The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Identification of PLOD2 as Telopeptide Lysyl Hydroxylase, an Important Enzyme in Fibrosis
Open accessAbstract
The hallmark of fibrotic processes is an excessive accumulation of collagen. The deposited collagen shows an increase in pyridinoline cross-links, which are derived from hydroxylated lysine residues within the telopeptides. This change in cross-linking is related to irreversible accumulation of collagen in fibrotic tissues. The increase in pyridinoline cross-links is likely to be the result of increased activity of the enzyme responsible for the hydroxylation of the telopeptides (telopeptide lysyl hydroxylase, or TLH). Although the existence of TLH has been postulated, the gene encoding TLH has not been identified. By analyzing the genetic defect of Bruck syndrome, which is characterized by a pyridinoline deficiency in bone collagen, we found two missense mutations in exon 17 of PLOD2, thereby identifying PLOD2 as a putative TLH gene. Subsequently, we investigated fibroblasts derived from fibrotic skin of systemic sclerosis (SSc) patients and found that PLOD2 mRNA is highly increased indeed. Furthermore, increased pyridinoline cross-link levels were found in the matrix deposited by SSc fibroblasts, demonstrating a clear link between mRNA levels of the putative TLH gene (PLOD2) and the hydroxylation of lysine residues within the telopeptides. These data underscore the significance of PLOD2 in fibrotic processes.
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Cites
CROSS-LINKING IN COLLAGEN AND ELASTIN
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Quantitation of hydroxypyridinium crosslinks in collagen by high-performance liquid chromatography
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LeRoy, E. C. (1974) · Journal of Clinical Investigation · doi:10.1172/jci107827 · Cited by 544
Enzymatic and nonenzymatic cross‐linking of collagen and elastin
Reiser, K., McCormick, R. J., & Rucker, R. B. (1992) · The FASEB Journal · doi:10.1096/fasebj.6.7.1348714 · Cited by 450
Characterization of the collagen of human hypertrophic and normal scars
Bailey, A. J., Bazin, S., Sims, T. J., Le Lous, M., Nicoletis, C., & Delaunay, A. (1975) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(75)90106-3 · Cited by 289
Bank, R. A., Robins, S. P., Wijmenga, C., Breslau‐Siderius, L., Bardoel, A. F. J., van der Sluijs, H. A., Pruijs, H. E. H., & TeKoppele, J. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.3.1054 · Cited by 200
Self-citationYeowell, H. N., & Walker, L. C. (2000) · Molecular Genetics and Metabolism · doi:10.1006/mgme.2000.3076 · Cited by 175
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Cited by
Recent Developments in Myofibroblast Biology
Hinz, B., Phan, S. H., Thannickal, V. J., Prunotto, M., Desmoulière, A., Varga, J., De Wever, O., Mareel, M., & Gabbiani, G. (2012) · The American Journal of Pathology · doi:10.1016/j.ajpath.2012.02.004 · Cited by 1,193
Marini, J. C., Forlino, A., Bächinger, H. P., Bishop, N. J., Byers, P. H., Paepe, A. D., Fassier, F., Fratzl-Zelman, N., Kozloff, K. M., Krakow, D., et al. (2017) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2017.52 · Cited by 842
Kuo, D. S., Labelle-Dumais, C., & Gould, D. B. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds346 · Cited by 320
Procollagen lysyl hydroxylase 2 is essential for hypoxia-induced breast cancer metastasis
Gilkes, D. M., Bajpai, S., Wong, C. C., Chaturvedi, P., Hubbi, M. E., Wirtz, D., & Semenza, G. L. (2013) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-12-0629 · Cited by 252
RetractedMolecular insights into prolyl and lysyl hydroxylation of fibrillar collagens in health and disease
Gjaltema, R. A. F., & Bank, R. A. (2017) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2016.1269716 · Cited by 175
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Metadata
- Authors
- van der Slot, A. J., Zuurmond, A.-M., Bardoel, A. F. J., Wijmenga, C., Pruijs, H. E. H., Sillence, D. O., Brinckmann, J., Abraham, D. J., Black, C. M., Verzijl, N., DeGroot, J., Hanemaaijer, R., TeKoppele, J. M., Huizinga, T. W. J., & Bank, R. A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-10
- Volume
- 278
- Issue
- 42
- Pages
- 40967-40972
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2147016321
- Cited by
- 409
- References
- 23
- FWCI
- 7.53
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- van der Slot, A. J., Zuurmond, A.-M., Bardoel, A. F. J., Wijmenga, C., Pruijs, H. E. H., Sillence, D. O., Brinckmann, J., Abraham, D. J., Black, C. M., Verzijl, N., DeGroot, J., Hanemaaijer, R., TeKoppele, J. M., Huizinga, T. W. J., & Bank, R. A. (2003). Identification of PLOD2 as Telopeptide Lysyl Hydroxylase, an Important Enzyme in Fibrosis. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m307380200
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.