagen hydrolysate and its peptide fractions before and after a simulation of gastrointestinal digestion and their ability to reduce lipid accumulation in adipocytes. Peptides were identified by LC-MS/MS and homology database search and aligned to peptides widely recognized as ACE inhibitors. Nine peptides were identified as potential ACE inhibitors through docking with the active site cavity of this enzyme (mainly GAXGPXGPQ and GPPGPA), and interaction with Zn (II). Subsequently, adding digested peptide fractions into differentiated adipocytes resulted in a reduction of lipid accumulation in adipocytes.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105539"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145258205","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Visceral obesity is closely related to insulin resistance (IR), a key process in developing metabolic diseases. Adipocyte-derived extracellular vesicles (AdEVs) have emerged as mediators of intercellular communication, carrying signals reflecting adipose tissue's functional state. This study aimed to perform a comparative proteomic analysis of AdEVs to propose a molecular fingerprint of specific biomarker candidates for IR in early-onset obesity. AdEVs were isolated from epididymal adipocytes of 16-week-old male Wistar rats on a high-fat diet (HFD) and controls and analyzed by mass spectrometry coupled to a multi-software protein identification bioinformatics strategy. For relative quantification using the label-free method, more than 1200 proteins were identified, with 431 being overrepresented and unique to HFD, associated explicitly with energy metabolism, cellular stress, and insulin signaling. Based on biological plausibility, and/or the best log2FC and p-value scores, six proteins were proposed as part of the IR molecular fingerprint: Atp5f1b, Anxa6, Myo1c, GLUT4, Anxa5, and Aoc3. Phosphoproteomic analysis revealed key modifications in phosphorylated proteins such as CaATPase (S663), PLIN (S130), and PPM1H (S260,265). The results suggest that AdEVs reflect early mitochondrial alterations related to IR, which could be employed as potential non-invasive biomarker candidates for metabolic dysfunction and follow-up in early overweight or obesity.
Significance
In this study, we demonstrate that adipocyte-derived extracellular vesicles (AdEVs) encapsulate a stage-resolved molecular signature that reflects key pathophysiological events underlying the early development of insulin resistance in obesity. These vesicles carry proteins linked to lipotoxicity, mitochondrial and endoplasmic reticulum stress, and impaired vesicular trafficking, offering mechanistic insight into how local adipocyte dysfunction may trigger systemic metabolic impairment. This EV-based proteomic fingerprint advances our understanding of insulin resistance pathogenesis and identifies potential biomarker candidates for early metabolic risk stratification.
{"title":"Molecular signature of early obesity-associated insulin resistance: Adipocyte-derived extracellular vesicle proteins reveal stage-specific candidates for metabolic dysfunction","authors":"Jaime Delgadillo-Velázquez , Esaú Bojórquez-Velázquez , Eliel Ruiz-May , Elizabeth Carvajal-Millan , Magdalena Aguirre-García , Efraín Alday-Noriega , José Ángel Huerta-Ocampo , Humberto Astiazaran-Garcia","doi":"10.1016/j.jprot.2025.105540","DOIUrl":"10.1016/j.jprot.2025.105540","url":null,"abstract":"<div><div>Visceral obesity is closely related to insulin resistance (IR), a key process in developing metabolic diseases. Adipocyte-derived extracellular vesicles (AdEVs) have emerged as mediators of intercellular communication, carrying signals reflecting adipose tissue's functional state. This study aimed to perform a comparative proteomic analysis of AdEVs to propose a molecular fingerprint of specific biomarker candidates for IR in early-onset obesity. AdEVs were isolated from epididymal adipocytes of 16-week-old male Wistar rats on a high-fat diet (HFD) and controls and analyzed by mass spectrometry coupled to a multi-software protein identification bioinformatics strategy. For relative quantification using the label-free method, more than 1200 proteins were identified, with 431 being overrepresented and unique to HFD, associated explicitly with energy metabolism, cellular stress, and insulin signaling. Based on biological plausibility, and/or the best log2FC and <em>p</em>-value scores, six proteins were proposed as part of the IR molecular fingerprint: Atp5f1b, Anxa6, Myo1c, GLUT4, Anxa5, and Aoc3. Phosphoproteomic analysis revealed key modifications in phosphorylated proteins such as CaATPase (S663), PLIN (S130), and PPM1H (S260,265). The results suggest that AdEVs reflect early mitochondrial alterations related to IR, which could be employed as potential non-invasive biomarker candidates for metabolic dysfunction and follow-up in early overweight or obesity.</div><div>Significance</div><div>In this study, we demonstrate that adipocyte-derived extracellular vesicles (AdEVs) encapsulate a stage-resolved molecular signature that reflects key pathophysiological events underlying the early development of insulin resistance in obesity. These vesicles carry proteins linked to lipotoxicity, mitochondrial and endoplasmic reticulum stress, and impaired vesicular trafficking, offering mechanistic insight into how local adipocyte dysfunction may trigger systemic metabolic impairment. This EV-based proteomic fingerprint advances our understanding of insulin resistance pathogenesis and identifies potential biomarker candidates for early metabolic risk stratification.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105540"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145206649","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-06Epub Date: 2025-10-18DOI: 10.1016/j.jprot.2025.105548
Phetolo Motsa , Beric Muller , Lesetja R. Motadi , Benedict C. Offor , Lizelle A. Piater
The forest cobra (Naja melanoleuca) species represents one of the most widespread medically important elapid snakes across Africa. The immense tissue-damaging effect of cobra venoms is attributed to the cytotoxins (CTX), which predominate in virtually all cobra venoms. In this study a bottom-up venomic approach was followed for deciphering the composition of the N. melanoleuca, N. subfulva, and N. savannula venom proteomes. The results revealed complex venoms that constituted predominantly of proteins belonging to the three-finger toxins (3FTxs) followed by phospholipase A2 (PLA2s) and snake venom metalloproteinases (SVMPs). The cytotoxicity and selectivity of the crude venoms and fractions were evaluated against cancer and normal cell lines. The crude N. melanoleuca venom sample demonstrated weak/low cytotoxic activity across the different cell lines as corroborated by SI values of less than 2, thus highlighting its limited application against these cancer cells, while the N. subfulva venom demonstrated its highest cytotoxic activity against the HeLa cancer cell line with a moderate selectivity index of 2.04. It is crucial to emphasize that these findings are still in the preliminary stages, primarily based on in vitro studies, and there remains a significant gap to bridge before any therapeutic applications can be considered.
Significance
Biological significance: African forest cobra venom is a rich source of bioactive compounds such as cytotoxins, which cause tissue necrosis and descending paralysis. However, the venom has also been identified as a potential source of therapeutic agents, including anticancer agents. In this study, we evaluate the anticancer effects of the N. melanoleuca, N. subfulva, and N. savannula venoms and their fractions against the selected cell lines. The 3FTxs and PLA2s, which are the most abundant protein families in the venoms, are predominantly responsible for the cytotoxic effects. In conclusion, this research study highlights the important role of forest cobra venoms as potential resources that researchers can further exploit to investigate the molecules responsible for the anticancer effect and investigate their mechanisms of action.
森林眼镜蛇（Naja melanoleuca）物种代表了非洲最广泛的医学上重要的蛇之一。眼镜蛇毒液的巨大的组织破坏作用归因于细胞毒素（CTX），它在几乎所有的眼镜蛇毒液中占主导地位。在这项研究中，自下而上的毒液方法被用于破译N. melanoleuca， N. subfulva和N. savannula毒液蛋白质组的组成。结果显示，复杂的毒液主要由三指毒素（3FTxs）蛋白质组成，其次是磷脂酶A2 （PLA2s）和蛇毒金属蛋白酶（SVMPs）。研究了粗毒液和粗馏分对肿瘤和正常细胞株的细胞毒性和选择性。粗制黑素N.毒液样品在不同细胞系中表现出弱/低的细胞毒活性，SI值小于2，因此表明其对这些癌细胞的应用有限，而亚富尔N.毒液对HeLa癌细胞的细胞毒活性最高，选择性指数为2.04。必须强调的是，这些发现仍处于初步阶段，主要基于体外研究，在考虑任何治疗应用之前，仍有很大的差距需要弥合。生物学意义：非洲森林眼镜蛇毒液是一种丰富的生物活性化合物，如细胞毒素，可引起组织坏死和下降性麻痹。然而，毒液也被确定为治疗剂的潜在来源，包括抗癌剂。在这项研究中，我们评估了黑素N.， N. subfulva和N. savannula毒液及其组分对选定细胞系的抗癌作用。3FTxs和PLA2s是毒液中最丰富的蛋白质家族，它们主要负责细胞毒性作用。总之，本研究强调了森林眼镜蛇毒液作为潜在资源的重要作用，研究人员可以进一步研究负责抗癌作用的分子及其作用机制。
{"title":"Proteomic exploration of the recently Re-classified forest cobra Naja species and the potential cytotoxic activity in cancer cell lines","authors":"Phetolo Motsa , Beric Muller , Lesetja R. Motadi , Benedict C. Offor , Lizelle A. Piater","doi":"10.1016/j.jprot.2025.105548","DOIUrl":"10.1016/j.jprot.2025.105548","url":null,"abstract":"<div><div>The forest cobra (<em>Naja melanoleuca</em>) species represents one of the most widespread medically important elapid snakes across Africa. The immense tissue-damaging effect of cobra venoms is attributed to the cytotoxins (CTX), which predominate in virtually all cobra venoms. In this study a bottom-up venomic approach was followed for deciphering the composition of the <em>N. melanoleuca</em>, <em>N. subfulva</em>, and <em>N. savannula</em> venom proteomes. The results revealed complex venoms that constituted predominantly of proteins belonging to the three-finger toxins (3FTxs) followed by phospholipase A<sub>2</sub> (PLA<sub>2</sub>s) and snake venom metalloproteinases (SVMPs). The cytotoxicity and selectivity of the crude venoms and fractions were evaluated against cancer and normal cell lines. The crude <em>N. melanoleuca</em> venom sample demonstrated weak/low cytotoxic activity across the different cell lines as corroborated by SI values of less than 2, thus highlighting its limited application against these cancer cells, while the <em>N. subfulva</em> venom demonstrated its highest cytotoxic activity against the HeLa cancer cell line with a moderate selectivity index of 2.04. It is crucial to emphasize that these findings are still in the preliminary stages, primarily based on in vitro studies, and there remains a significant gap to bridge before any therapeutic applications can be considered.</div></div><div><h3>Significance</h3><div><em>Biological significance:</em> African forest cobra venom is a rich source of bioactive compounds such as cytotoxins, which cause tissue necrosis and descending paralysis. However, the venom has also been identified as a potential source of therapeutic agents, including anticancer agents. In this study, we evaluate the anticancer effects of the <em>N. melanoleuca</em>, <em>N. subfulva</em>, and <em>N. savannula</em> venoms and their fractions against the selected cell lines. The 3FTxs and PLA<sub>2</sub>s, which are the most abundant protein families in the venoms, are predominantly responsible for the cytotoxic effects. In conclusion, this research study highlights the important role of forest cobra venoms as potential resources that researchers can further exploit to investigate the molecules responsible for the anticancer effect and investigate their mechanisms of action.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105548"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145337249","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-06Epub Date: 2025-09-11DOI: 10.1016/j.jprot.2025.105526
Agyeya Pratap , Kadambot H.M. Siddique , Nicolas L. Taylor
Heat stress is a major threat to global wheat (Triticum aestivum L.) production, adversely affecting crop yields and grain quality. Understanding wheat's heat tolerance mechanisms is crucial for developing resilient cultivars. This study used targeted proteomics to validate heat-induced changes to protein abundances in seedling and flag leaves of heat-tolerant (Vixen-T) and heat-sensitive (HD2329-S) wheat genotypes. Proteomics samples were collected on days 1, 3 and 5 of heat exposure (32/16 °C day/night for 3 hours per day over 5 days) and day 12 post-recovery. Flag leaf gas exchange was studied under heat treatment during ear peep and significant genotype × heat treatment interactions were observed for all traits. Significant protein abundance changes occurred under heat stress for 15 and 14 proteins at the seedling and ear peep stages, respectively. Two key proteins—DM2 domain-containing protein (r = 0.99) and Rubisco activase (r = 0.96)—showed consistent responses across both developmental stages. Redox homeostasis and protein chaperone pathways emerged as major contributors to wheat heat tolerance. These findings highlight critical protein biomarkers that can support breeding efforts to develop heat-tolerant wheat varieties, offering valuable strategies for sustaining wheat productivity under climate change.
Significance
This study identifies and validates novel protein biomarkers associated with heat tolerance in wheat. These proteins were discovered in our previous study in the flag leaves of four genotypes with contrasting heat responses (tolerant: RAJ3765, HD2932; susceptible: HD2329, HD2733) under short-term heat stress at the ear peep stage. These biomarkers were further validated in two genotypes (tolerant: Vixen; susceptible: HD2329) under short-term heat stress at both seedling and ear peep stages. The validated protein isoforms span key biological processes, including photosynthesis, redox regulation, chromatin remodelling, protein folding, and carbohydrate and secondary metabolism. This panel of protein biomarkers offers a novel molecular framework for breeding heat-tolerant wheat, providing a strategic avenue, utilising targeted proteomics, to sustain yield under rising temperatures.
{"title":"Potential protein biomarkers for heat tolerance in wheat at seedling and ear peep stages","authors":"Agyeya Pratap , Kadambot H.M. Siddique , Nicolas L. Taylor","doi":"10.1016/j.jprot.2025.105526","DOIUrl":"10.1016/j.jprot.2025.105526","url":null,"abstract":"<div><div>Heat stress is a major threat to global wheat (<em>Triticum aestivum</em> L.) production, adversely affecting crop yields and grain quality. Understanding wheat's heat tolerance mechanisms is crucial for developing resilient cultivars. This study used targeted proteomics to validate heat-induced changes to protein abundances in seedling and flag leaves of heat-tolerant (Vixen-T) and heat-sensitive (HD2329-S) wheat genotypes. Proteomics samples were collected on days 1, 3 and 5 of heat exposure (32/16 °C day/night for 3 hours per day over 5 days) and day 12 post-recovery. Flag leaf gas exchange was studied under heat treatment during ear peep and significant genotype × heat treatment interactions were observed for all traits. Significant protein abundance changes occurred under heat stress for 15 and 14 proteins at the seedling and ear peep stages, respectively. Two key proteins—DM2 domain-containing protein (<em>r =</em> 0.99) and Rubisco activase (<em>r =</em> 0.96)—showed consistent responses across both developmental stages. Redox homeostasis and protein chaperone pathways emerged as major contributors to wheat heat tolerance. These findings highlight critical protein biomarkers that can support breeding efforts to develop heat-tolerant wheat varieties, offering valuable strategies for sustaining wheat productivity under climate change.</div></div><div><h3>Significance</h3><div>This study identifies and validates novel protein biomarkers associated with heat tolerance in wheat. These proteins were discovered in our previous study in the flag leaves of four genotypes with contrasting heat responses (tolerant: RAJ3765, HD2932; susceptible: HD2329, HD2733) under short-term heat stress at the ear peep stage. These biomarkers were further validated in two genotypes (tolerant: Vixen; susceptible: HD2329) under short-term heat stress at both seedling and ear peep stages. The validated protein isoforms span key biological processes, including photosynthesis, redox regulation, chromatin remodelling, protein folding, and carbohydrate and secondary metabolism. This panel of protein biomarkers offers a novel molecular framework for breeding heat-tolerant wheat, providing a strategic avenue, utilising targeted proteomics, to sustain yield under rising temperatures.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105526"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145058669","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-06Epub Date: 2025-10-08DOI: 10.1016/j.jprot.2025.105542
Celso Vitor A.Q. Calomeno , Hulyana Brum , Rodrigo S.C. Brant , Marlon D.M. Santos , Luis Miguel Muñoz-Gómez , Ana Gisele da Costa Neves-Ferreira , Richard Hemmi Valente , Michel Batista , Paulo C. Carvalho
Accurate sequencing of complete proteoforms—that is, all molecular variants generated by post-translational modification or sequence change—is essential for advancing our understanding of biological systems, guiding biopharmaceutical development, and enabling new biotechnological applications. We present SequenceAssembler (SA), a user-friendly software post-identification tool designed to assemble full-length protein sequences by integrating both peptide-spectrum matching (PSM) and de novo sequencing data. SA is compatible with widely used proteomics tools, including Novor Cloud, PEAKS Studio, and PatternLab for Proteomics, from which it efficiently aggregates input data. Our software offers an accessible and intuitive interface, enhancing its usability. We demonstrated SA's effectiveness by analyzing bovine serum albumin and the monoclonal antibody trastuzumab, each subjected to multiple enzymatic digestions followed by high-resolution mass spectrometry. The results were consistent with those of established tools like Stitch, with performance varying depending on threshold parameters. Notably, SA distinguishes itself through its user-friendly graphical interface, one-click installation, and streamlined workflow, making it an attractive solution for a wide range of proteomics researchers. The software is freely available for academic use at http://patternlabforproteomics.org/sa.
Significance
SequenceAssembler fills a critical gap in proteomics by unifying peptide-spectrum matching and de novo sequencing into a single assembly platform, enabling reconstruction of full-length proteins. The intuitive graphical interface lowers barriers to adoption in core laboratories, minimizing manual steps and enhancing reproducibility. By streamlining sequence assembly workflows, SequenceAssembler empowers rapid protein sequencing to broad protein research applications.
完整蛋白质形态的精确测序——即所有由翻译后修饰或序列变化产生的分子变异——对于提高我们对生物系统的理解、指导生物制药开发和实现新的生物技术应用至关重要。我们提出了SequenceAssembler (SA)，一个用户友好的软件后鉴定工具，旨在通过整合肽谱匹配（PSM）和从头测序数据来组装全长蛋白质序列。SA与广泛使用的蛋白质组学工具兼容，包括Novor Cloud， PEAKS Studio和PatternLab for proteomics，它可以有效地聚合输入数据。我们的软件提供了一个易于访问和直观的界面，提高了它的可用性。我们通过分析牛血清白蛋白和单克隆抗体曲妥珠单抗证明了SA的有效性，每一个都经过多次酶解和高分辨率质谱分析。结果与Stitch等已建立的工具一致，其性能取决于阈值参数。值得注意的是，SA以其用户友好的图形界面、一键安装和简化的工作流程而脱颖而出，使其成为广泛的蛋白质组学研究人员的有吸引力的解决方案。该软件可免费用于学术用途，网址为http://patternlabforproteomics.org/sa。意义：SequenceAssembler通过将肽谱匹配和从头测序统一到一个组装平台，填补了蛋白质组学的关键空白，使全长蛋白质的重建成为可能。直观的图形界面降低了在核心实验室采用的障碍，最大限度地减少了手动步骤并提高了再现性。通过简化序列组装工作流程，SequenceAssembler使快速蛋白质测序具有广泛的蛋白质研究应用。
{"title":"SequenceAssembler: A tool for protein sequence assembly from mass spectrometry data","authors":"Celso Vitor A.Q. Calomeno , Hulyana Brum , Rodrigo S.C. Brant , Marlon D.M. Santos , Luis Miguel Muñoz-Gómez , Ana Gisele da Costa Neves-Ferreira , Richard Hemmi Valente , Michel Batista , Paulo C. Carvalho","doi":"10.1016/j.jprot.2025.105542","DOIUrl":"10.1016/j.jprot.2025.105542","url":null,"abstract":"<div><div>Accurate sequencing of complete proteoforms—that is, all molecular variants generated by post-translational modification or sequence change—is essential for advancing our understanding of biological systems, guiding biopharmaceutical development, and enabling new biotechnological applications. We present SequenceAssembler (SA), a user-friendly software post-identification tool designed to assemble full-length protein sequences by integrating both peptide-spectrum matching (PSM) and <em>de novo</em> sequencing data. SA is compatible with widely used proteomics tools, including Novor Cloud, PEAKS Studio, and PatternLab for Proteomics, from which it efficiently aggregates input data. Our software offers an accessible and intuitive interface, enhancing its usability. We demonstrated SA's effectiveness by analyzing bovine serum albumin and the monoclonal antibody trastuzumab, each subjected to multiple enzymatic digestions followed by high-resolution mass spectrometry. The results were consistent with those of established tools like Stitch, with performance varying depending on threshold parameters. Notably, SA distinguishes itself through its user-friendly graphical interface, one-click installation, and streamlined workflow, making it an attractive solution for a wide range of proteomics researchers. The software is freely available for academic use at <span><span>http://patternlabforproteomics.org/sa</span><svg><path></path></svg></span>.</div></div><div><h3>Significance</h3><div>SequenceAssembler fills a critical gap in proteomics by unifying peptide-spectrum matching and <em>de novo</em> sequencing into a single assembly platform, enabling reconstruction of full-length proteins. The intuitive graphical interface lowers barriers to adoption in core laboratories, minimizing manual steps and enhancing reproducibility. By streamlining sequence assembly workflows, SequenceAssembler empowers rapid protein sequencing to broad protein research applications.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105542"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145274908","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-06Epub Date: 2025-10-23DOI: 10.1016/j.jprot.2025.105551
Robert Winkler , Aldo Moreno-Ulloa
The Mexican Proteomics Society (SMP) is the oldest proteomics organization in Latin America (LATAM), dedicated to advancing research in proteomics, metabolomics, and mass spectrometry (MS). As a non-profit, SMP organizes symposia and academic events, promoting collaboration and education. Since its founding in 2005, SMP has held biennial meetings and workshops in proteomics and metabolomics, invited international experts and fostered a multidisciplinary community. In this perspective manuscript, we provide a brief overview of the SMP, highlighting positive and negative aspects related to the economy, funding, infrastructure, technology and innovation, agriculture, health, and other fields. We also offer an overview of the MS equipment—critical infrastructure for omics research development—available within research centers and universities nationwide. Moreover, we present statistics on the contributions of Mexican-affiliated researchers to published research articles across various omics disciplines comparing Mexico's output to that of other LATAM countries. We believe that with this perspective the community will capture the role of the SMP in the development of omics research in Mexico, what is the country's contribution in the field, what are the country needs and how the new SMP board will contribute to advancing the field.
Significance
Omics-based societies play a crucial role in education, scientific development, and fostering multi-institutional collaborations. Although there are various societies worldwide focused on mass spectrometry-based omics, such as proteomics and metabolomics, their presence and impact on academia can be difficult to track. Therefore, in this manuscript, we provide a brief overview of the Mexican Proteomics Society (SMP), highlighting its contributions to omics research, the opportunities envisioned by the 2025-elected SMP leadership to advance omics science nationwide, and insights into the strategic directions for the coming decade.
{"title":"Advancing post-genomics research in Mexico: Opportunities and strategies for the next decade","authors":"Robert Winkler , Aldo Moreno-Ulloa","doi":"10.1016/j.jprot.2025.105551","DOIUrl":"10.1016/j.jprot.2025.105551","url":null,"abstract":"<div><div>The Mexican Proteomics Society (SMP) is the oldest proteomics organization in Latin America (LATAM), dedicated to advancing research in proteomics, metabolomics, and mass spectrometry (MS). As a non-profit, SMP organizes symposia and academic events, promoting collaboration and education. Since its founding in 2005, SMP has held biennial meetings and workshops in proteomics and metabolomics, invited international experts and fostered a multidisciplinary community. In this perspective manuscript, we provide a brief overview of the SMP, highlighting positive and negative aspects related to the economy, funding, infrastructure, technology and innovation, agriculture, health, and other fields. We also offer an overview of the MS equipment—critical infrastructure for omics research development—available within research centers and universities nationwide. Moreover, we present statistics on the contributions of Mexican-affiliated researchers to published research articles across various omics disciplines comparing Mexico's output to that of other LATAM countries. We believe that with this perspective the community will capture the role of the SMP in the development of omics research in Mexico, what is the country's contribution in the field, what are the country needs and how the new SMP board will contribute to advancing the field.</div></div><div><h3>Significance</h3><div>Omics-based societies play a crucial role in education, scientific development, and fostering multi-institutional collaborations. Although there are various societies worldwide focused on mass spectrometry-based omics, such as proteomics and metabolomics, their presence and impact on academia can be difficult to track. Therefore, in this manuscript, we provide a brief overview of the Mexican Proteomics Society (SMP), highlighting its contributions to omics research, the opportunities envisioned by the 2025-elected SMP leadership to advance omics science nationwide, and insights into the strategic directions for the coming decade.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105551"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145364006","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-06Epub Date: 2025-10-09DOI: 10.1016/j.jprot.2025.105545
José Ángel Huerta-Ocampo , Robert Winkler , Aldo Moreno-Ulloa , Sergio Encarnación-Guevara
The establishment of the Mexican Proteomics Society (Sociedad Mexicana de Proteómica, SMP) has provided a platform for researchers in proteomics and metabolomics to share ideas and collaborate on research. This initiative promotes scientific knowledge in México and facilitates the integration of national researchers into international projects. Founded twenty years ago, the SMP is the oldest proteomics society in Latin America. It is a non-profit organization that advocates for research in proteomics, metabolomics, and MS within the country.
This review seeks to trace the development of the field by highlighting the contributions of researchers, laboratories, institutions, and organizations such as the SMP that have played a role in establishing and advancing this science in México. However, we are an enthusiastic and diverse community that, through imagination, collaboration, and determination, will continue to advance proteomics, metabolomics, and related fields in México.
Significance
The Mexican Proteomics Society (Sociedad Mexicana de Proteómica, SMP) was established 20 years ago to foster proteomics in México. The organization of a biannual symposium has since evolved into a reliable academic event in proteomics, metabolomics, and mass spectrometry (MS), where international experts present their discoveries to our community, and vendors present their latest products. We encourage students and professionals to learn through hands-on workshops on protein electrophoresis, proteomics, metabolomics, and open-access computer tools for analyzing omics data. Additionally, SMP has hosted the Ibero-American Symposium on Mass Spectrometry, the Pan-American Human Proteome Organization (Pan-HUPO) meeting, and most recently, the Human Proteome Organization World Congress (HUPO-2022). This commentary does not offer a comprehensive overview of proteomics in México; instead, it follows its evolution by emphasizing the contributions of researchers, laboratories, and institutions that have played a significant role in establishing and expanding this field in México. It also endeavors to offer a comprehensive understanding of the current state of proteomics in México. The challenges, opportunities, and perspectives related to the SMP's role in advancing proteomics in the country will be discussed in a parallel commentary included in this special issue entitled “Advancing post-genomics research in México: Opportunities and strategies for the next decade”.
墨西哥蛋白质组学学会（Sociedad Mexicana de Proteómica， SMP）的成立为蛋白质组学和代谢组学的研究人员提供了一个交流思想和合作研究的平台。这一倡议促进了墨西哥的科学知识，并促进了国家研究人员融入国际项目。SMP成立于20年前，是拉丁美洲最古老的蛋白质组学学会。它是一个非营利性组织，倡导在国内进行蛋白质组学、代谢组学和质谱研究。这篇综述试图通过强调在墨西哥建立和推进这一科学方面发挥作用的研究人员、实验室、机构和组织（如SMP）的贡献来追溯这一领域的发展。然而，我们是一个充满热情和多元化的社区，通过想象、合作和决心，我们将继续在墨西哥推进蛋白质组学、代谢组学和相关领域的研究。意义：墨西哥蛋白质组学学会（Sociedad Mexicana de Proteómica， SMP）成立于20 年前，旨在促进墨西哥的蛋白质组学。一年两次的研讨会组织已经发展成为蛋白质组学，代谢组学和质谱（MS）的可靠学术活动，国际专家向我们的社区展示他们的发现，供应商展示他们的最新产品。我们鼓励学生和专业人士通过实践研讨会学习蛋白质电泳，蛋白质组学，代谢组学和开放获取的计算机工具来分析组学数据。此外，SMP还主办了伊比利亚-美洲质谱研讨会、泛美人类蛋白质组组织（Pan-HUPO）会议，以及最近的人类蛋白质组组织世界大会（HUPO-2022）。这篇评论没有提供墨西哥蛋白质组学的全面概述；相反，它通过强调在墨西哥建立和扩大这一领域中发挥重要作用的研究人员、实验室和机构的贡献来遵循其演变。它还努力提供对墨西哥蛋白质组学现状的全面了解。与SMP在推进墨西哥蛋白质组学方面的作用相关的挑战、机遇和前景将在本期特刊题为“推进墨西哥后基因组学研究：未来十年的机遇和战略”的平行评论中讨论。
{"title":"Two decades of the Mexican Proteomics Society: the history and evolution of proteomics and metabolomics in Mexico","authors":"José Ángel Huerta-Ocampo , Robert Winkler , Aldo Moreno-Ulloa , Sergio Encarnación-Guevara","doi":"10.1016/j.jprot.2025.105545","DOIUrl":"10.1016/j.jprot.2025.105545","url":null,"abstract":"<div><div>The establishment of the Mexican Proteomics Society (Sociedad Mexicana de Proteómica, SMP) has provided a platform for researchers in proteomics and metabolomics to share ideas and collaborate on research. This initiative promotes scientific knowledge in México and facilitates the integration of national researchers into international projects. Founded twenty years ago, the SMP is the oldest proteomics society in Latin America. It is a non-profit organization that advocates for research in proteomics, metabolomics, and MS within the country.</div><div>This review seeks to trace the development of the field by highlighting the contributions of researchers, laboratories, institutions, and organizations such as the SMP that have played a role in establishing and advancing this science in México. However, we are an enthusiastic and diverse community that, through imagination, collaboration, and determination, will continue to advance proteomics, metabolomics, and related fields in México.</div></div><div><h3>Significance</h3><div>The Mexican Proteomics Society (Sociedad Mexicana de Proteómica, SMP) was established 20 years ago to foster proteomics in México. The organization of a biannual symposium has since evolved into a reliable academic event in proteomics, metabolomics, and mass spectrometry (MS), where international experts present their discoveries to our community, and vendors present their latest products. We encourage students and professionals to learn through hands-on workshops on protein electrophoresis, proteomics, metabolomics, and open-access computer tools for analyzing omics data. Additionally, SMP has hosted the Ibero-American Symposium on Mass Spectrometry, the Pan-American Human Proteome Organization (Pan-HUPO) meeting, and most recently, the Human Proteome Organization World Congress (HUPO-2022). This commentary does not offer a comprehensive overview of proteomics in México; instead, it follows its evolution by emphasizing the contributions of researchers, laboratories, and institutions that have played a significant role in establishing and expanding this field in México. It also endeavors to offer a comprehensive understanding of the current state of proteomics in México. The challenges, opportunities, and perspectives related to the SMP's role in advancing proteomics in the country will be discussed in a parallel commentary included in this special issue entitled “Advancing post-genomics research in México: Opportunities and strategies for the next decade”.</div></div>","PeriodicalId":16891,"journal":{"name":"Journal of proteomics","volume":"322 ","pages":"Article 105545"},"PeriodicalIF":2.8,"publicationDate":"2026-01-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145258237","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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