Uncontrolled bleeding and infection can lead to a significant increase in mortality. Hydrogel sealant has attracted wide attention because of their ability to control bleeding. However, because water interface is a formidable barrier to a strong bonding surface, the challenge remains in finding a product that offers a strong network adhesion combined with anti-infective properties. Inspired by the mechanism of strong adhesive on the biofilm and mussels, we report a novel dual hydrogel adhesive bionic (DBAH) based on chitosan grafted with methacrylate (CS-MA), dopamine (DA), and N-hydroxymethyl acrylamide (NMA) through smooth a process radical polymerization.
CS-MA and DA simultaneously included in the adhesive polymer to mimic the key two-component adhesive: inter polysaccharide adhesin (PIA) on staphylococcal biofilms and 3,4-dihydroxy-L-phenylalanine (DOPA) of the protein shells foot, respectively. DBAH presented strong adhesion at 34 kPa even after three cycles of full immersion in water and can survive up to 168 mm Hg blood pressure, which is significantly higher than the 60-160 mm Hg measured in most clinical settings. Most importantly, these hydrogels presented remarkable hemostatic ability under wet and dynamic in vivo movement while displaying excellent antibacterial properties and biocompatibility. Therefore, DBAH a promising class of biomaterials for high efficiency hemostasis and wound healing.
The eluate denture adhesive is brought into contact with human gingival cells and compared to cells not treated (w / o any elution dental adhesives). cell toxicity was assessed by measuring cell viability (3- (4,5-dimethylthiazol-2-yl) -2,5-diphenyltetrazolium bromide) (MTT) test), the morphology of the cells (immunofluorescence assay), induction of apoptosis / necrosis and the production of oxygen species reactive (ROS) (flow cytometry tests). In addition, the pH of each sample was determined. Data were analyzed using one-way analysis of variance (ANOVA) followed by Dunnett’s multiple comparison test.
Chronic venous ulcers: a review of treatment with fibrin sealant and prognostic progress using proteomics strategy
Venous ulcers are a major cause of ulcers of lower-limb chronic. Difficulty healing encourage research and development of new products to achieve better therapeutic results. Fibrin sealant is one of the alternative routes. In addition to being validated scaffolding and drug delivery systems, it has excellent healing properties. This review covers the last 25 years of literature and shows that fibrin sealant used in a variety of clinical situations to promote the healing of various types of ulcers, particularly chronic. These are mostly veins in origin and usually do not respond to conventional treatment.
Commercially, only homologous fibrin sealant derived from human blood are available, which is very efficient but very expensive. The heterologous fibrin sealant is an experimental product non-commercial cost and easily manufactured because of the raw material. Phase I / II clinical trial has been completed and indicates that the product is safe and efficacious promisingly for the treatment of chronic venous ulcers. In addition, clinical proteomics strategy to assess the prognosis of the disease has been increasingly used.
Description: Caspase-3 activator 3 (compound 2h) induces apoptosis in HL-60 and K562 cells via significant caspase 3 activation. Caspase-3 activator 3 shows antileukemic acticity against HL-60 and K562 cells, with IC50 values of 42.89 and 33.61 μM, respectively[1].
Description: Caspase-3 Antibody: Caspases are a family of cysteine proteases that can be divided into the apoptotic and inflammatory caspase subfamilies. Unlike the apoptotic caspases, members of the inflammatory subfamily are generally not involved in cell death but are associated with the immune response to microbial pathogens. The apoptotic subfamily can be further divided into initiator caspases, which are activated in response to death signals, and executioner caspases, which are activated by the initiator caspases and are responsible for cleavage of cellular substrates that ultimately lead to cell death. Caspase-3 is synthesized as an inactive proenzyme that undergoes proteolytic cleavage by caspases 8, 9 and 10 to produce 2 subunits, termed p20 and p11. These subunits dimerize to form the active enzyme. Caspase-3 proteolytically cleaves and activates other proteins such as caspases 6, 7 and 9.
Description: Caspase-3 Antibody: Caspases are a family of cysteine proteases that can be divided into the apoptotic and inflammatory caspase subfamilies. Unlike the apoptotic caspases, members of the inflammatory subfamily are generally not involved in cell death but are associated with the immune response to microbial pathogens. The apoptotic subfamily can be further divided into initiator caspases, which are activated in response to death signals, and executioner caspases, which are activated by the initiator caspases and are responsible for cleavage of cellular substrates that ultimately lead to cell death. Caspase-3 is synthesized as an inactive proenzyme that undergoes proteolytic cleavage by caspases 8, 9 and 10 to produce 2 subunits, termed p20 and p11. These subunits dimerize to form the active enzyme. Caspase-3 proteolytically cleaves and activates other proteins such as caspases 6, 7 and 9.
Description: This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease. Alternative splicing of this gene results in two transcript variants that encode the same protein. [provided by RefSeq].
Description: This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease. Alternative splicing of this gene results in two transcript variants that encode the same protein. [provided by RefSeq].
Description: This gene encodes a protein which is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 10. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease. Alternative splicing of this gene results in two transcript variants that encode the same protein.
×
By analyzing a sample of fluid from the wound through proteomics strategy, it is possible to predict before treatment ulcers will develop positively and which will be difficult to cure. This prognosis is only possible to evaluate the expression of proteins isolated in exudate and analysis using free label strategy for the shotgun. multicentre clinical trials will be required to evaluate the efficacy of fibrin sealant to treat chronic ulcers, as well as to validate the proteomics strategies for assessing prognosis.