Desmocollin-1 (DSC1)

Desmocollin-1 (DSC1) is a calcium-dependent, transmembrane glycoprotein belonging to the cadherin superfamily, specifically the desmocollin subfamily[3][2][1]. It is a major constituent of desmosomes—specialized cell-cell junctions found primarily in epithelial tissues—where it mediates strong intercellular adhesion by forming adhesive heterodimers with desmogleins[4][1]. DSC1 is especially prominent in terminally differentiating keratinocytes of the upper epidermis and hair follicles, playing key roles in maintaining skin integrity and barrier function[1][3]. DSC1 is implicated in disease processes including the pathogenesis of autoimmune blistering disorders like IgA pemphigus (autoantibody target) and has been linked to metastatic progression in certain breast cancer subtypes: overexpression promotes tumor cell migration and invasion, and its downregulation reduces pro-metastatic pathways. Modulation of DSC1 (e.g., by parthenolide) can disrupt cell adhesion and related molecular networks, underlining its therapeutic target potential and associated safety considerations[2][3][1].

Other names

Desmocollin-1DSC1CDHF1DG2/DG3Cadherin family member 1Desmosomal glycoprotein 2/3desmocollin-1cadherin family member 1desmosomal glycoprotein 2/3

Modulation of DSC1 expression or protein-protein interactions affecting cell adhesion and signaling (parthenolide decreases DSC1 level and disrupts associated molecular pathways)