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and mastitis.BACKGROUND Total hemoglobin (tHb) measurement is indispensable for determining the patient's condition (hemorrhagic vs. ischemic) and need for blood transfusion. Conductivity- and absorbance-based measurement methods are used for blood gas analysis of tHb. For conductivity-based measurement, tHb is calculated after converting blood conductivity into a hematocrit value, whereas absorbance measurement is based on light absorbance after red blood cell hemolysis. Due to changes in plasma electrolytes and hemolysis, there is a possibility that conductivity- and absorbance-based measurement methods may cause a difference in tHb. METHODS In this study, test samples with controlled electrolyte changes and hemolysis were created by adding sodium chloride, distilled water or hemolytic blood to blood samples collected from healthy volunteers, and tHb values were compared between both methods. RESULTS Conductivity-based measurement revealed reduced tHb value (from 15.49 to 13.05 g/dl) following the addition of 10% sodium chloride, which was also reduced by the addition of hemolysate. Conversely, the addition of distilled water significantly increased tHb value than the expected value. In the absorbance method, there was no significant change in tHb value due to electrolyte change or hemolysis. CONCLUSIONS We have to recognize unexpected conductivity changes occur at all times when tHb is measured via conductivity- and absorbance-based measurement methods. The absorbance method should be used when measuring tHb in patients with expected blood conductivity changes. However, when using this method, the added contribution of hemoglobin from hemolytic erythrocytes lacking oxygen carrying capacity must be considered. We recognize that discrepancy can occur between conductivity- and absorbance-based measurement methods when tHb is measured.BACKGROUND Transient receptor potential (TRP) channels, especially canonical TRP channel subfamily members 3 (TRPC3) and 6 (TRPC6), have attracted attention as a putative therapeutic target of heart | 1 failure. Moreover, TRPC3 and TRPC6 channels are physiologically important for maintaining cellular homeostasis. How TRPC3/C6 channels alter intracellular signaling from adaptation to maladaptation has been discussed for many years. We recently showed that formation of a protein signal complex between TRPC3 and NADPH oxidase (Nox) 2 caused by environmental stresses (e.g., hypoxia, nutritional deficiency, and anticancer drug treatment) promotes Nox2-dependent reactive oxygen species production and cardiac stiffness, including myocardial atrophy and interstitial fibrosis, in rodents. In fact, pharmacological prevention of the TRPC3-Nox2 protein complex can maintain cardiac flexibility in mice after anti-cancer drug treatment. CONCLUSION In this mini-review, we discuss the relationship between TRPC3/C6 channels and cardiovascular disease, and propose a new therapeutic strategy by focusing on pathology-specific protein- protein interactions. Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.BACKGROUND Although film-forming hydrogels possess the advantages of both film and hydrogel dosage forms, certain limitations still remain. OBJECTIVE This study aims to investigate the use of film-forming hydrogels and the effects of nanocarriers on the sustained release of a poorly water-soluble drug, curcumin. METHODS The film-forming hydrogels contained either zein or polyvinylpyrrolidone as a film former, in addition to hydroxypropyl methylcellulose, oleic acid, ethanol and water. Curcumin was encapsulated in poly(lactic-co-glycolic acid) and gelatine nanoparticles using a sonoprecipitation method. Free drug and drug-loaded nanoparticles were later dispersed into blank hydrogels to produce the film-forming nanogels. RESULTS The results suggested that the encapsulation of curcumin in nanoparticles could reduce the drug particle size to less than 200nm for easier diffusion and could shield curcumin from chemical interactions that limit its topical permeability. curcumin was more compatible with gelatine nanoparticles than with poly(lactic-coglycolic acid) nanoparticles, and gelatine nanoparticles, in turn, were more compatible with zein than with polyvinylpyrrolidone film-forming nanogels. Therefore, gelatine nanoparticles in zein filmforming nanogels greatly elevated the permeability of curcumin by over five times that afforded by gelatine nanoparticles in polyvinylpyrrolidone film-forming nanogels. CONCLUSION This research suggested that film-forming nanogel is a promising drug delivery system for both improved permeability and sustained topical diffusion of the extremely hydrophobic drug curcumin depending on the compatibility between the nanocarrier and the film-forming hydrogel. selleckchem Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.BACKGROUND Mammary cancer is the most prevalent type of cancer in female dogs. The main cause of mortality is the occurrence of metastasis. The metastatic process is complex and involves the Epithelial-Mesenchymal Transition (EMT), which can be activated by Transforming Growth Factor beta (TGF-β) and involves changes in cellular phenotype, as well as, in the expression of proteins such as E-cadherin, N-cadherin, vimentin and claudin-7. Melatonin is a hormone with oncostatic and anti-metastatic properties and appears to participate in the TGF-β pathway. Thus, the present work aimed to evaluate the expression of EMT markers E-cadherin, N-cadherin, vimentin and claudin-7, as well as, the cell migration of the canine mammary cancer cell line, CF41, after treatment with melatonin and TGF-β silencing. METHODS Canine mammary cancer cell line, CF41, was cultured and characterized in relation to markers ER, PR and HER2. Cell line CF41 with reducing expression level of TGF-β was performed according to Leonel et al. (20with TGF- β1silencing and its effect on EMT. Thus, further studies are needed to confirm this hypothesis. Copyright© Bentham Science Publishers; For any queries, please email at epub@benthamscience.net.

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