Dermcidin (DCD)

Dermcidin (DCD) is a secreted human protein, predominantly expressed in eccrine sweat glands, and processed into multiple bioactive peptides[5][6]. Its primary role is as an anionic antimicrobial peptide (AMP) that directly disrupts bacterial and fungal cells by forming Zn²⁺-stabilized oligomeric channels in microbial membranes; these ion channels inhibit vital cellular functions resulting in pathogen death[1][3][7]. DCD-derived peptides also play key roles in human biology, such as promoting neural cell survival under stress (N-terminal domain) and inducing muscle proteolysis linked to cancer cachexia (PIF domain)[5][6]. Furthermore, DCD has been investigated as a putative oncogene for its ability to enhance tumor cell survival and proliferation, likely via regulation of pro-growth signaling networks such as VEGFB[2][3]. DCD and its processed peptides are stable in sweat and constitute part of the body’s constitutive, non-inducible innate skin defense system; reduced levels are linked to higher risk of skin infections such as atopic dermatitis and tinea pedis[1][3]. There are promising therapeutic opportunities and challenges for targeting DCD or harnessing its activity, but no approved interacting drugs at present[4].

Other names

Proteolysis-inducing factorSurvival-promoting peptideDCD-1AIDDDSEPPIFHCAPPreproteolysinDiffusible survival/evasion peptide

Antimicrobial: Oligomerizes (Zn²⁺-dependent), inserts into microbial membranes, forms ion channels, disrupts ionic homeostasis, inhibits DNA/RNA/protein synthesis, induces cell death. Survival promotion: N-terminal peptide protects neural cells from oxidative stress. Cachexia: PIF domain induces muscle proteolysis in cancer. Oncogenic: Putative, via upregulation of proliferative pathways in tumor cells (e.g., VEGFB hub).