Lysyl hydroxylase 2 is a specific telopeptide hydroxylase, while all three isoenzymes hydroxylate collagenous sequences
- 16 January 2007
- journal article
- research article
- Published by Elsevier in Matrix Biology
- Vol. 26 (5) , 396-403
- https://doi.org/10.1016/j.matbio.2007.01.002
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- Interleukin 4 and prolonged hypoxia induce a higher gene expression of lysyl hydroxylase 2 and an altered cross-link pattern: Important pathogenetic steps in early and late stage of systemic scleroderma?Matrix Biology, 2005
- Lysyl oxidase: Properties, specificity, and biological roles inside and outside of the cellJournal of Cellular Biochemistry, 2002
- The kyphoscoliotic type of Ehlers–Danlos syndrome (type VI): differential effects on the hydroxylation of lysine in collagens I and II revealed by analysis of cross-linked telopeptides from urineMolecular Genetics and Metabolism, 2002
- Different Pattern of Collagen Cross-Links in Two Sclerotic Skin Diseases: Lipodermatosclerosis and Circumscribed SclerodermaJournal of Investigative Dermatology, 2001
- Lysyl Hydroxylase 3 Is a Multifunctional Protein Possessing Collagen Glucosyltransferase ActivityJournal of Biological Chemistry, 2000
- Defective collagen crosslinking in bone, but not in ligament or cartilage, in Bruck syndrome: Indications for a bone-specific telopeptide lysyl hydroxylase on chromosome 17Proceedings of the National Academy of Sciences, 1999
- Molecular Site Specificity of Pyridinoline and Pyrrole Cross-links in Type I Collagen of Human BoneJournal of Biological Chemistry, 1996
- Structure and Expression of the Human Lysyl Hydroxylase Gene (PLOD): Introns 9 and 16 Contain Alu Sequences at the Sites of Recombination in Ehlers-Danlos Syndrome Type VI PatientsGenomics, 1994
- Cloning of human lysyl hydroxylase: Complete cDNA-derived amino acid sequence and assignment of the gene (PLOD) to chromosome 1p36.3→p36.2Genomics, 1992
- [7] Collagen cross-linking amino acidsPublished by Elsevier ,1987