Information de reference pour ce titreAccession Number: | 00124288-200504000-00003.
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Author: | Hug, Christopher 1,2,3; Lodish, Harvey F 1,4
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Institution: | (1)Whitehead Institute for Biomedical Research, Cambridge, MA 02142, USA (2)Division of Respiratory Disease, Children's Hospital, Boston, MA 02115, USA (3)Harvard Medical School, Boston, MA 02115, USA (4)Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142, USA
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Title: | |
Source: | Current Opinion in Pharmacology. 5(2):129-134, April 2005.
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Abstract: | : Adiponectin, a novel hormone made by fat tissue, regulates energy metabolism and endothelial activation. Serum levels of adiponectin are reduced in conditions that are associated with an increased risk of cardiovascular disease, such as diabetes and the metabolic syndrome. Adiponectin trimers assemble into higher-order oligomers, which have different signaling properties. Adiponectin trimers and a C-terminal globular domain activate AMP-activated protein kinase, whereas hexamer and high-molecular weight isoforms activate nuclear factor-[kappa]B signaling pathways. Exogenous adiponectin corrects metabolic defects that are associated with insulin resistance, and might protect the endothelium from the progression of cardiovascular disease. Receptors for adiponectin have been described and might provide future therapeutic targets for the treatment of cardiovascular disease.
(C) 2005Elsevier, Inc.
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References: | 1. Scherer PE, Williams S, Fogliano M, Baldini G, Lodish HF: A novel serum protein similar to C1q, produced exclusively in adipocytes. J Biol Chem 1995, 270:26746-26749.
2. Shapiro L, Scherer PE: The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor. Curr Biol 1998, 8:335-338.
3. Tsao TS, Tomas E, Murrey HE, Hug C, Lee DH, Ruderman NB, Heuser JE, Lodish HF: Role of disulfide bonds in Acrp30/adiponectin structure and signaling specificity. Different oligomers activate different signal transduction pathways. J Biol Chem 2003, 278:50810-50817.
4. Fruebis J, Tsao TS, Javorschi S, Ebbets-Reed D, Erickson MR, Yen FT, Bihain BE, Lodish HF: Proteolytic cleavage product of 30-kDa adipocyte complement-related protein increases fatty acid oxidation in muscle and causes weight loss in mice. Proc Natl Acad Sci USA 2001, 98:2005-2010.
5. Yamauchi T, Kamon J, Waki H, Terauchi Y, Kubota N, Hara K, Mori Y, Ide T, Murakami K, Tsuboyama-Kasaoka N, et al.: The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity. Nat Med 2001, 7:941-946.
6. Arita Y, Kihara S, Ouchi N, Takahashi M, Maeda K, Miyagawa J, Hotta K, Shimomura I, Nakamura T, Miyaoka K, et al.: Paradoxical decrease of an adipose-specific protein, adiponectin, in obesity. Biochem Biophys Res Commun 1999, 257:79-83.
7. Hotta K, Funahashi T, Arita Y, Takahashi M, Matsuda M, Okamoto Y, Iwahashi H, Kuriyama H, Ouchi N, Maeda K, et al.: Plasma concentrations of a novel, adipose-specific protein, adiponectin, in type 2 diabetic patients. Arterioscler Thromb Vasc Biol 2000, 20:1595-1599.
8*. Pajvani UB, Hawkins M, Combs TP, Rajala MW, Doebber T, Berger JP, Wagner JA, Wu M, Knopps A, Xiang AH, et al.: Complex distribution, not absolute amount of adiponectin, correlates with thiazolidinedione-mediated improvement in insulin sensitivity. J Biol Chem 2004, 279:12152-12162.The first paper to introduce the concept of clinically important distinctions in adiponectin complex distribution.
9. Tonelli J, Li W, Kishore P, Pajvani UB, Kwon E, Weaver C, Scherer PE, Hawkins M: Mechanisms of early insulin-sensitizing effects of thiazolidinediones in type 2 diabetes. Diabetes 2004, 53:1621-1629.
10. Kaplan NM: The deadly quartet. Upper-body obesity, glucose intolerance, hypertriglyceridemia, and hypertension. Arch Intern Med 1989, 149:1514-1520.
11. Kaplan NM: Obesity in hypertension: effects on prognosis and treatment. J Hypertens Suppl 1998, 16:S35-S37.
12. Kissebah AH, Sonnenberg GE, Myklebust J, Goldstein M, Broman K, James RG, Marks JA, Krakower GR, Jacob HJ, Weber J, et al.: Quantitative trait loci on chromosomes 3 and 17 influence phenotypes of the metabolic syndrome. Proc Natl Acad Sci USA 2000, 97:14478-14483.
13. Adamczak M, Wiecek A, Funahashi T, Chudek J, Kokot F, Matsuzawa Y: Decreased plasma adiponectin concentration in patients with essential hypertension. Am J Hypertens 2003, 16:72-75.
14. Ohashi K, Ouchi N, Kihara S, Funahashi T, Nakamura T, Sumitsuji S, Kawamoto T, Matsumoto S, Nagaretani H, Kumada M, et al.: Adiponectin I164T mutation is associated with the metabolic syndrome and coronary artery disease. J Am Coll Cardiol 2004, 43:1195-1200.
15. Lacquemant C, Froguel P, Lobbens S, Izzo P, Dina C, Ruiz J: The adiponectin gene SNP+45 is associated with coronary artery disease in Type 2 (non-insulin-dependent) diabetes mellitus. Diabet Med 2004, 21:776-781.
16*. Pischon T, Girman CJ, Hotamisligil GS, Rifai N, Hu FB, Rimm EB: Plasma adiponectin levels and risk of myocardial infarction in men. J Am Med Assoc 2004, 291:1730-1737.A clinical study that demonstrates the cardiovascular protective effects of elevated adiponectin levels.
17. Zoccali C, Mallamaci F, Tripepi G, Benedetto FA, Cutrupi S, Parlongo S, Malatino LS, Bonanno G, Seminara G, Rapisarda F, et al.: Adiponectin, metabolic risk factors, and cardiovascular events among patients with end-stage renal disease. J Am Soc Nephrol 2002, 13:134-141.
18. Marchlewska A, Stenvinkel P, Lindholm B, Danielsson A, Pecoits-Filho R, Lonnqvist F, Schalling M, Heimburger O, Nordfors L: Reduced gene expression of adiponectin in fat tissue from patients with end-stage renal disease. Kidney Int 2004, 66:46-50.
19. Combs TP, Pajvani UB, Berg AH, Lin Y, Jelicks LA, Laplante M, Nawrocki AR, Rajala MW, Parlow AF, Cheeseboro L, et al.: A transgenic mouse with a deletion in the collagenous domain of adiponectin displays elevated circulating adiponectin and improved insulin sensitivity. Endocrinology 2004, 145:367-383.
20. Kumar S, Coenen MJ, Scherer PE, Bahn RS: Evidence for enhanced adipogenesis in the orbits of patients with Graves' ophthalmopathy. J Clin Endocrinol Metab 2004,89:930-935.
21. Yaturu S, Prado S, Grimes SR: Changes in adipocyte hormones leptin, resistin, and adiponectin in thyroid dysfunction. J Cell Biochem 2004, 93:491-496.
22. Tsao TS, Murrey HE, Hug C, Lee DH, Lodish HF: Oligomerization state-dependent activation of NF-[kappa]B signaling pathway by adipocyte complement-related protein of 30 kDa (Acrp30). J Biol Chem 2002, 277:29359-29362.
23. Sato C, Yasukawa Z, Honda N, Matsuda T, Kitajima K: Identification and adipocyte differentiation-dependent expression of the unique disialic acid residue in an adipose tissue specific glycoprotein, adipo Q. J Biol Chem 2001, 276:28849-28856.
24. Wang Y, Xu A, Knight C, Xu LY, Cooper GJ: Hydroxylation and glycosylation of the four conserved lysine residues in the collagenous domain of adiponectin. Potential role in the modulation of its insulin-sensitizing activity. J Biol Chem 2002, 277:19521-19529.
25. Wang Y, Lu G, Wong WP, Vliegenthart JF, Gerwig GJ, Lam KS, Cooper GJ, Xu A: Proteomic and functional characterization of endogenous adiponectin purified from fetal bovine serum. Proteomics 2004, 12:3933-3942.
26. Ouchi N, Kihara S, Arita Y, Okamoto Y, Maeda K, Kuriyama H, Hotta K, Nishida M, Takahashi M, Muraguchi M, et al.: Adiponectin, an adipocyte-derived plasma protein, inhibits endothelial NF-[kappa]B signaling through a cAMP-dependent pathway. Circulation 2000, 102:1296-1301.
27. Kobayashi H, Ouchi N, Kihara S, Walsh K, Kumada M, Abe Y, Funahashi T, Matsuzawa Y: Selective suppression of endothelial cell apoptosis by the high molecular weight form of adiponectin. Circ Res 2004, 94:e27-e31.
28. Yamauchi T, Kamon J, Minokoshi Y, Ito Y, Waki H, Uchida S, Yamashita S, Noda M, Kita S, Ueki K, et al.: Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase. Nat Med 2002, 8:1288-1295.
29. Tomas E, Tsao TS, Saha AK, Murrey HE, Zhang Cc C, Itani SI, Lodish HF, Ruderman NB: Enhanced muscle fat oxidation and glucose transport by ACRP30 globular domain: acetyl-CoA carboxylase inhibition and AMP-activated protein kinase activation. Proc Natl Acad Sci USA 2002, 99:16309-16313.
30. Carling D: The AMP-activated protein kinase cascade - a unifying system for energy control. Trends Biochem Sci 2004, 29:18-24.
31. Ruderman NB, Saha AK, Kraegen EW: Minireview: malonyl CoA, AMP-activated protein kinase, and adiposity. Endocrinology 2003, 144:5166-5171.
32. Hardie DG: Minireview: the AMP-activated protein kinase cascade: the key sensor of cellular energy status. Endocrinology 2003, 144:5179-5183.
33. Zhou G, Myers R, Li Y, Chen Y, Shen X, Fenyk-Melody J, Wu M, Ventre J, Doebber T, Fujii N, et al.: Role of AMP-activated protein kinase in mechanism of metformin action. J Clin Invest 2001,108:1167-1174.
34. Ouchi N, Ohishi M, Kihara S, Funahashi T, Nakamura T, Nagaretani H, Kumada M, Ohashi K, Okamoto Y, Nishizawa H, et al.: Association of hypoadiponectinemia with impaired vasoreactivity. Hypertension 2003, 42:231-234.
35. Zeng G, Nystrom FH, Ravichandran LV, Cong LN, Kirby M, Mostowski H, Quon MJ: Roles for insulin receptor, PI3-kinase, and Akt in insulin-signaling pathways related to production of nitric oxide in human vascular endothelial cells. Circulation 2000, 101:1539-1545.
36*. Chen H, Montagnani M, Funahashi T, Shimomura I, Quon MJ: Adiponectin stimulates production of nitric oxide in vascular endothelial cells. J Biol Chem 2003, 278:45021-45026.Demonstrated that adiponectin, like insulin, simulated endothelial nitric oxide synthase activation in endothelial cells through AMPK; the authors hypothesized that adiponectin might coordinate vasodilatation and metabolic regulation.
37. Berg AH, Combs TP, Du X, Brownlee M, Scherer PE: The adipocyte-secreted protein Acrp30 enhances hepatic insulin action. Nat Med 2001, 7:947-953.
38. Ma K, Cabrero A, Saha PK, Kojima H, Li L, Chang BH, Paul A, Chan L: Increased [beta]-oxidation but no insulin resistance or glucose intolerance in mice lacking adiponectin. J Biol Chem 2002, 277:34658-34661.
39. Kubota N, Terauchi Y, Yamauchi T, Kubota T, Moroi M, Matsui J, Eto K, Yamashita T, Kamon J, Satoh H, et al.: Disruption of adiponectin causes insulin resistance and neointimal formation. J Biol Chem 2002, 277:25863-25866.
40. Ouchi N, Kihara S, Arita Y, Maeda K, Kuriyama H, Okamoto Y, Hotta K, Nishida M, Takahashi M, Nakamura T, et al.: Novel modulator for endothelial adhesion molecules: adipocyte-derived plasma protein adiponectin. Circulation 1999, 100:2473-2476.
41. Maeda N, Shimomura I, Kishida K, Nishizawa H, Matsuda M, Nagaretani H, Furuyama N, Kondo H, Takahashi M, Arita Y, et al.: Diet-induced insulin resistance in mice lacking adiponectin/ACRP30. Nat Med 2002, 8:731-737.
42. Schaffer JE, Lodish HF: Expression cloning and characterization of a novel adipocyte long chain fatty acid transport protein. Cell 1994, 79:427-436.
43. Stahl A, Evans JG, Pattel S, Hirsch D, Lodish HF: Insulin causes fatty acid transport protein translocation and enhanced fatty acid uptake in adipocytes. Dev Cell 2002, 2:477-488.
44. Matsuda M, Shimomura I, Sata M, Arita Y, Nishida M, Maeda N, Kumada M, Okamoto Y, Nagaretani H, Nishizawa H, et al.: Role of adiponectin in preventing vascular stenosis. The missing link of adipo-vascular axis. J Biol Chem 2002, 277:37487-37491.
45*. Wong GW, Wang J, Hug C, Tsao TS, Lodish HF: A family of Acrp30/adiponectin structural and functional paralogs. Proc Natl Acad Sci USA 2004, 101:10302-10307.Genomic analysis identified paralogs of adiponectin with potentially overlapping and compensatory functions.
46. Okamoto Y, Arita Y, Nishida M, Muraguchi M, Ouchi N, Takahashi M, Igura T, Inui Y, Kihara S, Nakamura T, et al.: An adipocyte-derived plasma protein, adiponectin, adheres to injured vascular walls. Horm Metab Res 2000, 32:47-50.
47*. Yamauchi T, Kamon J, Ito Y, Tsuchida A, Yokomizo T, Kita S, Sugiyama T, Miyagishi M, Hara K, Tsunoda M, et al.: Cloning of adiponectin receptors that mediate antidiabetic metabolic effects. Nature 2003, 423:762-769.Expression-cloning yielded the first description of putative adiponectin receptors with a novel membrane topology. The described activities of these molecules are consistent with their involvement in metabolic regulation, but questions persist concerning their ligand specificities.
48. Sohn J, Ryu K, Sievert G, Jeoung M, Ji I, Ji TH: Follicle-stimulating hormone interacts with exoloop 3 of the receptor. J Biol Chem 2002, 277:50165-50175.
49. Wiley SR, Cassiano L, Lofton T, Davis-Smith T, Winkles JA, Lindner V, Liu H, Daniel TO, Smith CA, Fanslow WC: A novel TNF receptor family member binds TWEAK and is implicated in angiogenesis. Immunity 2001, 15:837-846.
50*. Hug C, Wang J, Ahmad NS, Bogan JS, Tsao TS, Lodish HF: T-cadherin is a receptor for hexameric and high-molecular-weight forms of Acrp30/adiponectin. Proc Natl Acad Sci USA 2004, 101:10308-10313.Expression-cloning of an adiponectin receptor demonstrated that an unusual cadherin, T-cadherin, preferentially binds hexamer and HMW adiponectin isoforms.
51. Ranscht B, Dours-Zimmermann MT: T-cadherin, a novel cadherin cell adhesion molecule in the nervous system lacks the conserved cytoplasmic region. Neuron 1991, 7:391-402.
52. Ivanov D, Philippova M, Antropova J, Gubaeva F, Iljinskaya O, Tararak E, Bochkov V, Erne P, Resink T, Tkachuk V: Expression of cell adhesion molecule T-cadherin in the human vasculature. Histochem Cell Biol 2001, 115:231-242.
53. Kudrjashova E, Bashtrikov P, Bochkov V, Parfyonova Y, Tkachuk V, Antropova J, Iljinskaya O, Tararak E, Erne P, Ivanov D, et al.: Expression of adhesion molecule T-cadherin is increased during neointima formation in experimental restenosis. Histochem Cell Biol 2002, 118:281-290.
54. Qin M, Zeng Z, Zheng J, Shah PK, Schwartz SM, Adams LD, Sharifi BG: Suppression subtractive hybridization identifies distinctive expression markers for coronary and internal mammary arteries. Arterioscler Thromb Vasc Biol 2003, 23:425-433.
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Language: | English.
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Document Type: | Article.
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Journal Subset: | Pharmacology.
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ISSN: | 1471-4892
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NLM Journal Code: | 100966133
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DOI Number: | https://dx.doi.org/10.1016/j.cop...- ouverture dans une nouvelle fenêtre
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