Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links.
Involvement in disease
Defects in PLOD1 are the cause of Ehlers-Danlos syndrome type 6 (EDS6) [MIM:225400]. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS6 is characterized by the presence of ocular complications, particularly retinal detachment. Defects in PLOD1 are the cause of Nevo syndrome (NEVOS) [MIM:601451]. This is a rare, autosomal recessive disorder characterized by increased perinatal length, kyphosis, muscular hypotonia, and joint laxity. Nevo syndrome and EDS-VI have similar clinical phenotypes. Some authors consider that both syndromes are the same clinical entity.
Immunohistochemical analysis of formalin-fixed, paraffin-embedded Human heart tissue labeling PLOD1 with ab171140 at 1/10 diution, followed by peroxidase conjugation of the secondary antibody and DAB staining.
Flow cytometric analysis of U251 cells labeling PLOD1 with ab171140 at 1/10 dilution (right histogram) compared to negative control cells (left histogram). FITC-conjugated goat-anti-rabbit secondary antibodies were used for the analysis.