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PLOD3  -  procollagen-lysine, 2-oxoglutarate 5...

Homo sapiens

Synonyms: LH3, Lysyl hydroxylase 3, Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3
 
 
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Disease relevance of PLOD3

 

High impact information on PLOD3

  • We show that this unique role depends critically on the LH3 glycosyltransferase domain, and provide compelling evidence that diwanka (lh3) acts through myotomal type XVIII collagen, a ligand for neural-receptor protein tyrosine phosphatases that guide motor axons [4].
  • The overall amino acid sequence identity between the processed human lysyl hydroxylase 3 and 1 polypeptides is 59%, and that between the processed lysyl hydroxylase 3 and 2 polypeptides is 57%, whereas the identity to the processed Caenorhabditis elegans polypeptide is only 45% [1].
  • The data also reveal a DXD-like motif in LH3 characteristic of many glycosyltransferases and the mutagenesis of aspartates of this motif eliminated the GGT activity [5].
  • Gene expression of LH3 is highly regulated in adult human tissues [6].
  • The gene for LH3 (PLOD3) has been assigned to human chromosome 7q36 and rat chromosome 12 [6].
 

Biological context of PLOD3

 

Anatomical context of PLOD3

  • Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes [9].
  • LH3 in vivo is located in two compartments, in the ER and in the extracellular space, and the partitioning varies with tissue type [10].
  • Studies with in vitro cultured cells indicate that LH3, in addition to being an ER resident, is secreted from the cells and is found both in the medium and on the cell surface associated with collagens or other proteins with collagenous sequences [10].
  • Lysine modifications are known to occur in the endoplasmic reticulum (ER) prior to collagen triple-helix formation, but in this study we show that LH3 is also present and active in the extracellular space [10].
  • To define the biochemical defect, we have examined cultured fibroblasts from four EDS VIB patients for changes in the levels of the mRNAs for LH1, LH2, and LH3, collagen cross-linking patterns, and the extent of lysine hydroxylation of type I collagen alpha chains [11].
 

Associations of PLOD3 with chemical compounds

 

Other interactions of PLOD3

  • Large variations were found in mRNA expression of LH1 and LH2 but not LH3 [12].
  • In addition, no consistent increase in the mRNA expression levels of LH1, LH3 and LOX could be detected, suggesting that LH2b is responsible for the overhydroxylation of the collagen telopeptides and the concomitant formation of pyridinolines as found in the collagen matrix deposited in long-term cultures by the same fibrotic cells [13].
 

Analytical, diagnostic and therapeutic context of PLOD3

References

  1. Cloning and characterization of a third human lysyl hydroxylase isoform. Passoja, K., Rautavuoma, K., Ala-Kokko, L., Kosonen, T., Kivirikko, K.I. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  2. Probing the electronic structure and conformational flexibility of individual light-harvesting 3 complexes by optical single-molecule spectroscopy. Ketelaars, M., Segura, J.M., Oellerich, S., de Ruijter, W.P., Magis, G., Aartsma, T.J., Matsushita, M., Schmidt, J., Cogdell, R.J., Köhler, J. The journal of physical chemistry. B, Condensed matter, materials, surfaces, interfaces & biophysical. (2006) [Pubmed]
  3. Graft-versus-host disease associated T helper cell responses specific for minor histocompatibility antigens are mainly restricted by HLA-DR molecules. van Els, C.A., Zantvoort, E., Jacobs, N., Bakker, A., van Rood, J.J., Goulmy, E. Bone Marrow Transplant. (1990) [Pubmed]
  4. The myotomal diwanka (lh3) glycosyltransferase and type XVIII collagen are critical for motor growth cone migration. Schneider, V.A., Granato, M. Neuron (2006) [Pubmed]
  5. Identification of amino acids important for the catalytic activity of the collagen glucosyltransferase associated with the multifunctional lysyl hydroxylase 3 (LH3). Wang, C., Risteli, M., Heikkinen, J., Hussa, A.K., Uitto, L., Myllyla, R. J. Biol. Chem. (2002) [Pubmed]
  6. Primary structure, tissue distribution, and chromosomal localization of a novel isoform of lysyl hydroxylase (lysyl hydroxylase 3). Valtavaara, M., Szpirer, C., Szpirer, J., Myllylä, R. J. Biol. Chem. (1998) [Pubmed]
  7. The third activity for lysyl hydroxylase 3: galactosylation of hydroxylysyl residues in collagens in vitro. Wang, C., Luosujärvi, H., Heikkinen, J., Risteli, M., Uitto, L., Myllylä, R. Matrix Biol. (2002) [Pubmed]
  8. Complete exon-intron organization of the gene for human lysyl hydroxylase 3 (LH3). Rautavuoma, K., Passoja, K., Helaakoski, T., Kivirikko, K.I. Matrix Biol. (2000) [Pubmed]
  9. Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes. Ruotsalainen, H., Sipilä, L., Vapola, M., Sormunen, R., Salo, A.M., Uitto, L., Mercer, D.K., Robins, S.P., Risteli, M., Aszodi, A., Fässler, R., Myllylä, R. J. Cell. Sci. (2006) [Pubmed]
  10. Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a novel mechanism for matrix remodeling. Salo, A.M., Wang, C., Sipilä, L., Sormunen, R., Vapola, M., Kervinen, P., Ruotsalainen, H., Heikkinen, J., Myllylä, R. J. Cell. Physiol. (2006) [Pubmed]
  11. Heterogeneous basis of the type VIB form of Ehlers-Danlos syndrome (EDS VIB) that is unrelated to decreased collagen lysyl hydroxylation. Walker, L.C., Overstreet, M.A., Willing, M.C., Marini, J.C., Cabral, W.A., Pals, G., Bristow, J., Atsawasuwan, P., Yamauchi, M., Yeowell, H.N. Am. J. Med. Genet. A (2004) [Pubmed]
  12. Lack of collagen type specificity for lysyl hydroxylase isoforms. Wang, C., Valtavaara, M., Myllylä, R. DNA Cell Biol. (2000) [Pubmed]
  13. Increased formation of pyridinoline cross-links due to higher telopeptide lysyl hydroxylase levels is a general fibrotic phenomenon. van der Slot, A.J., Zuurmond, A.M., van den Bogaerdt, A.J., Ulrich, M.M., Middelkoop, E., Boers, W., Karel Ronday, H., DeGroot, J., Huizinga, T.W., Bank, R.A. Matrix Biol. (2004) [Pubmed]
  14. Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl hydroxylase 3/collagen glucosyltransferase. Ruotsalainen, H., Vanhatupa, S., Tampio, M., Sipilä, L., Valtavaara, M., Myllylä, R. Matrix Biol. (2001) [Pubmed]
 
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