Mine Celik, Mehmet Koca, Zekai Halici, Taha Tavaci, Hamza Halici, Mustafa Ozkaraca, Zeynep Karakoy, Zafer Bayraktutan
{"title":"The Effect of Inhaled Ozone Therapy in Two-Hit Rat Model of Lipopolysaccharides-Induced Acute Lung Injury and Bleomycin-Induced Pulmonary Fibrosis.","authors":"Mine Celik, Mehmet Koca, Zekai Halici, Taha Tavaci, Hamza Halici, Mustafa Ozkaraca, Zeynep Karakoy, Zafer Bayraktutan","doi":"10.1007/s10930-024-10247-4","DOIUrl":"https://doi.org/10.1007/s10930-024-10247-4","url":null,"abstract":"<p><p>Considering the limited treatment options for acute lung injury (ALI) and pulmonary fibrosis (PF), ozone treatment may be promising as a new immunological agent with its ability to modulate cytokines and interferons. We aimed to investigate the effects of inhaled ozone therapy on both ALI and PF in rat models. A total of 48 albino Wistar male rats were included in the study. Lipopolysaccharide (LPS) was used to induce the ALI model, and bleomycin was used for the PF model. The effects of inhaled ozone (O<sub>3</sub>) were investigated using the ELISA method. Hematoxylin&eosin staining, Masson's trichrome staining, and immunohistochemical methods were used for histopathological evaluation. The Interleukin-1 beta (IL-1β), Interleukin-6 (IL-6), Tumor Necrosis Factor-alpha (TNF-α), and Nuclear Factor kappa B subunit p65 (NF-κB p65) levels in the ALI + 0.08 ppm O<sub>3</sub>, ALI + 0.12 ppm O<sub>3</sub>, PF + 0.08 ppm O<sub>3</sub>, and PF + 0.12 ppm O<sub>3</sub> groups statistically decreased to the same extent and approached the levels of control animals. It was observed that IL-1β, IL-6, TNF-α, and NF-κB p65 levels in lung tissues were significantly and dose-dependently decreased compared to the untreated PF and ALI groups, respectively. While fibrosis was severe in the PF + 0.08 ppm O<sub>3</sub> group, it decreased to more moderate levels in the PF + 0.12 ppm O<sub>3</sub> group. The cytokine levels confirmed that inhaled ozone protected the lungs from both ALI and the development of PF.</p>","PeriodicalId":94249,"journal":{"name":"The protein journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-02-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143371416","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"From Crude Extracts to Purity: A Comparative Study of Butyrylcholinesterase Purification.","authors":"Gamze Sonmez, Bahattin Enes Karatas, Ebru Bodur","doi":"10.1007/s10930-025-10248-x","DOIUrl":"https://doi.org/10.1007/s10930-025-10248-x","url":null,"abstract":"<p><p>Butyrylcholinesterase (BChE; EC 3.1.1.8) is an enzyme found in blood plasma and various tissues, playing a key role in metabolizing esters and detoxifying various substances. In this study, we developed a modified purification protocol for BChE from human serum, achieving a higher purification yield (38.3%) and specific activity (60,500 U/mg) compared to previous reports. The method employed a single round of acid dialysis, Sephadex G50 gel filtration chromatography, and procainamide Sepharose 4 fast flow affinity chromatography. Our new approach excludes the commonly used DEAE Trisacryl M chromatography. The goal was to compare this method with our previously employed purification protocols. This study demonstrates that optimizing chromatography steps can enhance enzyme recovery and activity, though further refinement may be needed for higher purification folds. This improved methodology offers a valuable approach for efficient BChE purification with potential for broader applications.</p>","PeriodicalId":94249,"journal":{"name":"The protein journal","volume":" ","pages":""},"PeriodicalIF":0.0,"publicationDate":"2025-02-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143371415","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The protein journalPub Date : 2024-06-01Epub Date: 2024-05-17DOI: 10.1007/s10930-024-10203-2
Amir Sajjad Hojjati-Razgi, Shahram Nazarian, Hossein Samiei-Abianeh, Amir Vazirizadeh, Emad Kordbacheh, Seyed Mojtaba Aghaie
{"title":"Expression of Recombinant Stonustoxin Alpha Subunit and Preparation of polyclonal antiserum for Stonustoxin Neutralization Studies.","authors":"Amir Sajjad Hojjati-Razgi, Shahram Nazarian, Hossein Samiei-Abianeh, Amir Vazirizadeh, Emad Kordbacheh, Seyed Mojtaba Aghaie","doi":"10.1007/s10930-024-10203-2","DOIUrl":"10.1007/s10930-024-10203-2","url":null,"abstract":"<p><p>Stonustoxin (SNTX) is a lethal protein found in stonefish venom, responsible for many of the symptoms associated with stonefish envenomation. To counter stonefish venom challenges, antivenom is a well-established and effective solution. In this study, we aimed to produce the recombinant alpha subunit protein of Stonustoxin from Synanceia horrida and prepare antibodies against it The SNTXα gene sequence was optimized for E. coli BL21 (DE3) expression and cloned into the pET17b vector. Following purification, the recombinant protein was subcutaneously injected into rabbits, and antibodies were extracted from rabbit´s serum using a G protein column As a result of codon optimization, the codon adaptation index for the SNTXα cassette increased to 0.94. SDS-PAGE analysis validated the expression of SNTXα, with a band observed at 73.5 kDa with a yield of 60 mg/l. ELISA results demonstrated rabbits antibody titers were detectable up to a 1:256,000 dilution. The isolated antibody from rabbit´s serum exhibited a concentration of 1.5 mg/ml, and its sensitivity allowed the detection of a minimum protein concentration of 9.7 ng. In the neutralization assay the purified antibody against SNTXα protected mice challenged with 2 LD50. In conclusion, our study successfully expressed the alpha subunit of Stonustoxin in a prokaryotic host, enabling the production of antibodies for potential use in developing stonefish antivenom.</p>","PeriodicalId":94249,"journal":{"name":"The protein journal","volume":" ","pages":"627-638"},"PeriodicalIF":0.0,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140961268","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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