Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 1 (PLOD1)

Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 1 (PLOD1) is an essential enzyme involved in the hydroxylation of lysine residues in collagen and related proteins, a key post-translational modification required for stable intermolecular cross-linking and maturation of connective tissue structures[1][2][3][6]. PLOD1 is a membrane-bound homodimer primarily localized to the endoplasmic reticulum, requiring iron and ascorbate (vitamin C) cofactors for enzymatic activity[3][6]. Deficiency or mutations in PLOD1 result in decreased hydroxylysine formation, unstable collagen cross-linking, and manifestations of genetic diseases such as kyphoscoliotic type Ehlers-Danlos syndrome and familial thoracic aortic aneurysm/dissection[1][2][5]. Emerging research indicates that PLOD1 may participate in the regulation of actin cytoskeletal networks and support cancer cell migration and metastasis, notably in hepatocellular carcinoma[4]. Recent mechanistic insights also suggest minor glycosyltransferase activity by PLOD1, with potential impacts on extracellular matrix composition, though this function is considerably lower compared to homologous enzymes[5]. There are currently no known approved drugs directly targeting PLOD1, and therapeutic modulation carries notable risks due to its fundamental role in tissue stability.

Other names

Lysyl hydroxylase 1LH1Procollagen lysyl hydroxylase 1Lysine hydroxylaseEDS6EDSKCL1LLHLHPLOD