The HPDL (4-hydroxyphenylpyruvate dioxygenase-like) protein is a recently characterized enzyme encoded by the *HPDL* gene, belonging to the Fe(II)/2-oxoglutarate-dependent dioxygenase family. Although its exact biological role remains under investigation, HPDL shares structural homology with 4-hydroxyphenylpyruvate dioxygenase (HPD), a key enzyme in tyrosine catabolism. Emerging studies suggest HPDL may influence cellular processes such as lipid metabolism, redox homeostasis, and mitochondrial function, though its substrate specificity and catalytic activity are not fully defined.
Interest in HPDL surged after its genetic link to early-onset neurodegenerative disorders. In 2020. biallelic *HPDL* mutations were identified as causative for a spectrum of neurological conditions, including progressive spastic paraplegia, encephalopathy, and Leigh-like syndrome. These mutations impair HPDL function, leading to mitochondrial dysfunction and neuronal degeneration, though the precise molecular mechanisms remain unclear.
HPDL antibodies are critical tools for studying the protein's expression, localization, and role in disease. They enable detection via Western blot, immunohistochemistry, and immunofluorescence, aiding in tissue-specific expression profiling and subcellular localization studies (e.g., mitochondrial vs. cytoplasmic distribution). Researchers also utilize these antibodies to explore HPDL interactions and regulatory pathways in disease models. As therapeutic strategies targeting metabolic enzymes advance, HPDL antibodies may further contribute to biomarker discovery or therapeutic development for related neurogenetic disorders. Current research continues to unravel HPDL's physiological and pathological significance, positioning it as a compelling target in neurology and metabolism.