Protein and Peptide Letters最新文献

{"title":"Evaluation of Anti-cancer Potential of Abelmoschus esculentus (Okra).","authors":"Maanniya Gakhar, Lovepreet Singh, Sanjeev Routh, Arunika Mukhopadhaya, Desh Deepak Singh","doi":"10.2174/0109298665365981250801110725","DOIUrl":"https://doi.org/10.2174/0109298665365981250801110725","url":null,"abstract":"<p><strong>Introduction: </strong>Abelmoschus esculentus (okra) from the Malvaceae family is widely used in culinary applications and is reported to have many potential therapeutic effects attributed to the compounds isolated from it. In this work, we set out to explore its seed proteome for the isolation of lectins and characterize them Method: A protein of about 21kDa was isolated and purified using chromatography techniques from the ammonium sulphate crude protein extract. It was evaluated for hemagglutination activity on rabbit erythrocyte suspension, trypsin inhibitory activity using chemical assay, and evaluation of anti-cancer activity using cell lines. Mass and transcriptome analysis were done to deduce the complete sequence of the isolated protein.</p><p><strong>Results: </strong>Using functional, mass, and transcriptome analysis, the protein was identified as AEL (Abelmoschus esculentus lectin), which was reported earlier. Only a partial sequence of AEL was known, and in this work, we have deduced its complete sequence. It showed significant anti-- cancer activity against HeLa (cervical cancer) and T84 (colon cancer) with MIC (Minimum inhibitory concentration) of 20μg/ml and 40% and 30% reduction in cell viability at 100μg/ml and insignificant effect on ACHN (adenocarcinoma) cell lines. No significant effect was seen with the tested doses on normal control human cell lines HEK293 (human embryonic kidney cells). The purified protein shows specificity for lactose and galactose in the hemagglutination assay and trypsin inhibition activity.</p><p><strong>Discussion: </strong>Studies of okra seed proteome lead to purification of AEL, a 21 kDa protein with dual hemagglutination activity and trypsin inhibitory activity. It showed potential anticancer activity in cervical, colon cancer cell lines and minimal effects on adenocarcinoma and control cell lines, suggesting specificity. The complete sequence of AEL was elucidated which will aid in its bioinformatics analysis, was isolated from okra seeds.</p><p><strong>Conclusion: </strong>There are very few reported dual-acting lectins with potential anticancer activity, and this work will help understand their mechanistic interactions better.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":""},"PeriodicalIF":1.1,"publicationDate":"2025-08-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144966262","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"F18 Promiscuous Epitope of Acr1 Protein of Mycobacterium tuberculosis Induces the Secretion of IL-10 and Tregs But Not IL-6.","authors":"Taruna Lamba, Shivank Prajapati, Arnab Chowdhury, Anupam Bandyopadhyay, Javed N Agrewala","doi":"10.2174/0109298665398349250728195645","DOIUrl":"https://doi.org/10.2174/0109298665398349250728195645","url":null,"abstract":"<p><strong>Introduction: </strong>Mycobacterium tuberculosis (Mtb) is a Gram-positive bacterium that causes tuberculosis (TB). It remains viable for extended periods within host macrophages by entering a dormant state. Alpha crystallin 1 (Acr1) is a 16 kDa protein of Mtb and is reported to be highly upregulated in latent TB. Acr1 suppresses the host's immune system by impairing the differentiation and maturation of dendritic cells and macrophages. We hypothesize that Mtb judiciously utilizes its Acr1 protein to paralyse the immune system of the host by inducing the release of IL-10 and generating an immunosuppressive environment.</p><p><strong>Methods: </strong>We employed in silico tools to identify highly promiscuous, IL-10-inducing and IL-6- non-inducing epitopes of Mtb. Moreover, the selected epitope was synthesized and tested for its suppressive activity and generation of Tregs.</p><p><strong>Results: </strong>We identified the presence of a specific epitope in Acr1 (F18) that is responsible for bolstering the release of IL-10 and Tregs through in silico tools and verified the activity by in vitro assays. In hPBMCs, the F18 epitope could suppress the proliferation of CD4 T cells stimulated with PHA and expand the pool of Tregs in a dose-dependent manner.</p><p><strong>Discussion: </strong>The F18 epitope from Mtb's Acr1 protein promotes IL-10 and Treg responses without triggering pro-inflammatory IL-6, suggesting a potential immunoregulatory role. While it holds potential for treating autoimmune diseases, its impact on infection tolerance in tuberculosis should be further investigated.</p><p><strong>Conclusion: </strong>Our findings suggest that the F18 epitope induces IL-10 production and Treg differentiation while inhibiting CD4+ T cell proliferation and IL-6 secretion, thereby promoting an immunosuppressive environment. Furthermore, this study highlights the potential of Acr1 and its immunosuppressive epitope F18 as therapeutic agents for inducing suppressive Tregs in the management of autoimmune diseases.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":""},"PeriodicalIF":1.1,"publicationDate":"2025-08-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144837483","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Recombinant Proteins: Evolution to their Therapeutic Potential.","authors":"Kalyani R Thombre, Krishna R Gupta, Tejaswini P Masne, Milind Janrao Umekar","doi":"10.2174/0109298665387985250710041016","DOIUrl":"https://doi.org/10.2174/0109298665387985250710041016","url":null,"abstract":"<p><p>Recombinant proteins, which are produced using recombinant DNA technology, have transformed the domains of biotechnology and biomedicine by allowing the production of proteins that are often expensive or difficult to obtain from natural sources. More than 130 recombinant proteins are currently in clinical use by the US FDA, demonstrating the importance of these proteins in both research and therapeutic applications. Bacterial, yeast, mammalian cell cultures, and hybridoma technology are examples of recombinant protein production systems that have enabled the large-scale production of therapeutic proteins, including monoclonal antibodies, which are now essential tools in disease treatment. From their origins with human insulin in the 1980s to the most recent developments in third-generation proteins, this brief review examines the development of recombinant protein therapies. The first generation concentrated on natural structures; the second generation focused on enhancing safety, pharmacokinetics, and specificity; and the third generation is ready to present innovative formulations and delivery systems. This review also covers the use of recombinant proteins in cancer treatment, different protein production systems, and design techniques that keep improving the safety and effectiveness profiles of protein therapies.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":""},"PeriodicalIF":1.1,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144785124","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Unlocking the Keratinolytic Potential of Brevibacillusagri Derived Keratinase: A Molecular Characterization Study.","authors":"Hira Batool, Beenish Maqsood, Hira Muzzamal, Hamama Islam Butt, Roquyya Gul, Farooq Latif, Mahjabeen Saleem","doi":"10.2174/0109298665378063250628211031","DOIUrl":"https://doi.org/10.2174/0109298665378063250628211031","url":null,"abstract":"<p><strong>Background: </strong>Keratinases have an established role in degrading highly stable and insoluble fibers of keratin proteins, which are otherwise difficult to be hydrolyzed by conventional proteases. Keratinases find promising application in degrading poultry waste to valuable products. Moreover, their role in cosmetics, detergents, agriculture and the leather industry is well recognized.</p><p><strong>Objectives: </strong>In this study, the keratinase gene from locally isolated Brevibacillus agri bacteria was cloned and expressed in Escherichia coli, and some of its potential applications were explored.</p><p><strong>Methods: </strong>1300 bp amplified gene from Brevibacillus agri was cloned into E. coli DH5α competent cells using pTZ57R/T vector. After blue-white screening, the positive clone was confirmed by colony PCR and restriction analysis. Purified keratinase gene KerH from recombinant pTZR/KerH plasmid was ligated into pET-28a (+) and transferred into competent cells of E. coli DH5α. Following conformation through colony PCR, and restriction analysis, recombinant plasmid (pET-28a/Ker) from the positive clone was transferred into competent E. coli BL21 cells. The transformed cells were then cultured for up to 8 hours after induction with 0.8 mM IPTG and lysed by sonication. The resulting recombinant keratinase (KerH) was purified by heat treatment and Ni-affinity column and characterized.</p><p><strong>Results: </strong>The blast analysis and homologous sequences in the NCBI database established a close link to Brevibacillus agri. The highest expression from transformed E. coli BL21 was achieved with 0.8 mM IPTG following 6 hours of induction. The resulting recombinant keratinase (KerH), purified by Ni-affinity chromatography, possessed 283 U/mg specific activity and displayed ~45 kDa band on SDS-PAGE and zymogram. Secondary structure analysis and active site prediction was performed computationally. Considering the extensive applications of keratinase, KerH was found to be useful in dehairing animal skin surfaces without any damage. The encapsulated KerH possessed improved stability and better compatibility with commercial detergents. It efficiently removed blood, turmeric, strawberry, and egg yolk stains from the fabric. Furthermore, KerH significantly degraded the poultry feathers and provided a protein hydrolysate that helped in converting damaged, dull and curly hair into healthier, shiny and straightened hair.</p><p><strong>Conclusion: </strong>The recombinant KerH from Brevibacillus agri can be considered as a valuable microbial keratinase that can be used as an alternative to the eco hazardous chemicals used in commercial applications of feather degradation, hair protein treatment, feather keratin hydrolysate production and hide dehairing.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":""},"PeriodicalIF":1.0,"publicationDate":"2025-07-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144691292","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Antimicrobial Activity of a Defensin-Rich Fraction from Capsicum Chinense Fruits: Insights for Biotechnological Applications against Fungal Infections.","authors":"Mariana C L Aguieiras, Érica O Mello, Larissa M Resende, Gabriel B Taveira, Thaynã A M Souza, Milena B Cherene, Arielle P B F Oliveira, Celso S Nagano, Renata P Chaves, Andre O Carvalho, Rosana Rodrigues, Fernanda Trindade, Maura Da Cunha, Valdirene M Gomes","doi":"10.2174/0109298665377738250626233111","DOIUrl":"https://doi.org/10.2174/0109298665377738250626233111","url":null,"abstract":"<p><strong>Background: </strong>The increasing resistance of fungal pathogens to conventional antifungal treatments has led to a global rise in fungal infections, affecting human health (Candida spp.) and agricultural productivity (Colletotrichum and Fusarium spp.). Antimicrobial peptides (AMPs), such as defensins, have gained attention for their potential in controlling these infections due to their broad-spectrum activity.</p><p><strong>Objectives: </strong>The aim of this study was to partially purify and characterize the antifungal activity of a defensin-enriched fraction (F3) from Capsicum chinense fruits. Specifically, we sought to evaluate its efficacy against pathogenic fungi and yeasts, and to assess the relative abundance of defensins in the fraction.</p><p><strong>Methods: </strong>The F3 fraction was obtained using ion exchange and molecular exclusion chromatography. Reverse-phase chromatography (HPLC) was then employed for further purification. The antifungal activity of F3 was tested against Colletotrichum, Fusarium, and Candida species. Mass spectrometry was used to identify and characterize the defensin (CcDef3) within the fraction. The presence of the defensin relative to other components was inferred from electrophoretic profiles and peptide analysis.</p><p><strong>Results: </strong>The F3 fraction exhibited significant antifungal activity, with growth inhibition of Colletotrichum lindemuthianum of 51% and 60.9% at concentrations of 100 and 200 μg mL-1, respectively. The fraction also inhibited the growth of several Candida species, notably C. nivariensis (93.8%) and C. bracarensis (79.6%) at 100 μg mL-1. Cell viability analysis indicated a fungistatic effect. Fluorescence microscopy assays showed that F3 induced membrane permeabilization in C. parapsilosis and C. lindemuthianum, and increased ROS production in C. pelliculosa and F. solani. The defensin-rich H8 fraction, containing a 6.5 kDa protein (CcDef3), was identified as a major component via mass spectrometry.</p><p><strong>Conclusion: </strong>These results suggest that the F3 fraction, particularly the defensin CcDef3, has potential as an antifungal agent for biotechnological and therapeutic applications. However, further studies are needed to quantify the contribution of CcDef3 relative to other components in the fraction and to fully isolate the defensin for in-depth analysis.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":""},"PeriodicalIF":1.0,"publicationDate":"2025-07-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144660020","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Purification, Crystallization, and Preliminary X-Ray Diffraction Studies on Hemoglobin from the Angora Goat (Capra Aegagrus Hircus).","authors":"Farheen Pervez, Shobana Nagaraj, Mpho Setshedi, Arshad Mather, Ponnuswamy Mondikalipudur Nanjappa Gounder, Yasien Sayed, Ramesh Pandian","doi":"10.2174/0109298665370730250708065019","DOIUrl":"https://doi.org/10.2174/0109298665370730250708065019","url":null,"abstract":"<p><strong>Introduction: </strong>Angora goats are a distinct breed that differs significantly from common goats and shares a similar appearance to sheep. In Angora goats, only the level of glutathione (GSH) is elevated during under-stimulated conditions, as well as after the period of hypoxic stress; however, no changes are found in 2,3-diphosphoglycerate (2,3-DPG) levels, which are commonly present in the red blood cells (RBCs) of most mammals. We chose the Angora goat for our investigation because no previous studies have been conducted on the structural and functional aspects of hemoglobin (Hb). In addition, no sequence or structural information is currently available in any database.</p><p><strong>Methods: </strong>Angora goat Hb was isolated and purified by anion-exchange chromatography, followed by crystallization using various methods. X-ray data collection for Angora goat Hb was performed under a liquid nitrogen cryo-stream using a Bruker D8 Venture Bio Photon III 28-pixel array area detector system.</p><p><strong>Results: </strong>Good diffracting crystals were obtained using the hanging-drop vapor-diffusion method with polyethylene glycol (PEG) 3350 as the precipitant in water, without the addition of any salt or buffer. The Angora goat Hb diffracted to a resolution of 1.85 Å, and the structure solution was obtained by the molecular replacement method, using the structure of domestic goat Hb as the starting model.</p><p><strong>Discussion: </strong>The solved structure of Angora goat crystallized in the monoclinic space group P21, consisting of one whole biological molecule in the asymmetric unit, with unit cell dimensions of a = 52.08 Å, b = 76.70 Å, c = 74.08 Å, and β = 91.77 °. The solvent content and Matthews coefficient (Vm) for the Angora goat Hb are 49.05% and 2.41 Å3/Da, respectively, and are within the normal range for protein crystals.</p><p><strong>Conclusion: </strong>Purification, crystallization, and preliminary X-ray diffraction studies of Angora goat Hb were performed successfully. Structural refinement and biophysical characterization of Angora goat Hb are in progress in the absence and presence of GSH and 2,3-DPG.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":""},"PeriodicalIF":1.0,"publicationDate":"2025-07-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144637804","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Innovative Immunoinformatics Tools for Enhancing MHC (Major Histocompatibility Complex) Class I Epitope Prediction in Immunoproteomics.","authors":"Virendra S Gomase, Rupali Sharma, Suchita P Dhamane","doi":"10.2174/0109298665373152250625054723","DOIUrl":"https://doi.org/10.2174/0109298665373152250625054723","url":null,"abstract":"<p><p>Immune responses depend on the identification and prediction of peptides that bind to MHC (major histocompatibility complex) class I molecules, especially when it comes to the creation of vaccines, cancer immunotherapy, and autoimmune disorders. The ability to predict and evaluate MHC class immunoproteomics have completely transformed I epitopes in conjunction with immunoinformatics technologies. However, precisely identifying epitopes across various populations and situations is extremely difficult due to the complexity and diversity of MHC class I binding peptides. The most recent developments in immunoinformatics technology that have improved MHC class I epitope prediction are examined in this article. The sensitivity and specificity of epitope prediction have been greatly enhanced by recent developments that have concentrated on bioinformatics algorithms, artificial intelligence, and machine learning models. Potential epitopes are predicted using large-scale peptide-MHC binding data, structural characteristics, and interaction dynamics using tools like NetMHC, IEDB, and MHCflurry. Additionally, the integration of proteomic, transcriptomic, and genomic data has improved prediction accuracy in real-world scenarios by enabling more accurate identification of naturally occurring peptides. Furthermore, newer techniques like deep learning and multi-omics data integration have the potential to overcome peptide binding prediction constraints. Utilizing these technologies is expected to speed up the identification of new epitopes, improve the accuracy of immunotherapy techniques, and enable customized vaccine development. These innovative techniques, their uses, and potential future developments for improving MHC class I epitope prediction in immunoproteomics are highlighted in this study.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":""},"PeriodicalIF":1.0,"publicationDate":"2025-07-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144637801","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Optimizing Sleep in Athletes: The Potential of α-Lactalbumin in Nutrition Intervention.","authors":"Jingjing Li, Xuepeng Bian","doi":"10.2174/0109298665363873250623103811","DOIUrl":"https://doi.org/10.2174/0109298665363873250623103811","url":null,"abstract":"<p><p>Athletes frequently encounter sleep deprivation due to the demands of high-intensity training and competition, which can significantly impair their physical recovery and athletic performance. α-Lactalbumin (α-LA), a key component of whey protein that is rich in tryptophan, has been shown to promote the synthesis of serotonin and melatonin, thereby regulating sleep cycles. Moreover, α-LA has demonstrated the ability to reduce inflammation and oxidative stress associated with fatigue and stress, further contributing to improved sleep quality. This review provides a critical evaluation of the current evidence supporting the role of α-LA in enhancing sleep quality in athletes through mechanisms such as neurotransmitter regulation, immune function improvement, and enhancement of antioxidant defenses. Additionally, it highlights the necessity for further research into the differential effects of α-LA on sleep across various sports and gender groups, as well as its potential synergistic interactions with other nutrients. These insights are essential for developing optimized nutritional interventions aimed at enhancing athletic performance.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":""},"PeriodicalIF":1.0,"publicationDate":"2025-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144637802","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Protein and Peptide Therapeutics: Stability Challenges, Regulatory Demands, and Innovative Formulation Solutions for Enhanced Clinical Effectiveness.","authors":"Megha Patel, Dhruv Parikh, Akshay Parihar, Bhupendra Prajapati, Meenakshi B Patel, Sagar Salave, Ravi Patel, Rishabha Malviya, Rahul Maheshwari, Dignesh Khunt","doi":"10.2174/0109298665375151250626124048","DOIUrl":"https://doi.org/10.2174/0109298665375151250626124048","url":null,"abstract":"<p><p>Proteins and peptides play a crucial role in biological functions and contemporary therapeutic approaches; however, their clinical effectiveness is frequently hindered by swift renal clearance and enzymatic degradation. Peptides possess structured amino acid sequences that facilitate targeted drug delivery and enhance patient adherence. In contrast, proteins demonstrate intricate stability behaviors affected by pH and environmental conditions, requiring careful formulation strategies. Addressing these challenges necessitates a comprehensive understanding of stability and regulatory requirements. Regulatory agencies, including the FDA, EMA, and PMDA, require comprehensive stability testing per guidelines such as ICH Q5C and ICH Q1A(R2). This ensures meticulous management of factors such as temperature control, formulation optimization, and aggregation mitigation. Stability enhancement requires the application of innovative techniques, including protein engineering, lyoprotection, and nanoparticle encapsulation, in conjunction with ongoing quality monitoring. Integrating scientific expertise with regulatory standards enables researchers and pharmaceutical manufacturers to develop safe, effective, and compliant protein and peptide therapeutics for various patient populations.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":""},"PeriodicalIF":1.0,"publicationDate":"2025-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144637803","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Serum and Urinary Proteomic Signatures Revealing Redox and Metabolic Dysregulation in Acute Achilles Tendon Rupture.","authors":"Bayixiati Qianman, Tuomilisi Jiasharete, Aikeremu Wupuer, Aerziguli Tuerxun, Ayidaer Jialihasi, Abuduhilil Mamately, Naertai Yeerbo, Nuerai Shawutali, Ayinazi Badalihan, Amuding Aisaiding, Darebai Redati, Jianati Wuerliebieke, Adili Aizezi, Yemenlehan Bahesutihan, Bo Zhao, Nuermaimaiti Ainiwaer, Jiasharete Jielile","doi":"10.2174/0109298665374669250627205138","DOIUrl":"https://doi.org/10.2174/0109298665374669250627205138","url":null,"abstract":"<p><strong>Objectives: </strong>The etiology of acute Achilles tendon rupture (ATR) remains elusive. A comprehensive case-control study of the proteome profile was conducted to gain insights into the potential pathogenesis of acute ATR and identify novel biomarkers.</p><p><strong>Method: </strong>Serum and urine samples were collected from 15 acute ATR patients and 15 healthy individuals for proteome analysis. Protein levels were assessed using isobaric tags for relative and absolute quantitation (iTRAQ) for serum and label-free proteomic approaches for urine. Differential expression was considered significant at levels exceeding 2-fold (for urine) and 1.2-fold (for serum), with a p-value below 0.05.</p><p><strong>Results: </strong>In serum and urine samples, 44 and 198 proteins were identified, respectively, which exhibit significant differences between acute ATRs and normal Achilles tendons. Our bioinformatics analysis revealed the involvement of multiple biological processes and pathways in acute ATRs, including immune response, metabolism, and redox regulatory pathways. Several differentially expressed proteins were found to participate in various metabolic pathways, suggesting their potential pivotal roles in ATR pathogenesis. Furthermore, protein-protein interaction analysis of the differentially expressed proteins (P<0.05) highlighted abnormalities in major protein-protein interaction hubs, specifically pyruvate kinase (PKM), peroxiredoxin-1 (PRDX1), phosphoglycerate kinase 1 (PKG1), profilin-1, and apolipoprotein A-IV, observed in the serum and urine samples of acute ATR patients.</p><p><strong>Conclusion: </strong>Abnormal nitrogen, carbohydrate, glucose, and long-chain fatty acid metabolic proteins, as well as PKM, PRDX1, and PGK1 abnormalities, may be involved in the pathogenesis of acute ATR.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":""},"PeriodicalIF":1.0,"publicationDate":"2025-07-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144609198","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}