ArticleJournal of cellular and molecular medicine2009
The glycosyltransferase activities of lysyl hydroxylase 3 (LH3) in the extracellular space are important for cell growth and viability.
Article in Journal of cellular and molecular medicine, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 49 citations in OpenAlex.
- Adhesion to aggression: unravelling sLeClinical & experimental metastasis · 2025Review
- The life cycle of type IV collagen.Matrix biology : journal of the International Society for Matrix Biology · 2025Review
- Integrated Systems Analysis Deciphers Transcriptome and Glycoproteome Links in Alzheimer's Disease.bioRxiv : the preprint server for biology · 2024Article
- Glycosylation Modulates the Structure and Functions of Collagen: A Review.Molecules (Basel, Switzerland) · 2024Review
- Exploring links between 2-oxoglutarate-dependent oxygenases and Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2022Review
- COLGALT1 is a potential biomarker for predicting prognosis and immune responses for kidney renal clear cell carcinoma and its mechanisms of ceRNA networks.European journal of medical research · 2022Article
- Article
- Effect of hydroxylysine-O-glycosylation on the structure of type I collagen molecule: A computational study.Glycobiology · 2020Article
- PLOD3 promotes lung metastasis via regulation of STAT3.Cell death & disease · 2018Article
- Downregulation of Glt25d1 aggravates carbon tetrachloride‑induced acute hepatic injury through activation of the TGF‑β1/Smad2 signaling pathway.Molecular medicine reports · 2018Article
- Article
- Collagen Accumulation in Osteosarcoma Cells lacking GLT25D1 Collagen Galactosyltransferase.The Journal of biological chemistry · 2016Article
- Regulation of post-Golgi LH3 trafficking is essential for collagen homeostasis.Nature communications · 2016Article
- Recruitment of Matrix Metalloproteinase-9 (MMP-9) to the Fibroblast Cell Surface by Lysyl Hydroxylase 3 (LH3) Triggers Transforming Growth Factor-β (TGF-β) Activation and Fibroblast Differentiation.The Journal of biological chemistry · 2015Article
- RNAi-mediated gene silencing of WsSGTL1 in W.somnifera affects growth and glycosylation pattern.Plant signaling & behavior · 2015Article
- Glycosylation modulates melanoma cell α2β1 and α3β1 integrin interactions with type IV collagen.The Journal of biological chemistry · 2014Article
- Lysyl hydroxylase 3 modifies lysine residues to facilitate oligomerization of mannan-binding lectin.PloS one · 2014Article
- Effects of fish collagen peptides on collagen post-translational modifications and mineralization in an osteoblastic cell culture system.Dental materials journal · 2013Article
- Identification of genes with a correlation between copy number and expression in gastric cancer.BMC medical genomics · 2012Article
- The activities of lysyl hydroxylase 3 (LH3) regulate the amount and oligomerization status of adiponectin.PloS one · 2012Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lysyl hydroxylase (LH) isoform 3 is a post-translational enzyme possessing LH, collagen galactosyltransferase (GT) and glucosyltransferase (GGT) activities. We have demonstrated that LH3 is found not only intracellularly, but also on the cell surface and in the extracellular space, suggesting additional functions for LH3. Here we show that the targeted disruption of LH3 by siRNA causes a marked reduction of both glycosyltransferase activities, and the overexpression of LH3 in HT-1080 cells increases hydroxylation of lysyl residues and the subsequent galactosylation and glucosylation of hydroxylysyl residues. These data confirm the multi-functionality of LH3 in cells. Furthermore, treatment of cells in culture medium with a LH3 N-terminal fragment affects the cell behaviour, rapidly leading to arrest of growth and further to lethality if the fragment is glycosyltransferase-deficient, and leading to stimulation of proliferation if the fragment contains LH3 glycosyltransferase activities. The effect is reversible, the cells recovering after removal of the glycosyltransferase-deficient fragment. The findings were confirmed by overexpressing the full-length LH3 in native or mutated forms in the cells. The data indicate that the increase in proliferation depends on the glycosyltransferase activity of LH3. The overexpression of a glycosyltransferase-deficient mutant or targeted disruption of LH3 by siRNA in cells results in abnormal cell morphology followed by cell death. Our data clearly indicate that the deficiency of LH3 glycosyltransferase activities, especially in the extracellular space, causes growth arrest revealing the importance of the glycosyltransferase activities of LH3 for cell growth and viability, and identifying LH3 as a potential target for medical applications, such as cancer therapy.
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