High glucose downregulates the number of caveolae in monocytes through oxidative stress from NADPH oxidase: Implications for atherosclerosis

Biochimica et Biophysica Acta - Molecular Basis of Disease

Volumn 1772, Issue 3, 2007, Pages 364-372

  Hayashi, Toshio ^a   Juliet, Packiasamy A R ^a   Miyazaki, Asaka ^a   Ignarro, Louis J ^b   Iguchi, Akihisa ^a  

^a NAGOYA UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Caveolae; Glucose; Macrophage; NADPH oxidase; Nitric oxide

Indexed keywords

CAVEOLIN; DNA; GLUCOSE; INDUCIBLE NITRIC OXIDE SYNTHASE; MESSENGER RNA; NITRATE; NITRIC OXIDE; NITRITE; PROTEIN P47; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE;

ARTICLE; ATHEROGENESIS; ATHEROSCLEROSIS; ATOMIC FORCE MICROSCOPY; CAVEOLA; CONFOCAL MICROSCOPY; CONTROLLED STUDY; DIABETES MELLITUS; ENZYME ACTIVITY; FLOW CYTOMETRY; FLUORESCENCE MICROSCOPY; GENE EXPRESSION; HUMAN; HUMAN CELL; HYPERGLYCEMIA; IMMUNOPRECIPITATION; MONOCYTE; NUCLEOTIDE SEQUENCE; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN LOCALIZATION; SCANNING ELECTRON MICROSCOPY;

APOPTOSIS; ATHEROSCLEROSIS; CAVEOLAE; CAVEOLIN 1; CELL DIFFERENTIATION; CELLS, CULTURED; GLUCOSE; HUMANS; MACROPHAGES; MONOCYTES; NADPH OXIDASE; NITRIC OXIDE; NITRIC OXIDE SYNTHASE TYPE II; OXIDATIVE STRESS; SUPEROXIDES;

EID: 33847016018     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2006.11.011     Document Type: Article

References (44)

1. Stamler J., Vaccaro O., Neaton J.D., and Wentworth D. Diabetes, other risk factors, and 12-yr cardiovascular mortality for men screened in the Multiple Risk Factor Intervention Trial. Diabetes Care 16 (1993) 434-444
2. McCarron P., Greenwood R., and Elwood P. The incidence and etiology of stroke in the Caerphilly and Speedwell Collaborative Studies II: risk factors for ischemic stroke. Public Health 15 (2001) 12-20
3. Chun B.Y., Dobson A.J., and Heller R.F. The impact of diabetes on survival among patients with first myocardial infarction. Diabetes Care 20 (1997) 704-708
4. Wannamethee G., Whincup P.H., Shaper A.G., Walker M., and MacFarlane P.W. Factors determining case fatality in myocardial infarction "who dies in a heart attack"?. Br. Heart J. 74 (1995) 324-331
5. Rosen P., Nawroth P.P., and King G. The role of oxidative stress in the onset and progression of diabetes and its complications: a summary of a Congress Series sponsored by UNESCO-MCBN, the American Diabetes Association and the German Diabetes Society. Diabetes Metab. Res. Rev. 17 (2001) 189-212
6. Ross R. Atherosclerosis-An inflammatory disease. N. Engl. J. Med. 340 (1999) 115-126
7. Steinberg D. Low density lipoprotein oxidation and its pathobiological significance. J. Biol. Chem. 272 (1997) 20963-20966
8. Chang F.Y., and Shaio M.F. Respiratory burst activity of monocytes from patients with non-insulin-dependent diabetes mellitus. Diabetes Res. Clin. Pract. 29 (1995) 121-127
9. Juliet P.A., Hayashi T., Iguchi A., and Ignarro L.J. Concomitant production of nitric oxide and superoxide in human macrophages. Biochem. Biophys. Res. Commun. 310 (2003) 367-370
10. Cathcart M.K. Regulation of superoxide anion production by NADPH oxidase in monocytes/macrophages: contributions to atherosclerosis. Arterioscler. Thromb. Vasc. Biol. 24 (2004) 23-28
11. Aviram M. Macrophage foam cell formation during early atherogenesis is determined by the balance between pro-oxidants and anti-oxidants in arterial cells and blood lipoproteins. Antioxid. Redox Signal. 1 (1999) 585-594
12. Groemping Y., Lapouge K., Smerdon S.J., and Rittinger K. Molecular basis of phosphorylation-induced activation of the NADPH oxidase. Cell 113 (2003) 343-355
13. Parthasarathy S., and Santanam N. Mechanisms of oxidation, antioxidants, and atherosclerosis. Curr. Opin. Lipidol. 5 (1994) 371-375
14. Segal A.W., and Abo A. The biochemical basis of the NADPH oxidase of phagocytes. Trends Biochem. Sci. 18 (1993) 43-47
15. Leto T.L., Lomax K.J., and Volpp B.D. Cloning of a 67-kD neutrophil oxidase factor with similarity to a noncatalytic region of p60c-src. Science 248 (1990) 727-730
16. Kadri-Hassani N., Leger C.L., and Descomps B. The fatty acid bimodal action on superoxide anion production by human adherent monocytes under phorbol 12-myristate 13-acetate or diacylglycerol activation can be explained by the modulation of protein kinase C and p47phox translocation. J. Biol. Chem. 270 (1995) 15111-15118
17. Cachia O., Benna J.E., Pedruzzi E., Descomps B., Gougerot-Pocidalo M.A., and Leger C.L. alpha-tocopherol inhibits the respiratory burst in human monocytes. Attenuation of p47(phox) membrane translocation and phosphorylation. J. Biol. Chem. 273 (1998) 32801-32805
18. Yanagitani Y., Rakugi H., and Okamura A. Angiotensin II type 1 receptor-mediated peroxide production in human macrophages. Hypertension 33 (1999) 335-339
19. Monier S., Dietzen D.J., Hastings W.R., Lublin D.M., and Kurzchalia T.V. Oligomerization of VIP21-caveolin in vitro is stabilized by long chain fatty acylation or cholesterol. FEBS Lett. 388 (1996) 143-149
20. Frank P.G., Woodman S.E., Park D.S., and Lisanti M.P. Caveolin, caveolae, and endothelial cell function. Arterioscler. Thromb. Vasc. Biol. 23 (2003) 1161-1168
21. Matveev S., van der Westhuyzen D.R., and Smart E.J. Co-expression of scavenger receptor-BI and caveolin-1 is associated with enhanced selective cholesteryl ester uptake in THP-1 macrophages. J. Lipid Res. 40 (1999) 1647-1654
22. Parpal S., Karlsson M., Thorn H., and Stralfors P. Cholesterol depletion disrupts caveolae and insulin receptor signaling for metabolic control via insulin receptor substrate-1, but not for mitogen-activated protein kinase control. J. Biol. Chem. 276 (2001) 9670-9678
23. Hayashi T., Sumi D., and Juliet P.A. Gene transfer of endothelial NO synthase, but not eNOS plus inducible NOS, regressed atherosclerosis in rabbits. Cardiovasc. Res. 61 (2004) 339-351
24. Niu X.L., Yang X., and Hoshiai Y. Inducible nitric oxide synthase deficiency does not affect the susceptibility of mice to atherosclerosis but increases collagen content in lesions. Circulation 103 (2001) 1115-1120
25. Hayashi T., Esaki T., Mu-to E., and Iguchi A. Dehydroepiandrosterone retards atherosclerosis formation through its conversion to estrogen: the possible role of nitric oxide. Arterioscler. Thromb. Vasc. Biol. 20 (2000) 782-792
26. Hayashi T., Yamada K., Esaki T., Muto E., Chaudhuri G., and Iguchi A. Physiological concentrations of 17beta-estradiol inhibit the synthesis of nitric oxide synthase in macrophages via a receptor-mediated system. J. Cardiovasc. Pharmacol. 31 (1998) 292-298
27. Lucius H., Friedrichson T., Kurzchalia T.V., and Lewin G.R. Identification of caveolae-like structures on the surface of intact cells using scanning force microscopy. J. Membr. Biol. 194 (2003) 97-108
28. Zhang X., Chen A., De Leon D., Li H., Noin E., Moy V.T., and Goligorsky M.S. Atomic force microscopy measurement of leukocyte-endothelial interaction. Am. J. Physiol.: Heart Circ. Physiol. 286 (2004) H359-H367
29. Xu H., Dinsdale D., Nemery B., and Hoet P.H. Role of residual additives in the cytotoxicity and cytokine release caused by polyvinyl chloride particles in pulmonary cell cultures. Toxicol. Sci. 72 (2003) 92-102
30. Pogatsa G. Altered responsiveness of vascular smooth muscle to drug in diabetes. In: Szekeres L., and Papp J.G. (Eds). Pharmacology of Smooth Muscle (1994), Springer-Verlag, New York 693-712
31. Burke A.P., Kolodgie F.D., and Zieske A. Morphologic findings of coronary atherosclerotic plaques in diabetics: a postmortem study. Arterioscler. Thromb. Vasc. Biol. 24 (2004) 1266-1271
32. Abrink M., Gobl A.E., Huang R., Nilsson K., and Hellman L. Human cell lines U-937, THP-1 and Mono Mac 6 represent relatively immature cells of the monocyte-macrophage cell lineage. Leukemia 8 (1994) 1579-1584
33. White C.C., Brock T.A., and Chang L.Y. Superoxide and peroxynitrite in atherosclerosis. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 1044-1048
34. Okamoto T., Schlegel A., Scherer P.E., and Lisanti M.P. Caveolins, a family of scaffolding proteins for organizing "preassembled signaling complexes" at the plasma membrane. J. Biol. Chem. 273 (1998) 5419-5422
35. - imbalance in insulin-resistant rat aorta. Diabetes 48 (1999) 2437-2445
36. Hayashi T., Juliet P.A., Kano-Hayashi H., Tsunekawa T., Dingqunfang D., Sumi D., et al. NADPH oxidase inhibitor, apocynin, restores the impaired endothelial-dependent and -independent responses and scavenges superoxide anion in rats with type 2 diabetes complicated by NO dysfunction. Diabetes. Obes. Metab. 7 (2005) 334-343
37. Llaverias G., Vazquez-Carrera M., Sanchez M.R., Noe V., Ciudad L.C., Laguna C.J., and Alegret M. Rosiglitazone upregulates caveolin-1 expression in THP-1 cells through a PPAR-dependent mechanism. J. Lipid Res. 45 (2004) 2015-2024
38. Navarro-Lerida I., Portoles M.T., Barrientos A.A., Gavilanes F., Bosca L., and Rodriguez-Crespo I. Induction of nitric oxide synthase-2 proceeds with the concomitant downregulation of the endogenous caveolin levels. J. Cell Sci. 117 (2004) 1687-1697
39. Shigematsu S., Watson R.T., Khan A.H., and Pessin J.E. The adipocyte plasma membrane caveolin functional/structural organization is necessary for the efficient endocytosis of GLUT4. J. Biol. Chem. 278 (2003) 10683-10690
40. Cohen A.W., Combs T.P., Scherer P.E., and Lisanti M.P. Role of caveolin and caveolae in insulin signaling and diabetes. Am. J. Physiol.: Endocrinol. Metab. 285 (2003) E1151-E1160
41. Fra A.M., Williamson E., Simons K., and Parton R.G. De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 8655-8659
42. Smart E.J., Ying Y., Donzell W.C., and Anderson R.G. A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane. J. Biol. Chem. 271 (1996) 29427-29435
43. Jayachandran M., Hayashi T., Sumi D., Iguchi A., and Miller V.M. Temporal effects of 17beta-estradiol on caveolin-1 mRNA and protein in bovine aortic endothelial cells. Am. J. Physiol.: Heart Circ. Physiol. 281 (2001) H1327-H1333
44. Anderson R.G., and Jacobson K. A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains. Science 296 (2002) 1821-1825