Cellular Physiology and Biochemistry最新文献

{"title":"Tendon Cell Biology: Effect of Mechanical Loading.","authors":"Mikołaj Stańczak, Bartłomiej Kacprzak, Piotr Gawda","doi":"10.33594/000000743","DOIUrl":"https://doi.org/10.33594/000000743","url":null,"abstract":"<p><p>Tendons play a crucial role in the musculoskeletal system, connecting muscles to bones and enabling efficient force transfer. However, they are prone to acute and chronic injuries, which, if not properly repaired, can significantly impair function. Tendinopathy, a prevalent condition affecting approximately 20% of musculoskeletal complaints, arises from an imbalance between micro-injury accumulation and repair processes. The extracellular matrix (ECM) of tendons is a hierarchical structure comprising collagen fibrils, proteoglycans, and glycoproteins that regulate organization, hydration, and mechanical properties. Mechanotransduction pathways, mediated by integrins and focal adhesion complexes, activate signaling cascades such as MAPK/ERK and PI3K/Akt, driving tenocyte gene expression and ECM remodeling. Adaptations to load involve region-specific remodeling, with tensile regions favoring aligned Type I collagen and compressive regions promoting proteoglycans like aggrecan. Stress shielding or reduced loading disrupts these pathways, leading to matrix disorganization and inflammation, predisposing tendons to degenerative changes. Insights into these molecular mechanisms inform rehabilitation strategies to enhance tendon repair and mitigate tendinopathy progression in both athletic and general populations.</p>","PeriodicalId":9845,"journal":{"name":"Cellular Physiology and Biochemistry","volume":"58 6","pages":"677-701"},"PeriodicalIF":2.5,"publicationDate":"2024-11-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142680959","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":"Antibacterial Activity of Silver Nanoparticles Prepared from Camellia Sinensis Extracts in Multi-Drug Resistant Staphylococcus Aureus.","authors":"Hawazen Salih, Rami Altameemi, Ahmed Al-Azawi","doi":"10.33594/000000741","DOIUrl":"https://doi.org/10.33594/000000741","url":null,"abstract":"&lt;p&gt;&lt;strong&gt;Background/aims: &lt;/strong&gt;The nano-method has been used as a technique for creating novel, non-traditional antimicrobial agents. This effective method for treating infectious diseases has many advantages over conventional antibiotics, including increased efficacy against species that have developed drug resistance, and the ability to circumvent the development of resistance that disrupts a number of biological pathways. As a result, the objective of this study was to synthesize and characterize silver nanoparticles using phenolic compounds obtained from &lt;i&gt;Camellia sinensis&lt;/i&gt; . The nanoparticles were then used as antibacterial agents on the multidrug resistant &lt;i&gt;Staphylococcus aureus,&lt;/i&gt; as well as&lt;i&gt;,&lt;/i&gt; biofilm formation mechanism were also investigated.&lt;/p&gt;&lt;p&gt;&lt;strong&gt;Methods: &lt;/strong&gt;Ten isolates of &lt;i&gt;Staphylococcus aureus&lt;/i&gt; were acquired from the labs of the University of Baghdad's Genetic Engineering and Biotechnology Institute. The VITEK-2 system was used to confirm the diagnosis. Aqueous and methanolic extracts of &lt;i&gt;Camellia sinensis&lt;/i&gt; leaves were used to create silver nanoparticles and obtain CAgNPs, which were then characterized using Atomic Fluorescence Microscopy (AFM), X-ray diffractometer (XRD), and Zeta potential analyzers. The extracts were put through a series of assays, including High-performance liquid chromatography (HPLC), antibacterial activity assessments, and the microtiter plate method to determine the lowest inhibitory concentration (MIC) and antibiofilm formation.&lt;/p&gt;&lt;p&gt;&lt;strong&gt;Results: &lt;/strong&gt;Both aqueous and methanolic extracts containing silver nanoparticles included spherical nanoparticles that may be single or combined. The HPLC results showed the presence of two phenolic compounds (gallic acid and caffeine) by comparing their retention durations to those of the reference compounds. The results of the antibacterial activity of (CAgNPs) showed that the methanolic (CAgNPs) extract was more effective than the aqueous (CAgNPs) extract, producing inhibitory zones of 15.67 ± 0.58 and 20.33 ± 0.58 mm, at 375 and 750 ppm respectively, when compared to the aqueous (CAgNPs) extract, which produced inhibitory zones of 12.33 ± 0.58 and 15.67 ± 0.58 mm, respectively. The MIC result also showed that the CAgNPs methanolic extract was more effective than the CAgNPs aqueous extract. The MIC of the CAgNPs methanolic extract on &lt;i&gt;S. aureus&lt;/i&gt; isolates were 11.718 and 23.43 µg/ml, while the MIC of the CAgNPs aqueous extract on all &lt;i&gt;S. aureus&lt;/i&gt; isolates were 46.87 µg/ml except isolate No. 3 and 6 which was 11.718 and 93.75 µg/ml respectively. Additionally, The anti-biofilm in &lt;i&gt;S. aureus&lt;/i&gt; was increased when CAgNPs methanolic extract were used compared with the CAgNPs aqueous extract, the CAgNPs methanolic extract inhibited 80%, 90% and 100% of the biofilm formation of &lt;i&gt;S. aureus&lt;/i&gt; in 23.43, 46.87 and 93.75 µg/ml respectively, while the anti-biofilm activity of the CAgNPs aqueous extract on &lt;i&gt;S. au","PeriodicalId":9845,"journal":{"name":"Cellular Physiology and Biochemistry","volume":"58 6","pages":"659-676"},"PeriodicalIF":2.5,"publicationDate":"2024-11-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142615695","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":"Retraction.","authors":"","doi":"10.33594/000000739","DOIUrl":"https://doi.org/10.33594/000000739","url":null,"abstract":"","PeriodicalId":9845,"journal":{"name":"Cellular Physiology and Biochemistry","volume":"58 5","pages":"657"},"PeriodicalIF":2.5,"publicationDate":"2024-10-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142615690","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":"Retraction.","authors":"","doi":"10.33594/000000736","DOIUrl":"https://doi.org/10.33594/000000736","url":null,"abstract":"","PeriodicalId":9845,"journal":{"name":"Cellular Physiology and Biochemistry","volume":"58 5","pages":"654"},"PeriodicalIF":2.5,"publicationDate":"2024-10-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142615617","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":"Retraction.","authors":"","doi":"10.33594/000000740","DOIUrl":"https://doi.org/10.33594/000000740","url":null,"abstract":"","PeriodicalId":9845,"journal":{"name":"Cellular Physiology and Biochemistry","volume":"58 5","pages":"658"},"PeriodicalIF":2.5,"publicationDate":"2024-10-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142615693","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":"Retraction.","authors":"","doi":"10.33594/000000738","DOIUrl":"https://doi.org/10.33594/000000738","url":null,"abstract":"","PeriodicalId":9845,"journal":{"name":"Cellular Physiology and Biochemistry","volume":"58 5","pages":"656"},"PeriodicalIF":2.5,"publicationDate":"2024-10-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142615640","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":"Retraction.","authors":"","doi":"10.33594/000000737","DOIUrl":"https://doi.org/10.33594/000000737","url":null,"abstract":"","PeriodicalId":9845,"journal":{"name":"Cellular Physiology and Biochemistry","volume":"58 5","pages":"655"},"PeriodicalIF":2.5,"publicationDate":"2024-10-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142615620","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":"A Comprehensive Pan-Cancer Analysis of the Mitochondrial Uncoupling Protein UCP2, with a Focus on Sex and Gender-Related Aspects.","authors":"Soha Sadeghi, Vanessa Checchetto, Tatiana Varanita","doi":"10.33594/000000735","DOIUrl":"10.33594/000000735","url":null,"abstract":"<p><strong>Background/aims: </strong>Mitochondrial uncoupling protein 2 (UCP2) plays a crucial role in regulating oxidative stress and cellular metabolism, positioning it as an important subject in oncological research. The involvement of UCP2 in cancer is complex and context-dependent, suggesting it as a potential therapeutic target. In this study, we aimed to perform a comprehensive pan-cancer analysis of UCP2, with a particular focus on gender-related malignancies such as breast (BRCA), prostate (PRAD), ovarian (OV), and testicular tumors (TGCT).</p><p><strong>Methods: </strong>We analyzed <i>UCP2</i> expression in The Cancer Genome Atlas (TCGA), examining correlations with prognosis, tumor mutational burden (TMB), microsatellite instability (MSI), immune cell infiltration, immune checkpoint genes, genes involved in steroidogenesis, sex hormone receptor genes, and drug sensitivity.</p><p><strong>Results: </strong>Significant variability in UCP2 expression was observed across cancer types. <i>UCP2</i> levels were elevated in BRCA and OV but reduced in PRAD and TGCT. High <i>UCP2</i> expression was associated with a better prognosis in OV and poorer overall survival in PRAD. Furthermore, <i>UCP2</i> correlated with TMB and MSI in OV, TGCT, and BRCA. <i>UCP2</i> expression was also linked to immune cell infiltration, immune checkpoint genes, steroidogenic genes, and sex hormone receptor genes, with variable effects depending on cancer type and gender. Additionally, <i>UCP2</i> also demonstrated sensitivity to specific anticancer drugs.</p><p><strong>Conclusion: </strong>Our findings highlight the interplay between UCP2, immune and hormonal pathways, and drug response and reveal potential opportunities for new therapeutic combinations, especially in gender-related cancers.</p>","PeriodicalId":9845,"journal":{"name":"Cellular Physiology and Biochemistry","volume":"58 5","pages":"630-653"},"PeriodicalIF":2.5,"publicationDate":"2024-10-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142521115","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":"Nitric Oxide-Dependent Regulation of Oxygen-Related Processes in a Rat Model of Lead Neurotoxicity: Influence of the Hypoxia Resistance Factor.","authors":"Natalia Kurhaluk, Piotr Kamiński, Oleksandr Lukash, Halina Tkaczenko","doi":"10.33594/000000734","DOIUrl":"https://doi.org/10.33594/000000734","url":null,"abstract":"&lt;p&gt;&lt;strong&gt;Background/aims: &lt;/strong&gt;Lead exposure is known to induce oxidative stress and neurotoxicity. Nitric oxide (NO) plays an important role in modulating oxidative stress, with L-arginine as a precursor of NO and N&lt;sup&gt;ω&lt;/sup&gt;-nitro-L-arginine (L-NNA) as an inhibitor of NO synthase, an enzyme that catalyses the production of nitric oxide (NO) from L-arginine.&lt;/p&gt;&lt;p&gt;&lt;strong&gt;Methods: &lt;/strong&gt;This study investigated the differential effects of L-arginine and L-NNA on markers of oxidative stress and biochemical changes in brain tissue from rats with different levels of resistance to hypoxia exposed to lead nitrate. Rats with either low or high resistance to hypoxia were exposed to lead nitrate (oral 3.6 mg lead nitrate/kg b.w. per day for 30 days) and treated with L-arginine (600 mg/kg b.w., i.p., 30 min before and after exposure to lead nitrate) or L-NNA (35 mg/kg b.w., i.p., 30 min before and after exposure to lead nitrate). Brain tissue samples were analysed for lipid peroxidation, oxidative modification of proteins, and activity of antioxidant enzymes, including superoxide dismutase, catalase, glutathione reductase, and peroxidase, and total antioxidant status (TAS). We also examined the biomarkers of biochemical pathways involving the activity of alanine and aspartate aminotransferases, succinate dehydrogenase (SDH), and α-ketoglutarate dehydrogenase (KGDH). In addition, the trend observed was supported by assessments of the acetylcholine levels and acetylcholinesterase activity (ACh-AChE system) in brain tissue.&lt;/p&gt;&lt;p&gt;&lt;strong&gt;Results: &lt;/strong&gt;In rats with low resistance to hypoxia, the L-arginine treatment significantly reduced lipid peroxidation and oxidative protein modification but increased antioxidant enzyme activity, suggesting a protective effect against lead-induced oxidative stress. Conversely, in rats with high resistance to hypoxia, L-NNA had a protective effect, reducing lead-induced oxidative damage and decreasing lipid peroxidation, whereas L-arginine exacerbated oxidative stress and impaired antioxidant defences. These findings were supported by corresponding changes in the acetylcholine-acetylcholinesterase system, reflecting the observed patterns of lead-induced oxidative stress and neurotoxicity. The study shows that L-arginine exerts a protective effect by reducing lead-induced oxidative damage via an improvement in TAS. Our study shows that lead nitrate exposure significantly increases ala-nine and aspartate aminotransferase activity in brain tissue, with L-arginine exacerbating and L-NNA reversing this effect. The lead nitrate exposure also affected the activities of SDH and KGDH, which are important for cellular energy production and hypoxia resistance, with L-arginine altering SDH activity depending on the level of resistance and L-NNA enhancing both SDH and KGDH activities. These trends were further validated by alterations in the ACh-AChE system, highlighting the differential role of NO-dependent mechanisms in","PeriodicalId":9845,"journal":{"name":"Cellular Physiology and Biochemistry","volume":"58 5","pages":"597-629"},"PeriodicalIF":2.5,"publicationDate":"2024-10-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142496045","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":"BMI-1 in Breast Cancer - Biological Role and Clinical Implications.","authors":"Aleksandra Szustka, Anna Krześlak","doi":"10.33594/000000733","DOIUrl":"10.33594/000000733","url":null,"abstract":"<p><p>Breast cancer is the most frequent cancer among women. Despite extensive research in recent years the molecular basis of breast cancer development, growth and metastasis remains unclear. Numerous studies highlight the involvement of BMI-1 in tumorigenesis. BMI-1 protein is a key component of Polycomb Repressive Complex 1, which by ubiquitinylation of histone H2A, regulates expression of genes involved in various cellular processes including cell cycle, proliferation and programmed cell death. Overexpression of BMI-1 has been often associated with breast cancer development and progression. This review summarizes the current state of knowledge of BMI-1's role in breast cancer biology and its potential significance as prognostic marker and potential target of new anticancer therapy.</p>","PeriodicalId":9845,"journal":{"name":"Cellular Physiology and Biochemistry","volume":"58 5","pages":"584-596"},"PeriodicalIF":2.5,"publicationDate":"2024-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142459218","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}