PLOD1
PLOD1 (procollagen-lysine,2-oxoglutarate 5-dioxygenase 1, also known as LH1, LLH and PLOD) is an endoplasmic reticulum enzyme that hydroxylates lysine residues in collagen. These hydroxylysines support carbohydrate attachment and the stability of intermolecular collagen cross-links. Browse Assay Genie's current range of PLOD1 research reagents below, or read on for the biology behind the target.
PLOD1 is a lysyl hydroxylase that forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. It acts as part of a complex composed of PLOD1, P3H3 and P3H4, which catalyses hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linking of collagen fibrils. The resulting hydroxylysines serve as attachment sites for carbohydrate units and are essential for the stability of intermolecular collagen cross-links. The enzyme uses iron and ascorbate as cofactors.
The PLOD1 protein is a membrane-bound homodimer localised to the cisternae of the endoplasmic reticulum, and UniProt places it at the rough endoplasmic reticulum membrane. It belongs to the procollagen-lysine,2-oxoglutarate 5-dioxygenase family, which also includes PLOD2 and PLOD3. Two transcript variants of the PLOD1 gene encode different isoforms.
The gene's previous HGNC name, procollagen-lysine 1, 2-oxoglutarate 5-dioxygenase (lysine hydroxylase, Ehlers-Danlos syndrome type VI), reflects its disease association: some patients with Ehlers-Danlos syndrome type VI have deficiencies in lysyl hydroxylase activity. This makes PLOD1 a point of interest for researchers studying collagen biosynthesis, cross-linking and connective tissue disorders. Mouse and rat orthologs, both named Plod1, are also recognised.
PLOD1 hydroxylates lysine in collagen alpha chains, a step required for normal assembly of collagen fibrils.
Hydroxylysines formed by PLOD1 are essential for the stability of intermolecular collagen cross-links.
Deficient lysyl hydroxylase activity is found in some patients with Ehlers-Danlos syndrome type VI, linking PLOD1 to connective tissue disease.
PLOD1 is a membrane-bound homodimer of the ER, working with P3H3 and P3H4 in a collagen-modifying complex.
PLOD1 catalyses hydroxylation of lysine residues in -Xaa-Lys-Gly- sequences of collagens, using iron and ascorbate as cofactors. It acts in a complex with P3H3 and P3H4. The hydroxylysines formed are carbohydrate attachment sites and are essential for stable intermolecular collagen cross-links.
PLOD1 is also known as LH1, LLH and PLOD, and as lysyl hydroxylase 1. Its earlier HGNC name referred to lysine hydroxylase and Ehlers-Danlos syndrome type VI. Two transcript variants encoding different isoforms have been described for the gene.
Some patients with Ehlers-Danlos syndrome type VI have deficiencies in lysyl hydroxylase activity, which is the basis for the disease link. Orthologs named Plod1 exist in mouse and rat; check the datasheet of any product for its validated reactivity.
Other members of the procollagen-lysine,2-oxoglutarate 5-dioxygenase family involved in collagen modification.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q02809; product specifications from Assay Genie datasheets.