A disintegrin and metallopeptidase domain 30 (ADAM30)

A disintegrin and metallopeptidase domain 30 (ADAM30) is a membrane-anchored zinc-dependent metalloprotease belonging to the ADAM (a disintegrin and metalloproteinase) family[1][3][5]. These enzymes are characterized by a large multidomain structure involved in cell adhesion, proteolysis, and signaling pathways. ADAM30 is primarily expressed in the testis and exhibits metallopeptidase activity, catalyzing proteolytic events such as the activation of lysosomal cathepsin D, which influences the degradation of amyloid precursor protein[1]. ADAM30 and its family members regulate critical processes including cell-cell and cell-matrix interactions, development, neurogenesis, and reproductive biology[1][3][5]. Dysregulation in ADAM family activity is implicated in diseases such as cancer, chronic inflammatory states, and neurodegenerative disorders, although direct disease associations for ADAM30 remain limited. There are currently no drugs or established biomarkers specific to ADAM30, and its detailed physiological and pathological roles are still being elucidated[1][3][5].

Other names

ADAM metallopeptidase domain 30Disintegrin and metalloproteinase domain-containing protein 30ADAM30UNQ2509/PRO5997svph4a disintegrin and metalloproteinase domain 30

General for ADAM family: Ectodomain shedding (proteolytic cleavage of membrane proteins, regulating signaling and cell surface molecule activity) For ADAM30 specifically: Activation of lysosomal cathepsin D, leading to degradation of amyloid precursor protein (potentially relevant to Alzheimer’s)