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Epidermal skin proteins are a diverse group of structural and functional molecules essential for maintaining the skin's integrity and barrier function. Key members include keratins, which provide mechanical resilience; filaggrin, which aggregates keratin filaments and contributes to the natural moisturizing factor; and cornified envelope proteins like loricrin and involucrin [1][2]. These proteins are synthesized during the terminal differentiation of keratinocytes as they migrate from the basal layer to the stratum corneum. Dysregulation or genetic mutations in these proteins are central to the pathogenesis of various dermatological conditions, such as atopic dermatitis and ichthyosis [2][4]. Therapeutic strategies often focus on modulating the expression of these proteins or compensating for their deficiency to restore the skin barrier. For instance, retinoids and vitamin D analogs are used to regulate keratinocyte proliferation and differentiation, thereby influencing the protein profile of the epidermis [3]. Additionally, topical agents like urea and alpha-hydroxy acids interact with these proteins to improve skin hydration and facilitate the removal of excess scales in hyperkeratotic conditions [1].
Therapeutic agents typically function by regulating the transcription of genes encoding these proteins via nuclear receptors, promoting enzymatic cross-linking of the cornified envelope, or chemically disrupting protein-protein interactions to facilitate desquamation [1][3].
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