Functional diversity of lysyl hydroxylase 2 in collagen synthesis of human dermal fibroblasts

• Published in: Experimental cell research Vol. 312; no. 18; pp. 3485 - 3494
• Main Authors: Wu, Jiang, Reinhardt, Dieter P., Batmunkh, Chimedtseren, Lindenmaier, Werner, Far, Rosel Kretschmer-Kazemi, Notbohm, Holger, Hunzelmann, Nico, Brinckmann, Jürgen
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.11.2006; Elsevier BV
• Subjects: Adenoviridae - genetics; Adenoviridae - metabolism; Animals; Cells, Cultured; Cellular biology; Collagen; Collagen Type I - biosynthesis; Collagen Type I - genetics; Dermis - cytology; Enzymes; Fibrillin-1; Fibrillins; Fibroblasts - cytology; Fibroblasts - physiology; Fibronectins - genetics; Fibronectins - metabolism; Fibrosis; Fibrosis - metabolism; Gene expression; Genetic Vectors - genetics; Genetic Vectors - metabolism; Human subjects; Humans; Lysyl hydroxylase; Microfilament Proteins - genetics; Microfilament Proteins - metabolism; Molecular biology; Post-translational modification; Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase - genetics; Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase - metabolism; Procollagen-Proline Dioxygenase - genetics; Procollagen-Proline Dioxygenase - metabolism; Proto-Oncogene Proteins c-myc - genetics; Proto-Oncogene Proteins c-myc - metabolism; RNA, Messenger - metabolism; lys ald; Post-translational modification; HLNL; Lysyl hydroxylase; DHLNL; ER; hyl ald; pNP; LOX; Collagen; Fibrosis; LH; pCP

The pathogenesis of fibrosis, especially involving post-translational modifications of collagen, is poorly understood. Lysyl hydroxylase 2 (long) (LH2 (long)) is thought to play a pivotal role in fibrosis by directing the collagen cross-link pattern. Here we show that LH2 (long) exerts a bimodal fun...