Alkaline ceramidase 1 (ACER1)

Alkaline ceramidase 1 (ACER1) is an integral membrane enzyme predominantly expressed in the skin, localized to the endoplasmic reticulum of epidermal keratinocytes[1]. It catalyzes the hydrolysis of ceramides with an unsaturated, very long acyl chain at an optimal alkaline pH (around 8), producing sphingosine, which is further converted to sphingosine-1-phosphate. Through this activity, ACER1 regulates cellular differentiation, growth arrest, and skin homeostasis. While it has not been directly linked to a specific human disease, its essential role in the skin and energy regulation suggests it could be implicated in skin pathologies or metabolic disorders when dysregulated[1][2]. Key details: Enzyme Commission number: 3.5.1.23[1]. Localization: Endoplasmic reticulum in keratinocytes[1]. Expression: Highly expressed in epidermal keratinocytes of the skin; not in dermal fibroblasts[1]. Functional significance: Essential for skin cell differentiation and whole-body energy balance[1]. No evidence was found for direct pharmacological modulation or established clinical biomarker use specific to ACER1.

Other names

N-acylsphingosine amidohydrolase 3ACER1

Not applicable (no known drugs directly targeting ACER1; mechanistic pathway is hydrolysis of ceramide to sphingosine)