成纤维细胞中的弹性蛋白微纤维界面定位蛋白 1 受两性胰岛素和角质形成细胞产生的白细胞介素-1α的调控。

IF 2.7 4区 医学 Q2 DERMATOLOGY International Journal of Cosmetic Science Pub Date : 2024-02-14 DOI:10.1111/ics.12947
Shinya Kondo, Soichiro Shiga, Tetsuhito Sakurai
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摘要

目的:弹性纤维的结构会随着年龄的增长而发生变化。众所周知,弹性蛋白微纤维界面定位蛋白 1(EMILIN-1)有助于弹性纤维结构的变化。EMILIN-1 是弹性纤维的成分之一,也与表皮附近的氧合纤维共定位。因此,EMILIN-1 可能会受到表皮-真皮相互作用的影响。本研究旨在确定弹性纤维结构退化过程中表皮与真皮相互作用的关键因素:方法:共同培养角质形成细胞和成纤维细胞,评估弹性纤维相关蛋白质的变化。此外,还使用细胞因子阵列来确定参与表皮-真皮相互作用的因子:结果:在有角质形成细胞存在的情况下,成纤维细胞中 EMILIN-1 的表达增加,而当角质形成细胞受到压力时,EMILIN-1 的表达减少。研究发现,安非他酮(AREG)和白细胞介素-1α(IL-1α)是影响成纤维细胞分泌的 EMILIN-1 的产生的角质形成细胞因子。AREG促进EMILIN-1的表达,而IL-1α则通过增加蛋白酶K(一种分解代谢酶)减少EMILIN-1的表达。AREG和IL-1α与成纤维细胞中EMILIN-1水平的变化有关:结论:研究结果表明,抑制表皮中 IL-1α 的表达和促进 AREG 的表达可能是防止因弹性纤维结构变化而产生的皱纹和下垂的一种新方法。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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Elastin microfibril interface-located protein 1 in fibroblasts is regulated by amphiregulin and interleukin-1α produced by keratinocytes

Objective

The structure of elastic fibres changes with ageing. Elastin microfibril interface–located protein 1 (EMILIN-1) is known to contribute to structural changes in elastic fibres. EMILIN-1 is one of the components of elastic fibres and also colocalizes with oxytalan fibres near the epidermis. Therefore, EMILIN-1 may be affected by epidermal–dermal interactions. The purpose of this study is to identify the key factors involved in epidermal–dermal interactions during the structural degeneration of elastic fibres.

Methods

Keratinocytes and fibroblasts were co-cultured, and changes in elastic fibre-related proteins were evaluated. Additionally, cytokine arrays were used to identify the factors involved in epidermal–dermal interactions.

Results

EMILIN-1 expression in fibroblasts was increased in the presence of keratinocytes, and its expression decreased when keratinocytes were stressed. Amphiregulin (AREG) and interleukin-1α (IL-1α) were identified as the keratinocyte-derived cytokines that influence the production of EMILIN-1, which is secreted by the fibroblasts. EMILIN-1 expression was promoted by AREG and decreased by IL-1α via an increase in cathepsin K (a catabolic enzyme). AREG and IL-1α were associated with changes in EMILIN-1 levels in fibroblasts.

Conclusion

The findings suggest that the suppression of IL-1α expression and promotion of AREG expression in the epidermis could be a new approach that prevents the wrinkles and sagging caused by the structural changes in elastic fibres.

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来源期刊
CiteScore
4.60
自引率
4.30%
发文量
73
期刊介绍: The Journal publishes original refereed papers, review papers and correspondence in the fields of cosmetic research. It is read by practising cosmetic scientists and dermatologists, as well as specialists in more diverse disciplines that are developing new products which contact the skin, hair, nails or mucous membranes. The aim of the Journal is to present current scientific research, both pure and applied, in: cosmetics, toiletries, perfumery and allied fields. Areas that are of particular interest include: studies in skin physiology and interactions with cosmetic ingredients, innovation in claim substantiation methods (in silico, in vitro, ex vivo, in vivo), human and in vitro safety testing of cosmetic ingredients and products, physical chemistry and technology of emulsion and dispersed systems, theory and application of surfactants, new developments in olfactive research, aerosol technology and selected aspects of analytical chemistry.
期刊最新文献
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