α1,6-Fucosyltransferase (Fut8) is implicated in vulnerability to elastase-induced emphysema in mice and a possible non-invasive predictive marker for disease progression and exacerbations in chronic obstructive pulmonary disease (COPD)

Biochemical and Biophysical Research Communications

Volumn 424, Issue 1, 2012, Pages 112-117

  Kamio, Koichiro ^a   Yoshida, Takayuki ^b   Gao, Congxiao ^c   Ishii, Takeo ^a   Ota, Fumi ^c   Motegi, Takashi ^a   Kobayashi, Satoshi ^c   Fujinawa, Reiko ^c   Ohtsubo, Kazuaki ^c   Kitazume, Shinobu ^c   Angata, Takashi ^c   Azuma, Arata ^a   Gemma, Akihiko ^a   Nishimura, Masaharu ^b   Betsuyaku, Tomoko ^d   Kida, Kozui ^a   Taniguchi, Naoyuki ^c  

^a NIPPON MEDICAL SCHOOL   (Japan)

^b HOKKAIDO UNIVERSITY   (Japan)

^c RIKEN   (Japan)

^d KEIO UNIVERSITY SCHOOL OF MEDICINE   (Japan)

Author keywords

1,6 Fucosyltransferase (Fut8); Biomarker; COPD; Emphysema

Indexed keywords

ALPHA 1,6 FUCOSYLTRANSFERASE; FUCOSYLTRANSFERASE; GELATINASE B; UNCLASSIFIED DRUG;

AIRFLOW; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CHRONIC OBSTRUCTIVE LUNG DISEASE; CONTROLLED STUDY; DISEASE COURSE; DISEASE EXACERBATION; DISEASE SEVERITY; EMPHYSEMA; ENZYME ACTIVITY; FORCED EXPIRATORY VOLUME; HUMAN; MAJOR CLINICAL STUDY; MOUSE; NONHUMAN; PRIORITY JOURNAL; SMOKING;

ANIMALS; BIOLOGICAL MARKERS; DISEASE MODELS, ANIMAL; DISEASE PROGRESSION; FEMALE; FUCOSYLTRANSFERASES; HUMANS; MALE; MATRIX METALLOPROTEINASE 9; MICE; MICE, INBRED C57BL; PANCREATIC ELASTASE; PULMONARY DISEASE, CHRONIC OBSTRUCTIVE; PULMONARY EMPHYSEMA;

MUS; SUS;

EID: 84864088936     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.06.081     Document Type: Article

References (41)

1. Global initiative for chronic obstructive lung disease, Global strategy for the diagnosis, management, and prevention of chronic obstructive pulmonary disease. Updated 2011 (accessed 2012 May 25). Available from: http://www.goldcopd.org.1.
2. Zhao Y., Sato Y., Isaji T., et al. Branched N-glycans regulate the biological functions of integrins and cadherins. FEBS J. 2008, 275(9):1939-1948.
3. Gu J., Taniguchi N. Regulation of integrin functions by N-glycans. Glycoconj J. 2004, 21(1-2):9-15.
4. Taniguchi N., Korekane H. Branched N-glycans and their implications for cell adhesion, signaling and clinical applications for cancer biomarkers and in therapeutics. BMB Rep. 2011, 44(12):772-781.
5. Taniguchi N., Miyoshi E., Gu J., et al. Decoding sugar functions by identifying target glycoproteins. Curr. Opin. Struct. Biol. 2006, 16(5):561-566.
6. Taniguchi N, Gu J, Takahashi M, et al. Functional glycomics and evidence for gain- and loss-of-functions of target proteins for glycosyltransferases involved in N-glycan biosynthesis: their pivotal roles in growth and development, cancer metastasis and antibody therapy against cancer. Proceeding of the Japan Academy, Ser. B, 80 (2) (2004).
7. Wang X., Inoue S., Gu J., et al. Dysregulation of TGF-beta1 receptor activation leads to abnormal lung development and emphysema-like phenotype in core fucose-deficient mice. Proc. Natl. Acad. Sci. USA 2005, 102(44):15791-15796.
8. Gao C., Maeno T., Ota F., et al. Sensitivity of heterozygous α1,6-fucosyltransferase knock-out mice to cigarette smoke-induced emphysema: implication of aberrant transforming growth factor-β signaling and matrix metalloproteinase gene expression. J. Biol. Chem. 2012, 287:16699-16708.
9. Wang X., Gu J., Ihara H., et al. Core fucosylation regulates epidermal growth factor receptor-mediated intracellular signaling. J. Biol. Chem. 2006, 281(5):2572-2577.
10. Wang X., Gu J., Miyoshi E., et al. Phenotype changes of Fut8 knockout mouse: core fucosylation is crucial for the function of growth factor receptor(s). Methods Enzymol. 2006, 417:11-22.
11. Vanhooren V., Dewaele S., Kuro O.M., et al. Alteration in N-glycomics during mouse aging: a role for FUT8. Aging Cell 2011, 10(6):1056-1066.
12. Wang X., Fukuda T., Li W., et al. Requirement of Fut8 for the expression of vascular endothelial growth factor receptor-2: a new mechanism for the emphysema-like changes observed in Fut8-deficient mice. J. Biochem. 2009, 145(5):643-651.
13. Kasahara Y., Tuder R.M., Taraseviciene-Stewart L., et al. Inhibition of VEGF receptors causes lung cell apoptosis and emphysema. J. Clin. Invest. 2000, 106(11):1311-1319.
14. Valipour A., Schreder M., Wolzt M., et al. Circulating vascular endothelial growth factor and systemic inflammatory markers in patients with stable and exacerbated chronic obstructive pulmonary disease. Clin. Sci. (Lond) 2008, 115(7):225-232.
15. Sala E., Villena C., Balaguer C., et al. Abnormal levels of circulating endothelial progenitor cells during exacerbations of COPD. Lung 2010, 188(4):331-338.
16. Lindahl P., Karlsson L., Hellstrom M., et al. Alveogenesis failure in PDGF-A-deficient mice is coupled to lack of distal spreading of alveolar smooth muscle cell progenitors during lung development. Development 1997, 124(20):3943-3953.
17. Hogg J.C., Senior R.M. Chronic obstructive pulmonary disease - part 2: pathology and biochemistry of emphysema. Thorax 2002, 57(9):830-834.
18. Betsuyaku T., Nishimura M., Takeyabu K., et al. Neutrophil granule proteins in bronchoalveolar lavage fluid from subjects with subclinical emphysema. Am. J. Respir. Crit. Care Med. 1999, 159(6):1985-1991.
19. Atkinson J.J., Senior R.M. Matrix metalloproteinase-9 in lung remodeling. Am. J. Respir. Cell Mol. Biol. 2003, 28(1):12-24.
20. Boschetto P., Quintavalle S., Zeni E., et al. Association between markers of emphysema and more severe chronic obstructive pulmonary disease. Thorax 2006, 61(12):1037-1042.
21. Atkinson J.J., Lutey B.A., Suzuki Y., et al. The role of matrix metalloproteinase-9 in cigarette smoke-induced emphysema. Am. J. Respir. Crit. Care Med. 2011, 183(7):876-884.
22. Higashimoto Y., Iwata T., Okada M., et al. Serum biomarkers as predictors of lung function decline in chronic obstructive pulmonary disease. Respir. Med. 2009, 103(8):1231-1238.
23. Mercer P.F., Shute J.K., Bhowmik A., et al. MMP-9, TIMP-1 and inflammatory cells in sputum from COPD patients during exacerbation. Respir. Res. 2005, 6:151.
24. Kamio, Assessment of usefulness of fut8 activity as a novel bio-marker for COPD. Am. J. Respir. Crit. Care Med. (2010) 181 (181) A4369.
25. Bivas-Benita M., Zwier R., Junginger H.E., et al. Non-invasive pulmonary aerosol delivery in mice by the endotracheal route. Eur. J. Pharm. Biopharm. 2005, 61(3):214-218.
26. Suzuki M., Betsuyaku T., Ito Y., et al. Curcumin attenuates elastase- and cigarette smoke-induced pulmonary emphysema in mice. Am. J. Physiol. Lung Cell Mol. Physiol. 2009, 296(4):L614-L623.
27. Koscielak J., Pacuszka T., Miller-Podraza H., et al. Activities of fucosyltransferases in sera of leukaemic patients: platelet origin of serum alpha-6-l-fucosyltransferase. Biochem. Soc. Trans. 1987, 15(4):603-606.
28. Hurst J.R., Vestbo J., Anzueto A., et al. Susceptibility to exacerbation in chronic obstructive pulmonary disease. N. Engl. J. Med. 2010, 363(12):1128-1138.
29. Nakano Y., Muro S., Sakai H., et al. Computed tomographic measurements of airway dimensions and emphysema in smokers. Correlation with lung function. Am. J. Respir. Crit. Care Med. 2000, 162(3 Pt 1):1102-1108.
30. Fukuchi Y. The aging lung and chronic obstructive pulmonary disease: similarity and difference. Proc. Am. Thorac. Soc. 2009, 6(7):570-572.
31. Rajendrasozhan S., Yang S.R., Kinnula V.L., et al. SIRT1, an antiinflammatory and antiaging protein, is decreased in lungs of patients with chronic obstructive pulmonary disease. Am. J. Respir. Crit. Care Med. 2008, 177(8):861-870.
32. Anthonisen N.R., Connett J.E., Kiley J.P., et al. Effects of smoking intervention and the use of an inhaled anticholinergic bronchodilator on the rate of decline of FEV1. The Lung Health Study. JAMA 1994, 272(19):1497-1505.
33. Scanlon P.D., Connett J.E., Waller L.A., et al. Smoking cessation and lung function in mild-to-moderate chronic obstructive pulmonary disease. The Lung Health Study. Am J Respir Crit Care Med 2000, 161(2 Pt 1):381-390.
34. Donaldson G.C., Seemungal T.A., Bhowmik A., et al. Relationship between exacerbation frequency and lung function decline in chronic obstructive pulmonary disease. Thorax 2002, 57(10):847-852.
35. Celli B.R., Thomas N.E., Anderson J.A., et al. Effect of pharmacotherapy on rate of decline of lung function in chronic obstructive pulmonary disease: results from the TORCH study. Am. J. Respir. Crit. Care Med. 2008, 178(4):332-338.
36. Decramer M., Celli B., Kesten S., et al. Effect of tiotropium on outcomes in patients with moderate chronic obstructive pulmonary disease (UPLIFT): a prespecified subgroup analysis of a randomised controlled trial. Lancet 2009, 374(9696):1171-1178.
37. Nishimura M., Makita H., et al. Annual change in pulmonary function and clinical phenotype in chronic obstructive pulmonary disease. Am. J. Respir. Crit. Care Med. 2012, 185(1):44-52.
38. Yamada M., Ishii T., Ikeda S., et al. Association of fucosyltransferase 8 (FUT8) polymorphism Thr267Lys with pulmonary emphysema. J. Hum. Genet. 2011, 56(12):857-860.
39. Opdenakker G., Van den Steen P.E., Dubois B., et al. Gelatinase B functions as regulator and effector in leukocyte biology. J. Leukoc. Biol. 2001, 69(6):851-859.
40. Chakrabarti S., Zee J.M., Patel K.D. Regulation of matrix metalloproteinase-9 (MMP-9) in TNF-stimulated neutrophils: novel pathways for tertiary granule release. J. Leukoc. Biol. 2006, 79(1):214-222.
41. Pugin J., Widmer M.C., Kossodo S., et al. Human neutrophils secrete gelatinase B in vitro and in vivo in response to endotoxin and proinflammatory mediators. Am. J. Respir. Cell Mol. Biol. 1999, 20(3):458-464.