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Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3 (PLOD3, also known as LH3) is a multifunctional membrane-bound enzyme in the rough endoplasmic reticulum. It catalyzes critical steps in collagen biosynthesis, including the hydroxylation and subsequent glycosylation (galactosylation and glucosylation) of specific lysine residues in procollagen. These post-translational modifications are essential for proper collagen cross-linking, extracellular matrix organization, and the mechanical stability of connective tissues[1][3][4]. PLOD3 functions as part of the KOGG complex (in combination with galactosyltransferase ColGalT1), and defects in its activity result in a spectrum of connective tissue disorders and have been implicated in fibrosis-related diseases and cancer. Elevated expression of PLOD3 is associated with poor prognosis, radioresistance, and chemoresistance in lung cancer, making it both a disease marker and a pre-clinical therapeutic target[2][3][4].
Enzyme inhibition (siRNA-mediated suppression reduces tumor chemoresistance and radioresistance by promoting apoptosis in cancer models[2])
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