Sunburn causes inflammation, which increases melanin production in skin and causes hyperpigmentation. Angiopoietin-like protein (ANGPTL) 2 is an inflammatory mediator induced in sun-exposed skin areas. However, whether ANGPTL2 functions in melanin production remains unclear.
View Article and Find Full Text PDFUV-induced wrinkle formation owing to the degeneration of the extracellular matrix (ECM) is a major dermatological problem in which abnormal activation of matrix metalloproteinases (MMPs) and elastases have important roles. Heat shock protein 70 (HSP70) has cytoprotective and anti-inflammatory activities. In this study, we examined the effect of HSP70 expression on UV-induced wrinkle formation.
View Article and Find Full Text PDFThe expression of heat shock proteins (HSPs), particularly HSP70, provides resistance to stressors. We recently reported that ultraviolet (UV)-induced melanin production and skin damage were suppressed in transgenic mice expressing HSP70 and that an extract of Eupatorium lindleyanum induces the expression of HSP70 in cells. Here we report the purification of eupalinolide A and B (EA and EB) from E.
View Article and Find Full Text PDFSkin hyperpigmentation disorders due to abnormal melanin production induced by ultraviolet (UV) irradiation are both a clinical and cosmetic problem. UV irradiation stimulates melanin production in melanocytes by increasing intracellular cAMP. Expression of heat shock proteins (HSPs), especially HSP70, is induced by various stressors, including UV irradiation, to provide cellular resistance to such stressors.
View Article and Find Full Text PDFSkin hyperpigmentation disorders as a result of abnormal melanin production induced by ultraviolet (UV) irradiation are both a clinical and a cosmetic problem. This melanin production is mediated by tyrosinase whose expression is positively regulated by microphthalmia-associated transcription factor (MITF). We recently found that expression of heat shock protein 70 (HSP70) inhibits melanin production.
View Article and Find Full Text PDFIrradiation with UV light, especially UVB, causes epidermal damage via the induction of apoptosis, inflammatory responses, and DNA damage. Various stressors, including UV light, induce heat shock proteins (HSPs) and the induction, particularly that of HSP70, provides cellular resistance to such stressors. The anti-inflammatory activity of HSP70, such as its inhibition of nuclear factor kappa B (NF-kappaB), was recently revealed.
View Article and Find Full Text PDFOur previous study suggested that hetero-oligomer formation of guinea pig liver UDP-glucuronosyltransferases (UGTs) 2B21 and 2B22 enhances UGT2B21-catalyzed morphine-6-glucuronidation. In this work, further evidence for a functional hetero-oligomer between UGT2B21 and UGT2B22 was provided by studies of the glucuronidation of chloramphenicol with dual expression in COS-7 cells. UGT2B21 expressed in COS cells was capable of glucuronidating the 3-hydroxyl group of morphine, 4-hydroxybiphenyl, borneol, testosterone, androsterone, and estriol, whereas it had some effect on chloramphenicol.
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