PLOD3 (procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3), also known as lysyl hydroxylase 3 (LH3), is an enzyme encoded by the PLOD3 gene in humans. It belongs to the PLOD family of enzymes that catalyze the hydroxylation of lysine residues in collagen and other proteins, a critical post-translational modification required for the stability and cross-linking of collagen fibrils. Unlike other PLOD family members (PLOD1 and PLOD2), PLOD3 exhibits unique bifunctional activity: it not only hydroxylates lysine but also glucosylates galactosyl-hydroxylysine residues in collagen, contributing to tissue integrity and extracellular matrix (ECM) organization.
PLOD3 is localized in the endoplasmic reticulum and plays a vital role in collagen biosynthesis, particularly in basement membranes and connective tissues. Dysregulation of PLOD3 has been linked to various pathologies, including cancer, fibrosis, and skeletal disorders. Overexpression of PLOD3 is observed in multiple cancers, where it promotes tumor progression, metastasis, and chemoresistance by enhancing collagen remodeling and ECM stiffness. Conversely, PLOD3 mutations or deficiencies are associated with connective tissue abnormalities and impaired wound healing.
Antibodies targeting PLOD3 are essential tools for studying its expression, localization, and function in both physiological and disease contexts. They are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to investigate PLOD3's role in ECM dynamics, cellular signaling, and therapeutic targeting. Research on PLOD3 antibodies continues to advance insights into tissue fibrosis, cancer biology, and regenerative medicine.