Protein and Peptide Letters最新文献

{"title":"Aloperine Protects Against Cisplatin-Induced Injury in Kidney Cells <i>Via</i> Modulating PI3K/AKT/Nfκb-Mediated NLRP3 Inflammasome.","authors":"Mingning Qiu, Shuai Zhang, Jinglan Liang, Xuguang Wang, Jie Liu","doi":"10.2174/0109298665334965251007043325","DOIUrl":"10.2174/0109298665334965251007043325","url":null,"abstract":"<p><strong>Background: </strong>Aloperine (ALO) is a vital alkaloid present in the traditional Chinese herb Sophora alopecuroides, which has demonstrated effective anti-inflammatory activity. However, the effects and the mechanism of action of ALO on cisplatin (CDDP)-induced nephrotoxicity remain unclear.</p><p><strong>Objective: </strong>This study aimed to investigate the effects of ALO on CDDP-induced nephrotoxicity and its potential mechanism of action <i>in vitro</i>.</p><p><strong>Methods: </strong>Cell viability, lactate dehydrogenase cytotoxicity, apoptosis, activity of Caspase-Glo 3/7 and 1, in-cell western blotting, immunohistochemical staining, and enzyme-linked immunosorbent assay (ELISA) were performed to assess the influence of ALO on CDDP-treated kidney cells. Inhibitors of phosphatidylinositol 3-kinase (PI3K, LY294002), protein kinase B (Akt, AKT inhibitor VIII), and nuclear factor kappa B (NFκB, BAY 11-7082) were used to determine their potential mechanisms of action.</p><p><strong>Results: </strong>The results indicated that ALO significantly reversed the inhibition of cell viability, cytotoxicity, apoptosis, and the release of inflammatory factors induced by CDDP in kidney cells. ALO attenuated the PI3K/AKT/NFκB-mediated pathway activated by CDDP treatment and downregulated the CDDP-induced nucleotide-binding domain, leucine-rich-containing family, pyrin domain-containing-3 (NLRP3) inflammasome. Furthermore, the PI3K and AKT inhibitors diminished the effects of ALO on CDDP-treated kidney cells. Additionally, NFκB inhibitors reversed the effects of the PI3K and AKT inhibitors on ALO in CDDP-treated kidney cells.</p><p><strong>Conclusion: </strong>These results suggest that ALO protects against CDDP-induced injury in kidney cells by modulating the PI3K/AKT/NFκB-mediated NLRP3 inflammasome.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"731-741"},"PeriodicalIF":1.1,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145438997","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":"Role of TPD52 in Endometrial Cancer: Impact on EMT and the PI3K/AKT and ERK/MAPK Signaling.","authors":"Lu Miao, Buze Chen, Linlin Li, Benhong Ma, Guochen Yang, Li Jing","doi":"10.2174/0109298665400400251003013958","DOIUrl":"10.2174/0109298665400400251003013958","url":null,"abstract":"<p><strong>Introduction: </strong>Endometrial carcinoma (EC) incidence and mortality continue to rise, and reliable therapeutic targets remain scarce. We aimed to define the oncogenic role and mechanism of tumor protein D52 (TPD52) in EC, focusing on epithelial-mesenchymal transition (EMT) and the PI3K/AKT and ERK/MAPK signaling pathways.</p><p><strong>Methods: </strong>In this study, we assessed the expression levels of TPD52 in EC tissues and benign endometrial tissues using immunohistochemistry. To further investigate the role of TPD52, we performed experiments both <i>in vitro</i> and <i>in vivo</i>. We transfected siRNA and overexpression (OE) plasmids into Ishikawa and HEC-1-A cell lines to knock down (KD) or overexpress TPD52, respectively. We observed the effects of TPD52 knockdown on tumor growth and EMT through in vitro experiments.</p><p><strong>Results: </strong>TPD52 was significantly upregulated in EC tissues compared with those of benign endometrial tissues. Silencing TPD52 significantly inhibited cell proliferation, migration, and invasion, whereas TPD52 overexpression produced the opposite effects. TPD52 facilitates epithelial-mesenchymal transition (EMT). Moreover, TPD52 stimulates the PI3K/AKT and ERK/MAPK signaling pathways.</p><p><strong>Discussion: </strong>These data position TPD52 as a bona fide EC oncoprotein that drives EMT via dual PI3K/AKT-ERK/MAPK signaling. Limitations include the modest patient cohort and the lack of clinical-pathological correlation analyses.</p><p><strong>Conclusion: </strong>TPD52 promotes EC progression through EMT and PI3K/AKT and ERK/MAPK activation, offering a promising therapeutic target whose clinical utility warrants further investigation.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"718-730"},"PeriodicalIF":1.1,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145372898","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":"Margatoxin Peptide: Preparation and the Potential Use for Biological Applications in Cancer and Neurological Disorders.","authors":"Faride Ranjbari, Masoomeh Dadkhah, Zahra Pirdel, Farzaneh Fathi","doi":"10.2174/0109298665415268251024053300","DOIUrl":"10.2174/0109298665415268251024053300","url":null,"abstract":"<p><p>Scorpion venom compounds are known to contain nucleotides, polypeptides, mucoproteins, lipids, biogenic amines, and other unidentified macromolecules. Several peptides in scorpion fluids have demonstrated a wide range of biological activities with strong specificity for their targeted sites. Margatoxin, isolated from the venom of the scorpion, exhibits desirable properties, including high selectivity, good permeability, and stability in cancer cells, which can be achieved at picomolar doses, thereby blocking voltage-gated K⁺ channels. This narrative review consolidates results from an extensive literature search conducted in major electronic databases up to September 2024. Important studies were identified using keywords associated with scorpion venom peptides, Kv1.3 channels, cancer treatment, and neurodegenerative disorders. The amino acids that make up Margatoxin have an effective molecular function in blocking voltage-gated K⁺ channels 1.3. Due to the abnormally high expression of voltage-gated K⁺ channel 1.3 in various types of cancers, blockers of this channel can inhibit apoptosis, metabolic changes, tumor angiogenesis, invasion, and migration. On the other hand, these channel blockers have emerged as a promising therapeutic approach for neurological disorders, such as Alzheimer's and Parkinson's diseases. The strong efficacy and targeted action of margatoxin further position it as a promising drug candidate. As the number of individuals affected by cancer and neurological conditions continues to rise, research into scorpion venom peptides like margatoxin may lead to innovative therapeutic options for future treatments.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"791-802"},"PeriodicalIF":1.1,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145900849","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":"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":"465-489"},"PeriodicalIF":1.1,"publicationDate":"2025-01-01","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":"Design, Expression, and Purification of a Fusion Enzyme Containing Terminal Deoxynucleotidyl Transferase from <i>B. bovis</i> and DNA-Binding Proteins from <i>E. coli</i>.","authors":"Antos Sachanka, Veronika Shchur, Yaraslau Dzichenka, Aleksei Yantsevich","doi":"10.2174/0109298665372636250504084653","DOIUrl":"10.2174/0109298665372636250504084653","url":null,"abstract":"<p><strong>Background: </strong>Gene fusion techniques have yielded promising results in the fusion of thermostable polymerases (Taq and Pfu) with single-stranded and double-stranded DNA-binding proteins. Constructing a terminal deoxynucleotidyl transferase (TdT) fusion enzyme with DNAbinding protein domains can enhance thermostability and broaden the enzyme's application field. This makes it a promising candidate for cost-effective <i>de novo</i> DNA synthesis and a more effective tool for demonstrating apoptosis and detecting viral DNA/RNA.</p><p><strong>Methods: </strong>The design of fusion proteins was based on molecular dynamics and homology modeling. Native and fusion proteins were isolated using affinity chromatography on HisTrap HP. Thermostability was assessed through differential scanning fluorimetry and dynamic light scattering. HPLC analysis was conducted to evaluate enzyme activity.</p><p><strong>Results: </strong>According to the <i>in silico</i> predictions of the fusion protein structure, a homotetramer was formed. The expressed fusion proteins were successfully purified under native conditions, similar to TdT. The total yields of the studied proteins were 130 mg/L for single-stranded binding protein from <i>E. coli</i> (EcSSB), 5 mg/L for TdT, 9 mg/L for TdT_L1_EcSSB, and 7 mg/L for TdT_L2_EcSSB. The measured radius of TdT (3.5 nm) was found to be consistent with a monomeric structure; however, the fusion proteins were expected to form a homotetramer. Additionally, fusion with EcSSB was found to prevent aggregation, which positively affected the thermal stability of the fusion protein. Instead of elongating the substrate by adding nucleotides, the fusion enzyme removed a nucleotide, specifically TTP, from the 3'-end of the DNA strand.</p><p><strong>Conclusion: </strong>The fusion of TdT with EcSSB resulted in increased thermal stability and a reduced ability to add nucleotides to the substrate.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"353-367"},"PeriodicalIF":1.1,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144142991","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":"MARVELD1 Promotes the Invasiveness in Pancreatic Adenocarcinoma through the Activation of Epithelial-to-Mesenchymal Transition.","authors":"Xianwei Luo, Zhenming Gao","doi":"10.2174/0109298665359781250114055525","DOIUrl":"10.2174/0109298665359781250114055525","url":null,"abstract":"<p><strong>Background: </strong>MARVEL domain-containing 1 (MARVELD1) has been implicated in the progression of several cancers, but its role in pancreatic adenocarcinoma (PAAD) remains poorly understood.</p><p><strong>Methods: </strong>RNA-seq data from the TCGA-PAAD and GTEx-Pancreas cohorts were analyzed to assess MARVELD1 expression. Stable MARVELD1 knockdown and overexpression were conducted in BxPC3 and PANC-1 cells. Cell viability, proliferation, migration, and invasion were evaluated using functional assays, and western blotting was employed to examine EMT-associated protein levels, including Vimentin, MMP2, MMP9, and E-cadherin. Differentially expressed genes (DEGs) between MARVELD1-high and MARVELD1-low groups were identified, and pathway enrichment analyses were performed.</p><p><strong>Results: </strong>We observed a significant increase of MARVELD1 in PAAD patient samples, with elevated MARVELD1 levels correlating with poor clinical survival. Knockdown of MARVELD1 in PAAD cells remarkably decreased cell proliferation and colony formation, while overexpression of MARVELD1 enhanced these properties. Moreover, simulated cell invasion and migration assay further suggested that MARVELD1 might contribute to PAAD cell aggressiveness. Mechanistically, MARVELD1 promoted tumor cell migration and invasion through the activation of Vimentin, MMP2, and MMP9 protein while suppressing E-cadherin. Bioinformatics analysis revealed that MARVELD1-high samples were enriched in EMT-related pathways, including TGF-β receptor signaling, actin cytoskeleton regulation, and cell adhesion.</p><p><strong>Conclusion: </strong>Taken together, our study highlights the roles of MARVELD1 in promoting tumor cell proliferation and invasion, suggesting its potential application as a prognostic and diagnostic biomarker for PAAD in the clinical context.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"224-233"},"PeriodicalIF":1.0,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143024413","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":"Targeting APE1: Advancements in the Diagnosis and Treatment of Tumors.","authors":"Minghui Hu, Yingyu Zhang, Pin Zhang, Kangbo Liu, Mengxin Zhang, Lifeng Li, Zhidan Yu, Xianwei Zhang, Wancun Zhang, Ying Xu","doi":"10.2174/0109298665338519241114103223","DOIUrl":"10.2174/0109298665338519241114103223","url":null,"abstract":"<p><p>With the emergence of the precision medicine era, targeting specific proteins has emerged as a pivotal breakthrough in tumor diagnosis and treatment. Apurinic/apyrimidinic Endonuclease 1 (APE1) is a multifunctional protein that plays a crucial role in DNA repair and cellular redox regulation. This article comprehensively explores the fundamental mechanisms of APE1 as a multifunctional enzyme in biology, with particular emphasis on its potential significance in disease diagnosis and strategies for tumor treatment. Firstly, this article meticulously analyzes the intricate biological functions of APE1 at a molecular level, establishing a solid theoretical foundation for subsequent research endeavors. In terms of diagnostic applications, the presence of APE1 can be detected in patient serum samples, biopsy tissues, and through cellular in situ testing. The precise detection methods enable changes in APE1 levels to serve as reliable biomarkers for predicting tumor occurrence, progression, and patient prognosis. Moreover, this article focuses on elucidating the potential role of APE1 in tumor treatment by exploring various inhibitors, including nucleic acid-based inhibitors and small molecule drug inhibitors categories, and revealing their unique advantages in disrupting DNA repair function and modulating oxidative-reduction activity. Finally, the article provides an outlook on future research directions for APE1 while acknowledging major technical difficulties and clinical challenges that need to be overcome despite its immense potential as a target for tumor therapy.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"18-33"},"PeriodicalIF":1.0,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142795056","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":"Anti-Cancer Bioactive Peptide Induces Apoptosis in Gastric Cancer Cells through TP53 Signaling Cascade.","authors":"Qimuge Suyila, Xian Li, Xiulan Su","doi":"10.2174/0109298665350654250111144722","DOIUrl":"10.2174/0109298665350654250111144722","url":null,"abstract":"<p><strong>Introduction: </strong>Gastric cancer has emerged as one of the major diseases threatening human health. Our previous studies indicated that the anti-cancer bioactive peptide (ACBP) inhibits the initiation and progression of gastric cancer through apoptosis and cell cycle arrest, yet the mechanisms remain unclear. To elucidate the relationships between the effects of ACBP and the levels of cell differentiation, as well as the functional mechanisms of ACBP, we conducted a study using three human gastric cancer cell lines: NCI-N87, MGC-803, and another unspecified line.</p><p><strong>Methods: </strong>We investigated the impact of ACBP on the survival and morphology of these cancer cell lines, examined apoptosis and cell cycle progression, and detected the expression of TP53, TP63, and TP73 in cancer cells, as well as the expression of Bax, PUMA, and Mcl-1 in a xenograft mouse model. ACBP inhibited the proliferation of all three cancer cell lines in a dose-dependent manner, similar to the positive control and 5-fluorouracil (5-FU). The effect of ACBP correlated with the degree of differentiation of the cancer cells; the lower the differentiation degree, the stronger the inhibitory effect.</p><p><strong>Results: </strong>After ACBP treatment, the expression of TP53, TP63, and TP73 increased in all cell lines. In the xenograft mouse model, ACBP inhibited the growth of MGC-803 cells in vivo. The apoptotic-related genes Bax and PUMA were upregulated, while Mcl-1 was downregulated. ACBP inhibited tumor cell growth by inducing apoptosis through the TP53 signaling cascade, upregulating TP53, TP63, and TP73 and their downstream apoptosis-promoting genes Bax and PUMA while downregulating the anti-apoptotic gene Mcl-1.</p><p><strong>Conclusion: </strong>Notably, after ACBP treatment, Mcl-1 expression was significantly reduced in the tumor tissue of the xenograft model, indicating that ACBP induced apoptosis through the TP53 signaling cascade. This project provides a scientific basis for exploring the antitumor mechanism of ACBP in gastric cancer therapy.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"194-205"},"PeriodicalIF":1.0,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143415054","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":"Molecular Interactions of the Antimicrobial Peptide Tritrpticin with Mixed Nanoaggregates: A Fluorescence Spectroscopy Study.","authors":"Kaio César Antunes Rocha, Maria Carolina Oliveira de Arruda Brasil, Eduardo Maffud Cilli, Luiz Carlos Salay","doi":"10.2174/0109298665359223241226091327","DOIUrl":"10.2174/0109298665359223241226091327","url":null,"abstract":"<p><strong>Introduction: </strong>Tritrpticin (TRP3) is a peptide belonging to the cathelicidin family and has a broad spectrum of antimicrobial activity. However, this class of biomolecules can be easily degraded in the body, making it necessary to use an efficient transport system. The ability to form stable nanostructures from the interaction of glycyrrhizin saponin with the pluronic polymer F127 was demonstrated, forming mixed biopolymeric micelles, highly promising as drug carriers.</p><p><strong>Objective: </strong>The present work sought to understand the physicochemical interaction of the antimicrobial peptide TRP3 with the mixed polymeric micelle made from pluronic F127 and the saponin glycyrrhizin.</p><p><strong>Methods: </strong>The interaction of tritrpticin with mixed nanostructured micelles was evaluated through fluorescence spectroscopy and fluorescence quenching with acrylamide. The experiments were performed at room temperature (25 ± 1°C), adopting an excitation wavelength set to 280 nm and emission between 300 and 500 nm, with a slit of 5 nm.</p><p><strong>Results: </strong>The interaction of the cationic peptide tritrpticin with the mixed biopolymeric micelles was observed through the blue shift of the fluorescence emission to shorter wavelengths, proving the change of tryptophan to a more hydrophobic environment. Through the fluorescence suppression technique, it was possible to indicate the location of the peptide in the mixed micelles, proving tritrpticin to be partially inserted inside them.</p><p><strong>Conclusion: </strong>It was concluded that tritrpticin interacted with mixed nanostructured micelles, forming a promising system for biotechnological applications.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"152-160"},"PeriodicalIF":1.0,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143060508","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":"Diminazene Aceturate (DIZE) Ameliorates Hypertension and Induces Anxiolytic- and Antidepressant-like Effects in TGR(mRen2)27.","authors":"Laura Amado Costa, Flavio A G Mourao, Natalia Alenina, Michael Bader, Maria Jose Campagnole-Santos, Lucas M Kangussu","doi":"10.2174/0109298665357730250213050214","DOIUrl":"10.2174/0109298665357730250213050214","url":null,"abstract":"<p><strong>Introduction: </strong>Diminazene aceturate (DIZE) was described as an angiotensin-converting enzyme 2 (ACE2) activator. ACE2/Angiotensin-(1-7)/Mas receptor axis presents protective actions on cardiovascular diseases and plays an important modulatory role in the neurobiology of mood and anxiety disorders.</p><p><strong>Objectives: </strong>To evaluate the effects of chronic intracerebroventricular (ICV) treatment with DIZE on blood pressure, anxiety- and depression-like behaviors in hypertensive transgenic (mRen2)27 rats (TGR).</p><p><strong>Methods: </strong>Male TGR and Sprague-Dawley rats (10-12 weeks old) were subjected to chronic ICV infusion of DIZE (1.0 μg/h for 7 days). Blood pressure and heart rate were measured by tail plethysmography and anxiety- and depression-like behaviors were evaluated through elevated plus maze, marble burying and forced swim tests, respectively.</p><p><strong>Results: </strong>Treatment with DIZE induced a significant reduction in mean arterial pressure in both TGR and SD rats. A decrease in heart rate was only observed in the hypertensive animals. Additionally, treatment with DIZE attenuated the anxiety- and depression-like behaviors that were observed in TGR.</p><p><strong>Conclusion: </strong>DIZE has central anti-hypertensive, anxiolytic, and anti-depressive effects.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"243-252"},"PeriodicalIF":1.1,"publicationDate":"2025-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143493446","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}