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.
Biofilm-inspired adhesive and antibacterial hydrogel with tough tissue integration performance for sealing hemostasis and wound healing
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 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: CASP3 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.
Description: CASP3 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.
Description: Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage.
Description: Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage.
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.
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.
Description: This recombinant Caspase-3 antibody reacts to human full length caspase-3 (35 kDa) and the large fragment of caspase-3 resulting from cleavage (17 kDa).
Description: Caspase-3, also known as YAMA, CPP32 or APOPAIN, is a member of the cysteine-aspartic acid protease family known to interact with family members -8 and -9. It is encoded by the CASP3 gene. Tiso et al.(1996) used radiation hybrid mapping to localize the gene to human chromosome 4q33-q35.1. Fernandes-Alnemri et al.(1994) found that overexpression of CASP3 in insect cells induced apoptosis. Coexpression of the two CASP3 subunits in insect cells also resulted in apoptosis. Tewari et al.(1995) showed that purified human CASP1 cleaved the CASP3 proenzyme into a proteolytically active form and that activated Caspase-3 cleaved PARP into the 85-kD apoptotic form.
Description: Cysteine-aspartic acid protease 3, also known as Apopain, CPP32, CPP32B, and YAMA, is a member of the cysteine-aspartic acid protease family. Western blot analysis of three cell lines revealed the prominent CASP3 band at 32 kD and 20 kD. Several human cancer cell lines showed coexpression of both variants at the mRNA and protein levels. Overexpression of the catalytically inactive Caspase-3 by human kidney cells offered some resistance to inducers of apoptosis, and CASP3 accumulation could be enhanced with addition of proteasome inhibitors. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Alternative splicing of this gene results in two transcript variants that encode the same protein. Orthologs have been identified in numerous mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts. Nicholson et al. developed a potent peptide aldehyde inhibitor and showed that it prevented apoptotic events in vitro, suggesting that the protein is important for the initiation of apoptotic cell death.
Description: Caspase-3 is a caspase protein which interacts with Survivin, XIAP, CFLAR, Caspase 8, HCLS1, Deleted in Colorectal Cancer, TRAF3 and GroEL. This gene which is located at 4q35 encodes a protein that 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 that 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 Alzheimers disease. And the caspase-3 activation in heart failure sequentially cleaves SRF and generates a truncated SRF that appears to function as a dominant-negative transcription factor. Additionally, the caspase-3 influence on bone mineral density should be considered in any in vivo application of caspase-3 inhibitors to the treatment of human disease. In erythroid precursors undergoing terminal differentiation, Hsp70 prevents active CASP3 from cleaving GATA1 and inducing apoptosis.
Description: Caspase-3 is an enzyme which interacts with Survivin, XIAP, CFLAR, CASP8, HCLS1, Deleted in Colorectal Cancer, TRAF3 and GroEL. This gene which is located on 4q35 encodes a protein that is a member of the cysteine-aspartic acid protease family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. They exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. CASP3 is the predominant cysteine-aspartic acid protease involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimers disease. And protein activation in heart failure sequentially cleaves SRF and generates a truncated SRF that appears to function as a dominant-negative transcription factor. Additionally, the proteins influence on bone mineral density should be considered in any in vivo application of Caspase-3 inhibitors to the treatment of human disease. In erythroid precursors undergoing terminal differentiation, Hsp70 prevents active CASP3 from cleaving GATA1 and inducing apoptosis.
Description: Caspase 3 is a caspase protein which interacts with Survivin, XIAP, CFLAR, Caspase 8, HCLS1, Deleted in Colorectal Cancer, TRAF3 and GroEL. This gene which is located on 4q35 encodes a protein that 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 that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. 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. And the caspase-3 activation in heart failure sequentially cleaves SRF and generates a truncated SRF that appears to function as a dominant-negative transcription factor. Additionally, the caspase-3 influence on bone mineral density should be considered in any in vivo application of caspase-3 inhibitors to the treatment of human disease. In erythroid precursors undergoing terminal differentiation, Hsp70 prevents active CASP3 from cleaving GATA1 and inducing apoptosis.
Description: Caspase 3 is a caspase protein which interacts with Survivin, XIAP, CFLAR, Caspase 8, HCLS1, Deleted in Colorectal Cancer, TRAF3 and GroEL. This gene which is located on 4q35 encodes a protein that 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 that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. 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. And the caspase-3 activation in heart failure sequentially cleaves SRF and generates a truncated SRF that appears to function as a dominant-negative transcription factor. Additionally, the caspase-3 influence on bone mineral density should be considered in any in vivo application of caspase-3 inhibitors to the treatment of human disease. In erythroid precursors undergoing terminal differentiation, Hsp70 prevents active CASP3 from cleaving GATA1 and inducing apoptosis.
Description: Available in various conjugation types.
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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.
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