{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPLOD3, also known as lysyl hydroxylase 3 (LH3), is a multifunctional enzyme that plays a critical role in collagen biosynthesis by catalyzing the post‐translational modifications of collagen. It performs lysyl hydroxylation and sequential O‐glycosylation reactions (galactosylation and glucosylation) on collagen lysyl residues, which are essential for the formation of stable collagen cross‐links and proper extracellular matrix organization. These catalytic functions have been demonstrated in studies using recombinant enzymes, which have mapped the activities to distinct domains of the protein."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its intracellular role in the endoplasmic reticulum, PLOD3 is also secreted into the extracellular space and can associate with cell surfaces or be found in serum, suggesting an expanded role in extracellular matrix remodeling. In particular, its regulated trafficking—extending into post-Golgi compartments—ensures proper collagen modification in diverse tissues. These observations underscore its dual compartmental function in both collagen maturation and tissue homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMutations or deficiencies in PLOD3 have been linked to a range of connective tissue disorders. For example, a compound heterozygous mutation affecting both its sugar-transfer and hydroxylase activities leads to a severe multisystem disorder with features overlapping several collagen-related pathologies, emphasizing the enzyme’s indispensable role in collagen modification. Additionally, decreased PLOD3 expression in conditions such as recessive dystrophic epidermolysis bullosa correlates with diminished basement membrane integrity."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of cancer, aberrant PLOD3 expression has emerged as a significant factor influencing tumor progression. In lung cancer, for instance, high PLOD3 levels not only promote radioresistance and chemoresistance via the modulation of apoptotic pathways but also contribute to tumor cell invasion and metastasis through interactions with key signaling molecules such as PKCδ and STAT3. Similar observations in other cancers—including renal cell carcinoma, ovarian cancer, and colorectal cancer—correlate high PLOD3 expression with advanced disease stages, reduced immune cell infiltration, and poor patient prognosis, underscoring its potential as both a diagnostic biomarker and a therapeutic target."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMoreover, PLOD3 appears to participate in additional cellular processes through its interactions and structural features. Its dimerization, mediated by a conserved region, is necessary for lysyl hydroxylase activity, although the glycosyltransferase functions may operate independently. Also, PLOD3 functions as a docking receptor for proteases such as MMP-9 on the surface of fibroblasts, thereby influencing myofibroblast differentiation and the remodeling of the tumor stroma. These multifaceted interactions further illustrate the complex role of PLOD3 in both normal physiology and pathology."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn summary, the collective findings from these diverse studies highlight that PLOD3 is a critical enzyme for collagen post-translational modification with significant implications in connective tissue integrity and extracellular matrix remodeling. Its activities not only underpin normal collagen biosynthesis but also contribute to the progression of various diseases, notably connective tissue disorders and multiple human cancers. As such, PLOD3 represents a promising biomarker and potential therapeutic target for intervening in a wide spectrum of pathological conditions."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}, {"type": "fg_fs", "start_ref": "21", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Kati Rautavuoma, Kati Takaluoma, Kaisa Passoja, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1-3. The 30-kDa N-terminal fragment is not required for lysyl hydroxylase activity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M112077200"}], "href": "https://doi.org/10.1074/jbc.M112077200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11956192"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11956192"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Chunguang Wang, Hanne Luosujärvi, Jari Heikkinen, et al. 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