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Houfu Guo

As seen in: Wiley Online Library, The Journal of Clinical Investigation, The Journal of Biological Chemistry
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Articles by Houfu Guo

Structure of an Fe2+‐binding‐deficient mimiviral collagen lysyl hydroxylase

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By Tingfei Chen, Christoph Buhlheller, Houfu Guo
| Wiley Online Library Verified
Collagen lysyl hydroxylases catalyze the hydroxylation of collagen lysine residues during collagen synthesis in animals and mimiviruses. Lysyl hydroxylation is crucial for collagen fibrogenesis and function. We previously demonstrated that recombinant mimiviral and human collagen lysyl hydroxylases, isolated from bacterial and mammalian cells, have Fe2+ in their active sites, suggesting that lysyl hydroxylases have a high affinity for Fe2+.
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Lysyl hydroxylase 2 glucosylates collagen VI to drive lung cancer progression

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By Shike Wang, Houfu Guo, Masahiko Terajima, Reo Fukushima
| The Journal of Clinical Investigation
Abstract Lysyl hydroxylase 2 (LH2) is highly expressed in multiple tumor types and accelerates disease progression by hydroxylating lysine residues on fibrillar collagen telopeptides to generate stable collagen cross links in tumor stroma. Here, we show that a galactosylhydroxylysyl glucosyltransferase (GGT) domain on LH2-modified type-VI collagen (Col6) to promote lung adenocarcinoma (LUAD) growth and metastasis.
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Lysyl Hydroxylase 2 Is Secreted by Tumor Cells and Can Modify Collagen in the Extracellular Space

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By Yulong Chen, Houfu Guo, Masahiko Terajima, Priyam Banerjee
| The Journal of Biological Chemistry Verified
Lysyl hydroxylase 2 (LH2) catalyzes the hydroxylation of lysine residues in the telopeptides of fibrillar collagens, which leads to the formation of stable collagen cross-links. Recently we reported that LH2 enhances the metastatic propensity of lung cancer by increasing the amount of stable hydroxylysine aldehyde-derived collagen cross-links (HLCCs), which generate a stiffer tumor stroma (Chen, Y., et al. (2015) J. Clin. Invest. 125, 125, 1147–1162).
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Lysyl Hydroxylase 2 Is Secreted By Tumor Cells and Can Modify Collagen in the Extracellular Space

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By Yulong Chen, Masahiko Terajima, Houfu Guo, Priyam Banerjee
| The Journal of Biological Chemistry Verified
Author contributions: Y.C., H-F.G., and M.T. conducted the experiments, including generating stable cell lines, purifying recombinant proteins, performing in vitro hydroxylase activity assays, performing biochemical and mass spectrometric analyses, and analyzing and interpreting data. A.M., H.K., and S.H. conducted and interpreted the stable isotope labeling of amino acids in cell culture analyses. A.R.B. conducted the Immunogold labeling and transmission electron microscopy experiment.
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