Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a novel mechanism for matrix remodeling

• DOI: 10.1002/jcp.20596
• Publication Date: 2006-01-30T23:16:55Z
• Authors: Antti M. Salo; Chunguang Wang; Laura Sipilä; Raija Sormunen; Miia Vapola; Päivi Kervinen; Heli Ruotsalainen; Jari Heikkinen; Raili Myllylä
• Keywords: Hydroxylysine

Abstract Lysyl hydroxylase 3 (LH3), the multifunctional enzyme associated with collagen biosynthesis that possesses lysyl and glycosyltransferase activities, has been characterized in extracellular space this study. Lysine modifications are known to occur endoplasmic reticulum (ER) prior triple‐helix formation, but study we show LH3 is also present active space. Studies vitro cultured cells indicate LH3, addition being an ER resident, secreted from found both medium on cell surface collagens or other proteins collagenous sequences. Furthermore, vivo, serum. protein levels correlate galactosylhydroxylysine glucosyltransferase (GGT) activity of mouse tissues. This, together data, indicates responsible for GGT tissues assays can be used quantify vivo located two compartments, space, partitioning varies tissue type. In kidney mainly intracellularly, whereas liver it solely The localization ability modify residues their native, nondenaturated conformation reveals a new dynamic matrix remodeling, suggesting novel mechanism adjusting amount hydroxylysine hydroxylysine‐linked carbohydrates proteins. © 2006 Wiley‐Liss, Inc.