对 "软骨素/硫酸软骨素蛋白聚糖,脱毛素,显示出对脱模小体的亲和力 "的更正

IF 2.7 4区 医学 Q2 DERMATOLOGY
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引用次数: 0

摘要

Laperdrix C, Duhieu S, Haftek M.软骨素/硫酸软骨素蛋白多糖脱毛素与脱毛小体的亲和力。在发表的文章中,英文摘要有误。英文摘要应为:Objective:脱落小体是角质细胞间最显著的连接点。表皮等分层上皮的正确屏障功能取决于它们的表达。在表皮分化过程中,脱丝体的分子组成发生变化,其物理和化学特性也随之变化。角质层表面角质细胞的脱屑取决于内源性酶对脱屑体的有序降解。这一过程可能受到糖基化分子的调控。我们重点研究了具有 "糖 "特征的潜在相关分子的检测和特征描述:方法:我们使用一种独创的单克隆抗体和生化方法,部分鉴定了一种完全属于软骨素/硫酸软骨素类型的蛋白多糖,这种蛋白多糖分泌到角质细胞间隙,并结合到脱丝体的细胞外部分,其数量与细胞分化程度成正比,免疫电子显微镜可对其进行观察:结果:我们将这种抗原命名为脱毛素,它所表现出的生物化学和免疫细胞化学特征明显有别于已知的脱模素。与迄今为止描述的属于硫酸肝素家族的表皮蛋白聚糖不同,脱毛素显示出软骨素/硫酸软骨素糖胺聚糖链。在有活力的表皮上层脱毛小体的细胞外 "核心 "和角质层最下层的角质小体中都能检测到脱毛素:结论:在角质细胞成熟的晚期阶段,蛋白聚糖广泛整合到脱模小体的细胞外部分,这可能具有重要的功能意义。鉴于其生化特征、在表皮中的表达模式及其脱模小体定位,脱毛素可能成为调节脱模小体加工、表皮内聚力和形成功能性表皮屏障的关键因素。我们对此错误深表歉意。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Correction to “Chondroitin/dermatan sulphate proteoglycan, desmosealin, showing affinity to desmosomes”

Laperdrix C, Duhieu S, Haftek M. Chondroitin/dermatan sulphate proteoglycan, desmosealin, showing affinity to desmosomes. Int J Cosmet Sci. 2024;46:494–505.

In the published article, the English abstract was incorrect. It should have been:

Objective: Desmosomes are the most prominent interkeratinocyte junctions. The correct barrier function of stratified epithelia such as epidermis depends on their expression. During epidermal differentiation, the molecular composition of desmosomes evolves and so do their physical and chemical properties. Desquamation of corneocytes at the surface of the stratum corneum depends on an orderly degradation of desmosomes by endogenous enzymes. This process may be regulated by glycosylated molecules. We focused on the detection and characterization of potentially implicated players bearing ‘sugar’ characteristics.

Methods: Using an original monoclonal antibody and biochemical methods, we partially characterized a proteoglycan of the exclusively chondroitin/dermatan sulphate type, secreted into the interkeratinocyte spaces, that is incorporated into the extracellular parts of desmosomes in quantities proportional to the degree of cell differentiation, as visualized with immuno-electron microscopy.

Results: This antigen, that we named desmosealin, displays biochemical and immunocytochemical characteristics that clearly differentiate it from known desmosomal elements. Unlike so far described epidermal proteoglycans, which belong to the heparan sulphate family, desmosealin displays chondroitin/dermatan sulphate glycosaminoglycan chains. It can be detected within the extracellular ‘cores’ of desmosomes in the upper viable epidermal layers and in corneodesmosomes from the lowermost part of the stratum corneum.

Conclusion: Extensive integration of proteoglycans into the extracellular parts of desmosomes at the late stages of keratinocyte maturation is likely of functional importance. Given its biochemical profile, its pattern of expression in the epidermis and its desmosomal localization, desmosealin may emerge as a key element in the regulation of desmosome processing, epidermal cohesion and formation of a functional epidermal barrier.

The online version has been corrected. We apologize for this error.

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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.
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