RESUMO
The lateral size effect of graphene oxide (GO) on surfaced-enhanced Raman scattering (SERS) property is systematically investigated by using size-fractionalized GO. For the size fractionalization without changes of chemical structure, large-sized GO (LGO) and small-sized GO (SGO) are separated from the as-synthesized GO (AGO) by centrifugation and membrane filtration, respectively. The size-fractionalized GO sheets are immobilized on a solid substrate for the parallel comparison of their SERS property. As a result, we find that LGO shows considerably higher SERS property than SGO for typical Raman probes such as rhodamine 6G and crystal violet. Furthermore, the lateral size effect of GO derivatives is consistently observed when they are hybridized with plasmonic silver nanoparticles. These results indicate that LGO is superior to AGO and SGO as a SERS platform, and it is also quantitatively confirmed by calculating their enhancement factor.
RESUMO
A strong and functional artificial nacre film is developed by using polyethyleneimine-functionalized GO (PEI-GO) and pyrogallol (PG) inspired by insect exoskeleton sclerotization. PEI-GO is macroscopically assembled into the laminated films and then reacted with PG under the optimized condition for their efficient cross-linking through Schiff-base reactions. The internal structure and physicochemical properties of PG-treated PEI-GO (PG@PEI-GO) films are systematically explored with various analytical tools. The optimized PG@PEI-GO films exhibit excellent tensile strength, modulus, and toughness of 216.0 ± 12.9 MPa, 17.0 ± 1.1 GPa, and 2192 ± 538.5 kJ m-3 which are 2.7, 2.8, and 2.3-fold higher than those of GO films, respectively. Furthermore, silver nanoparticles (AgNPs) are densely immobilized on the PG@PEI-GO films harnessing their abundant amine groups, and the AgNPs immobilized PG@PEI-GO films exhibit a high catalytic activity in the conversion of 4-nitrophenol (4-NP) to 4-aminophenol (4-AP) with maintaining structural integrity. Based on the results, we demonstrate that the rational design of interfaces, inspired by natural materials, is an efficient approach to achieving strong and functional GO laminated composite films.
RESUMO
An efficient protection strategy for silver nanowire-based transparent electrodes (AgNW TEs) is developed to enhance their poor adhesion force on substrates and thermal, optical, chemical, and electrical stabilities. Chitin nanofibers (CNFs) and alkali lignin (AL), which possess high mechanical property, a gas/moisture barrier, and UV absorption properties, are successively assembled on AgNW TEs through layer-by-layer (LBL) assembly based on their oppositely charged surfaces. The formation of LBL-assembled CNFs and AL (CNF/AL)10 bilayers, where 10 is the optimized number of bilayers, on the aldehyde-modified AgNW (Al-AgNW) TEs does not deteriorate their electrical conductivity (17.3 ± 2.1 Ω/â¡) and transmittance (90.1 ± 0.3% at 550 nm), and the (CNF/AL)10 bilayer-coated Al-AgNW [(CNF/AL)10@Al-AgNW] TEs present considerable enhancement in their adhesion force and thermal, optical, chemical, and electrical durability. In detail, their optoelectrical properties are stable over 200 cycles of the scotch peel-off test, for 10 h sonication, up to 350 °C, under UV/O3 treatment for 100 min, in 10% HCl and 28% NH3 for 6 and 12 h, and at an electrical potential up to 14 V, respectively. These features make (CNF/AL)10@Al-AgNW TEs suitable as a durable high-performance transparent heater.
RESUMO
BACKGROUND: Sphingosylphosphorylcholine (SPC) has been reported as a novel lipid mediator that exerts various actions on wound healing process. OBJECTIVE: The aim of this study is to evaluate the involvement of interleukin-6 (IL-6) in SPC-induced wound healing acceleration. METHODS: We performed immunohistochemical analysis to demonstrate the IL-6 induction by SPC. To analyze the signaling events, skin fibroblasts were treated with SPC, and then RT-PCR, ELISA and Western blot analyses were carried out. RESULTS: SPC markedly induced interleukin-6 (IL-6) expression in rabbit ear wound. SPC also induced IL-6 expression at both the mRNA and protein levels in human dermal fibroblasts cultured in vitro. SPC rapidly phosphorylated p42/44 extracellular signal-regulated kinase (ERK). Pretreatment with PD 98059, a specific MAPK kinase 1/2 inhibitor, markedly suppressed SPC-induced IL-6 expression in a dose-dependent manner. Protein kinase C (PKC) activation by phorbol myristate acetate (PMA) potentiated IL-6 mRNA expression, whereas PKC inhibition by bisindolylmaleimide blocked SPC-induced p42/44 ERK phosphorylation and IL-6 expression. Over-expression of PKCalpha markedly induced the IL-6 expression and p42/44 ERK activation. CONCLUSION: These results suggest that SPC-induced IL-6 production is mediated by PKC-dependent p42/44 ERK activation in human dermal fibroblasts cultured in vitro.
Assuntos
Derme/metabolismo , Fibroblastos/metabolismo , Interleucina-6/biossíntese , Sistema de Sinalização das MAP Quinases , Fosforilcolina/análogos & derivados , Proteína Quinase C/metabolismo , Esfingosina/análogos & derivados , Cicatrização , Animais , Células Cultivadas , Derme/citologia , Derme/efeitos dos fármacos , Relação Dose-Resposta a Droga , Ativação Enzimática , Epiderme/metabolismo , Epiderme/cirurgia , Fibroblastos/efeitos dos fármacos , Flavonoides/farmacologia , Humanos , Indóis/farmacologia , Interleucina-6/genética , Sistema de Sinalização das MAP Quinases/efeitos dos fármacos , Maleimidas/farmacologia , Proteína Quinase 1 Ativada por Mitógeno/metabolismo , Proteína Quinase 3 Ativada por Mitógeno/metabolismo , Fosforilação , Fosforilcolina/metabolismo , Fosforilcolina/farmacologia , Proteína Quinase C/genética , Proteína Quinase C-alfa/metabolismo , Inibidores de Proteínas Quinases/farmacologia , RNA Mensageiro/biossíntese , Coelhos , Esfingosina/metabolismo , Esfingosina/farmacologia , Acetato de Tetradecanoilforbol/farmacologia , Fatores de Tempo , Transfecção , Cicatrização/efeitos dos fármacosRESUMO
BACKGROUND: Aquaporins (AQPs) are a family of water transporting proteins present in many mammalian epithelial and endothelial cell types. Among the AQPs, AQP3 is known to be a water/glycerol transporter expressed in human skin. OBJECTIVE: The relationship between the expression level of AQP3 and transpidermal water loss (TEWL) in the lesional and peri-lesional skin of psoriasis-affected patients, and skin hydration in the lesional and peri-lesional skin of psoriasis patients, was investigated. METHODS: The expression of AQP3 in psoriasis-affected and healthy control skin was determined using immunohistochemical and immunofluroscence staining. TEWL and skin hydration were measured using a Tewameter® TM210 (Courage & Khazaka, Cologne, Germany) and a Corneometer® CM 820 (Courage & Khazaka), respectively. RESULTS: AQP3 was mainly expressed in the plasma membrane of stratum corneum and the stratum spinosum in normal epidermis. Unlike the normal epidermis, AQP3 showed decreased expression in the lesional and peri-lesional epidermis of psoriasis. TEWL was increased, and skin hydration was decreased, in the lesional and peri-lesional skin of psoriasis patients, compared with the healthy control sample. CONCLUSION: Although various factors contribute to reduced skin hydration in the lesional and peri-lesional skin of psoriasis, AQP3 appears to be a key factor in the skin dehydration of psoriasis-affected skin.
RESUMO
In a search for the wound healing accelerators, we found that tetraacetyl-phytosphingosine (TAPS), a sphingolipid metabolite produced by phytosphingosine acetylation, has significant inhibitory potential on healing of rabbit ear wound. As angiogenesis is fundamental to proper wound healing, we examined the effect of TAPS on angiogenesis using human umbilical vein endothelial cells cultured in vitro. TAPS markedly decreased vascular endothelial growth factor (VEGF)-induced chemotactic migration and capillary-like tube formation. Recognizing its inhibitory potential on angiogenesis, we further investigated the action mechanism of TAPS. TAPS significantly inhibited VEGF-induced proteolytic enzyme production, including matrix metalloproteinase-2, urokinase-type plasminogen activator and plasminogen activator inhibitor-1. TAPS also suppressed VEGF-induced phosphorylation of p42/44 extracellular signal-regulated kinase and c-Jun N-terminal kinase. In addition, TAPS abolished VEGF-induced intracellular calcium increase, measured using laser scanning confocal microscopy. Together, these results suggest that TAPS exerts its inhibitory action on angiogenesis through the inhibition of mitogen-activated protein kinase activation and intracellular calcium increase, thereby affecting the process of wound healing negatively.
Assuntos
Células Endoteliais/efeitos dos fármacos , Neovascularização Fisiológica/efeitos dos fármacos , Esfingosina/análogos & derivados , Cicatrização/efeitos dos fármacos , Acetilação , Animais , Cálcio/metabolismo , Movimento Celular , Células Cultivadas , Células Endoteliais/citologia , Células Endoteliais/enzimologia , MAP Quinases Reguladas por Sinal Extracelular/metabolismo , Humanos , Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo , Metaloproteinase 2 da Matriz/metabolismo , Fosforilação/efeitos dos fármacos , Inibidor 1 de Ativador de Plasminogênio/metabolismo , Coelhos , Transdução de Sinais/efeitos dos fármacos , Esfingosina/química , Esfingosina/farmacologia , Veias Umbilicais/citologia , Ativador de Plasminogênio Tipo Uroquinase/metabolismo , Fator A de Crescimento do Endotélio Vascular/farmacologiaRESUMO
Ceramide is an important constituent of stratum corneum lipids, which act as both physical barriers and signal modulators. We synthesized several ceramide derivatives and investigated their effects on keratinocyte differentiation. RT-PCR and Western blotting showed that the novel synthetic ceramide derivatives K6PC-4 [N-(2,3-dihydroxypropyl)-2-hexyl-3-oxo-decanamide], K6PC-5, [N-(1,3-dihydroxypropyl-2-hexyl-3-oxo-decanamide] and K6PC-9 (N-ethanol-2-hexyl-3-oxo-decanamide) [corrected] These ceramide derivatives elicited a rapid transient increase in intracellular calcium levels, which were measured using laser scanning confocal microscopy. In addition, K6PC-4, K6PC-5, and K6PC-9 stimulated the phosphorylation of p42/44 extracellular signal-regulated kinase and c-Jun N-terminal kinase. In a reconstituted epidermis model, K6PC-4, K6PC-5, and K6PC-9 significantly increased keratin 1 expression in the suprabasal layer. These results indicate that these novel synthetic ceramide derivatives have the potential to promote keratinocyte differentiation, suggesting that the lipid molecules are applicable for treating skin diseases involving abnormal keratinocyte differentiation.
Assuntos
Cálcio/metabolismo , Ceramidas/farmacologia , Queratinócitos/citologia , Queratinócitos/metabolismo , Diferenciação Celular/efeitos dos fármacos , Células Cultivadas , Humanos , Recém-Nascido , Queratinócitos/efeitos dos fármacos , Proteína Quinase 1 Ativada por Mitógeno/metabolismo , Proteína Quinase 3 Ativada por Mitógeno/metabolismoRESUMO
Sphingosylphosphorylcholine (SPC) is a bioactive sphingolipid metabolite that can enhance wound healing. In an effort to find downstream effectors of SPC, we performed microarray analysis and found that the expression of the gene for connective tissue growth factor (CTGF) was significantly affected in human skin fibroblasts cultured in vitro. Northern blot analysis showed that SPC markedly induced CTGF mRNA expression in a dose- and time-dependent manner. Consistent with this result, Western blot analysis also showed that SPC significantly induced the CTGF production. Pretreatment with cycloheximide did not prevent the CTGF induction by SPC, indicating that SPC stimulates CTGF mRNA expression without the increased synthesis of a regulatory protein. Inhibition by pretreatment with Y27632, but not by PD98059 (a mitogen-activated protein kinase 1/2 inhibitor) and LY294002 (a phosphatidylinositol 3-kinase inhibitor), indicated that rho-kinase pathway was involved in SPC-induced CTGF expression. Together, these results reveal the potential importance of CTGF induction as a downstream event in SPC-induced cellular responses.