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Adiponectin (also referred to as GBP-28, apM1, AdipoQ and Acrp30) is a protein which in humans is encoded by the ADIPOQ gene.^[1] It is involved in regulating glucose levels as well as fatty acid breakdown.

Structure

Adiponectin is a 244-amino-acid-long polypeptide. There are four distinct regions of adiponectin. The first is a short signal sequence that targets the hormone for secretion outside the cell; next is a short region that varies between species; the third is a 65-amino acid region with similarity to collagenous proteins; the last is a globular domain. Overall this gene shows similarity to the complement 1Q factors (C1Q). However, when the 3-dimensional structure of the globular region was determined, a striking similarity to TNFα was observed, despite unrelated protein sequences.^[2]

Function

Adiponectin is a protein hormone that modulates a number of metabolic processes, including glucose regulation and fatty acid catabolism.^[3] Adiponectin is exclusively secreted from adipose tissue (and also from the placenta in pregnancy^[4]) into the bloodstream and is very abundant in plasma relative to many hormones. Levels of the hormone are inversely correlated with body fat percentage in adults,^[5] while the association in infants and young children is less clear. Transgenic mice with increased adiponectin show impaired adipocyte differentiation and increased energy expenditure associated with protein uncoupling.^[6] The hormone plays a role in the suppression of the metabolic derangements that may result in type 2 diabetes,^[5] obesity, atherosclerosis,^[3] non-alcoholic fatty liver disease (NAFLD) and an independent risk factor for metabolic syndrome.^[7] Adiponectin in combination with leptin has been shown to completely reverse insulin resistance in mice.^[8]

Adiponectin is secreted into the bloodstream where it accounts for approximately 0.01% of all plasma protein at around 5-10 μg/mL. Plasma concentrations reveal a sexual dimorphism, with females having higher levels than males. Levels of adiponectin are reduced in diabetics compared to non-diabetics. Weight reduction significantly increases circulating levels.^[9]

Adiponectin automatically self-associates into larger structures. Initially, three adiponectin molecules bind together to form a homotrimer. The trimers continue to self-associate and form hexamers or dodecamers. Like the plasma concentration, the relative levels of the higher-order structures are sexually dimorphic, where females have increased proportions of the high-molecular weight forms. Recent studies showed that the high-molecular weight form may be the most biologically active form regarding glucose homeostasis.^[10] High-molecular-weight adiponectin was further found to be associated with a lower risk of diabetes with similar magnitude of association as total adiponectin.^[11]

Adiponectin exerts some of its weight reduction effects via the brain. This is similar to the action of leptin,^[12] but the two hormones perform complementary actions, and can have additive effects.

Receptors

Adiponectin binds to a number of receptors. So far, two receptors have been identified, with homology to G protein-coupled receptors and one receptor similar to the cadherin family:^[13]^[14]

adiponectin receptor 1 – ADIPOR1
adiponectin receptor 2 – ADIPOR2
T-cadherin - T-Cad

These have distinct tissue specificities within the body and have different affinities to the various forms of adiponectin. The receptors affect the downstream target AMP kinase, an important cellular metabolic rate control point. Expression of the receptors are correlated with insulin levels, as well as reduced in mouse models of diabetes, particularly in skeletal muscle and adipose tissue.^[15]^[16]

Discovery

Adiponectin was first characterised in 2007 in mice as a transcript overexpressed in preadipocytes^[17] (precursors of fat cells) differentiating into adipocytes.^[17]^[18]

The human homologue was identified as the most abundant transcript in adipose tissue. Contrary to expectations, despite being produced in adipose tissue, adiponectin was found to be decreased in obesity.^[3]^[5]^[12] This downregulation has not been fully explained. The gene was localised to chromosome 3q27, a region highlighted as affecting genetic susceptibility to type 2 diabetes and obesity. Supplementation by differing forms of adiponectin were able to improve insulin control, blood glucose and triglyceride levels in mouse models.

The gene was investigated for variants that predispose to type 2 diabetes.^[12]^[17]^[19]^[20]^[21]^[22] Several single nucleotide polymorphisms in the coding region and surrounding sequence were identified from several different populations, with varying prevalences, degrees of association and strength of effect on type 2 diabetes. Berberine, an herbal folk medicine, has been shown to increase adiponectin expression^[23] which partly explains its beneficial effects on metabolic disturbances. Mice fed the omega-3 fatty acids eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) have shown increased plasma adiponectin.^[24]

Metabolic effects

Adiponectin affects:

glucose flux
- decreased gluconeogenesis
- increased glucose uptake^[3]^[12]^[20]
lipid catabolism^[20]
- β-oxidation^[12]
- triglyceride clearance^[12]
protection from endothelial dysfunction (important facet of atherosclerotic formation)
insulin sensitivity
weight loss
control of energy metabolism.^[20]
upregulation of uncoupling proteins ^[6]

Hypoadiponectinemia

A low level of adiponectin is an independent risk factor for developing:

Metabolic syndrome^[7]
Diabetes mellitus^[12]^[17]^[19]^[21]^[22]

Pharmaceutical therapy

Because adiponectin is a novel hormone, no therapy has yet been developed with adiponectin and it may be some years before clinical trials commence. One obvious pharmaceutical treatment would be the administration of adiponectin; in mouse models such administration has shown positive effects.^[3] Problems to be overcome prior to human administration include establishing what the biologically active molecule is, what role post-translational modifications have upon the function and associated difficulties in generating biologically active molecules on a large scale. However, this remains a promising area of research for clinical therapy in diseases such as obesity, type 2 diabetes and fatty liver disease.^[21] Adiponectin levels may also affect breast cancer risk.^[25]

References

^ Maeda K, Okubo K, Shimomura I, Funahashi T, Matsuzawa Y, Matsubara K (April 1996). "cDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose Most abundant Gene transcript 1)". Biochem. Biophys. Res. Commun. 221 (2): 286–9. DOI:10.1006/bbrc.1996.0587. PMID 8619847.
^ Shapiro L, Scherer PE (March 1998). "The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor". Curr. Biol. 8 (6): 335–8. DOI:10.1016/S0960-9822(98)70133-2. PMID 9512423.
^ ^a ^b ^c ^d ^e Díez JJ, Iglesias P (March 2003). "The role of the novel adipocyte-derived hormone adiponectin in human disease". Eur. J. Endocrinol. 148 (3): 293–300. DOI:10.1530/eje.0.1480293. PMID 12611609.
^ Chen J, et al. (June 2006). "Secretion of adiponectin by human placenta: differential modulation of adiponectin and its receptors by cytokines.". Diabetalogica 49 (6): 1292–302. PMID 16570162.
^ ^a ^b ^c Ukkola O, Santaniemi M (November 2002). "Adiponectin: a link between excess adiposity and associated comorbidities?". J. Mol. Med. 80 (11): 696–702. DOI:10.1007/s00109-002-0378-7. PMID 12436346.
^ ^a ^b Bauche IB, El Mkadem SA, Pottier AM, Senou M, Many MC, Rezsohazy R, Penicaud L, Maeda N, Funahashi T, Brichard SM (April 2007). "Overexpression of adiponectin targeted to adipose tissue in transgenic mice: impaired adipocyte differentiation". Endocrinology 148 (4): 1539–49. DOI:10.1210/en.2006-0838. PMID 17204560.
^ ^a ^b Renaldi O, Pramono B, Sinorita H, Purnomo LB, Asdie RH, Asdie AH (January 2009). "Hypoadiponectinemia: a risk factor for metabolic syndrome". Acta Med Indones 41 (1): 20–4. PMID 19258676.
^ Yamauchi T, Kamon J, Waki H, Terauchi Y, Kubota N, Hara K, Mori Y, Ide T, Murakami K, Tsuboyama-Kasaoka N, Ezaki O, Akanuma Y, Gavrilova O, Vinson C, Reitman ML, Kagechika H, Shudo K, Yoda M, Nakano Y, Tobe K, Nagai R, Kimura S, Tomita M, Froguel P, Kadowaki T (August 2001). "The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity". Nat. Med. 7 (8): 941–6. DOI:10.1038/90984. PMID 11479627.
^ Coppola A, Marfella R, Coppola L, Tagliamonte E, Fontana D, Liguori E, Cirillo T, Cafiero M, Natale S, Astarita C (March 2008). "Effect of weight loss on coronary circulation and adiponectin levels in obese women". Int. J. Cardiol. 134 (3): 414–6. DOI:10.1016/j.ijcard.2007.12.087. PMID 18378021.
^ Oh DK, Ciaraldi T, Henry RR Adiponectin in health and disease. Diabetes Obes Metab 2007:9:282–289
^ Zhu N, Pankow JS, Ballantyne CM, Couper D, Hoogeveen RC, Pereira M, Duncan BB, Schmidt MI (November 2010). "High-molecular-weight adiponectin and the risk of type 2 diabetes in the ARIC study". J. Clin. Endocrinol. Metab. 95 (11): 5097–104. DOI:10.1210/jc.2010-0716. PMC 2968724. PMID 20719834. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2968724.
^ ^a ^b ^c ^d ^e ^f ^g Nedvídková J, Smitka K, Kopský V, Hainer V (2005). "Adiponectin, an adipocyte-derived protein". Physiol Res 54 (2): 133–40. PMID 15544426. http://www.biomed.cas.cz/physiolres/pdf/54/54_133.pdf.
^ Yamauchi T, Kamon J, Ito Y, Tsuchida A, Yokomizo T, Kita S, Sugiyama T, Miyagishi M, Hara K, Tsunoda M, Murakami K, Ohteki T, Uchida S, Takekawa S, Waki H, Tsuno NH, Shibata Y, Terauchi Y, Froguel P, Tobe K, Koyasu S, Taira K, Kitamura T, Shimizu T, Nagai R, Kadowaki T (June 2003). "Cloning of adiponectin receptors that mediate antidiabetic metabolic effects". Nature 423 (6941): 762–9. DOI:10.1038/nature01705. PMID 12802337.
^ Hug C, Wang J, Ahmad NS, Bogan JS, TSao TS, Lodish HF (2004). "T-cadherin is a receptor for hexameric and high-molecular-weight forms of Acrp30/adiponectin". Proc Natl Acad Sci U S A 101 (28): 10308–13. DOI:10.1073/pnas.0403382101. PMC 478568. PMID 15210937. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=478568.
^ Fang X, Sweeney G (November 2006). "Mechanisms regulating energy metabolism by adiponectin in obesity and diabetes". Biochem. Soc. Trans. 34 (Pt 5): 798–801. DOI:10.1042/BST0340798. PMID 17052201.
^ Bonnard C, Durand A, Vidal H, Rieusset J (February 2008). "Changes in adiponectin, its receptors and AMPK activity in tissues of diet-induced diabetic mice". Diabetes Metab. 34 (1): 52–61. DOI:10.1016/j.diabet.2007.09.006. PMID 18222103.
^ ^a ^b ^c ^d Lara-Castro C, Fu Y, Chung BH, Garvey WT (June 2007). "Adiponectin and the metabolic syndrome: mechanisms mediating risk for metabolic and cardiovascular disease". Curr. Opin. Lipidol. 18 (3): 263–70. DOI:10.1097/MOL.0b013e32814a645f. PMID 17495599.
^ Matsuzawa Y, Funahashi T, Kihara S, Shimomura I (January 2004). "Adiponectin and metabolic syndrome". Arterioscler. Thromb. Vasc. Biol. 24 (1): 29–33. DOI:10.1161/01.ATV.0000099786.99623.EF. PMID 14551151.
^ ^a ^b Hara K, Yamauchi T, Kadowaki T (April 2005). "Adiponectin: an adipokine linking adipocytes and type 2 diabetes in humans". Curr. Diab. Rep. 5 (2): 136–40. DOI:10.1007/s11892-005-0041-0. PMID 15794918.
^ ^a ^b ^c ^d Vasseur F, Leprêtre F, Lacquemant C, Froguel P (April 2003). "The genetics of adiponectin". Curr. Diab. Rep. 3 (2): 151–8. DOI:10.1007/s11892-003-0039-4. PMID 12728641.
^ ^a ^b ^c Hug C, Lodish HF (April 2005). "The role of the adipocyte hormone adiponectin in cardiovascular disease". Curr Opin Pharmacol 5 (2): 129–34. DOI:10.1016/j.coph.2005.01.001. PMID 15780820.
^ ^a ^b Vasseur F, Meyre D, Froguel P (2006). "Adiponectin, type 2 diabetes and the metabolic syndrome: lessons from human genetic studies". Expert Rev Mol Med 8 (27): 1–12. DOI:10.1017/S1462399406000147. PMID 17112391.
^ Choi BH, Kim YH, Ahn IS, Ha JH, Byun JM, Do MS (2009). "The inhibition of inflammatory molecule expression on 3T3-L1 adipocytes by berberine is not mediated by leptin signaling". Nutr Res Pract 3 (2): 84–8. DOI:10.4162/nrp.2009.3.2.84. PMC 2788178. PMID 20016706. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2788178.
^ Grimshaw CE, Matthews DA, Varughese KI, Skinner M, Xuong NH, Bray T, Hoch J, Whiteley JM (August 1992). "Characterization and nucleotide binding properties of a mutant dihydropteridine reductase containing an aspartate 37-isoleucine replacement". J. Biol. Chem. 267 (22): 15334–9. PMID 1639779.
^ Kaklamani VG, Sadim M, Hsi A, Offit K, Oddoux C, Ostrer H, Ahsan H, Pasche B, Mantzoros C (May 2008). "Variants of the adiponectin and adiponectin receptor 1 genes and breast cancer risk". Cancer Res. 68 (9): 3178–84. DOI:10.1158/0008-5472.CAN-08-0533. PMC 2685173. PMID 18451143. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2685173.

UpToDate Contents

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English Journal

AMP-activated protein kinase mediates insulin-like and lipo-mobilising effects of β-glucan-rich polysaccharides isolated from Pleurotus sajor-caju (Fr.), Singer mushroom, in 3T3-L1 cells.

Kanagasabapathy G, Chua KH, Malek SN, Vikineswary S, Kuppusamy UR.SourceDepartment of Biomedical Science, Faculty of Medicine, University of Malaya, 50603 Kuala Lumpur, Malaysia; Mushroom Research Centre, University of Malaya, 50603 Kuala Lumpur, Malaysia.
Food chemistry.Food Chem.2014 Feb 15;145:198-204. doi: 10.1016/j.foodchem.2013.08.051. Epub 2013 Aug 21.
Mushrooms have been used to treat various diseases for thousands of years. In the present study, the effects of Pleurotus sajor-caju mushroom on lipogenesis, lipolysis and oxidative stress in 3T3-L1 cells were investigated. The β-glucan-rich polysaccharides (GE) from P. sajor-caju stimulated lipoge
PMID 24128468

Piperine reverses high fat diet-induced hepatic steatosis and insulin resistance in mice.

Choi S, Choi Y, Choi Y, Kim S, Jang J, Park T.SourceDepartment of Food and Nutrition, Yonsei University, 50 Yonsei-ro, Seodaemun-gu, Seoul 120-749, Republic of Korea.
Food chemistry.Food Chem.2013 Dec 15;141(4):3627-35. doi: 10.1016/j.foodchem.2013.06.028. Epub 2013 Jun 17.
This study examined the effect of piperine on hepatic steatosis and insulin resistance induced in mice by feeding a high-fat diet (HFD) for 13 weeks and elucidated potential underlying molecular mechanisms. Administration of piperine (50 mg/kg body weight) to mice with HFD-induced hepatic steatosis
PMID 23993530

Effects of isolated GH deficiency on adipose tissue, feeding and adipokines in mice.

Recinella L, Shohreh R, Salvatori R, Orlando G, Vacca M, Brunetti L.SourceDepartment of Pharmacy, G. d'Annunzio University, Chieti, Italy.
Growth hormone & IGF research : official journal of the Growth Hormone Research Society and the International IGF Research Society.Growth Horm IGF Res.2013 Dec;23(6):237-42. doi: 10.1016/j.ghir.2013.08.004. Epub 2013 Aug 27.
OBJECTIVE: Growth hormone deficiency (GHD) leads to growth failure and changes in body composition including increased fat accumulation and reduced lean body mass in both humans and rodents. The aim of this study was to characterize the consequences of isolated GHD (IGHD) on adiposity, total body we
PMID 24021480

Japanese Journal

Anti-diabetic Action of 7-O-Galloyl-d-sedoheptulose, a Polyphenol from Corni Fructus, through Ameliorating Inflammation and Inflammation-Related Oxidative Stress in the Pancreas of Type 2 Diabetics

Park Chan Hum,Tanaka Takashi,Yokozawa Takako
Biological and Pharmaceutical Bulletin 36(5), 723-732, 2013-05-01
… The results showed that levels of glucose, leptin, insulin, C-peptide, resistin, tumor necrosis factor-α, and interleukin-6 in serum were down-regulated, while adiponectin was augmented by GS treatment. …
NAID 120005295876

Normalization of fasting hyperglycemia is beneficial for successful introduction of small amount of the GLP-1 analog liraglutide in an obese patient with type 2 diabetes mellitus

IIZUKA Katsumi,TOMITA Reiko,SUWA Tetsuya,HORIKAWA Yukio,TAKEDA Jun
Diabetology international 3(1), 61-64, 2013-03-01
NAID 10030925908

A case of mitochondrial kidney disease with insulin resistance and hypoadiponectinemia

BADEN YAMAGUCHI Megu,YAMADA Yuya,TAKAHI Yasumitsu,OBATA Yoshinari,SAISHO Kenji,TAMBA Sachiko,YAMAMOTO Koji,MURATSU Jun,MORISHIMA Atsuyuki,SAKAGUCHI Katsuhiko,MATSUZAWA Yuji
Diabetology international 3(1), 54-60, 2013-03-01
NAID 10030925882

Related Pictures

★リンクテーブル★

リンク元	「アディポネクチン」
拡張検索	「adiponectin receptor」「hypoadiponectinemia」

「アディポネクチン」

Adiponectin, C1Q and collagen domain containing
	; PDB rendering based on 1c28.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	4DOU
Identifiers
Symbols	ADIPOQ; ACDC; ACRP30; ADIPQTL1; ADPN; APM-1; APM1; GBP28
External IDs	OMIM: 605441 MGI: 106675 HomoloGene: 3525 GeneCards: ADIPOQ Gene
Gene Ontology
Molecular function	• receptor binding; • cytokine activity; • hormone activity; • protein binding; • sialic acid binding; • identical protein binding; • protein homodimerization activity; • eukaryotic cell surface binding;
Cellular component	• extracellular region; • collagen; • extracellular space; • endoplasmic reticulum;
Biological process	• response to hypoxia; • positive regulation of protein phosphorylation; • glucose metabolic process; • generation of precursor metabolites and energy; • fatty acid beta-oxidation; • response to nutrient; • response to sucrose stimulus; • response to glucose stimulus; • positive regulation of signal transduction; • negative regulation of platelet-derived growth factor receptor signaling pathway; • positive regulation of protein kinase A signaling cascade; • negative regulation of macrophage derived foam cell differentiation; • negative regulation of tumor necrosis factor-mediated signaling pathway; • positive regulation of cholesterol efflux; • regulation of glucose metabolic process; • negative regulation of smooth muscle cell migration; • fatty acid oxidation; • negative regulation of cell migration; • negative regulation of granulocyte differentiation; • negative regulation of protein autophosphorylation; • positive regulation of cellular protein metabolic process; • negative regulation of tumor necrosis factor production; • positive regulation of interleukin-8 production; • cellular response to insulin stimulus; • positive regulation of myeloid cell apoptosis; • adiponectin-mediated signaling pathway; • negative regulation of heterotypic cell-cell adhesion; • low-density lipoprotein particle clearance; • response to tumor necrosis factor; • cellular response to drug; • glucose homeostasis; • positive regulation of I-kappaB kinase/NF-kappaB cascade; • negative regulation of I-kappaB kinase/NF-kappaB cascade; • negative regulation of MAP kinase activity; • response to ethanol; • negative regulation of fat cell differentiation; • negative regulation of macrophage differentiation; • negative regulation of low-density lipoprotein particle receptor biosynthetic process; • negative regulation of gluconeogenesis; • negative regulation of blood pressure; • positive regulation of blood pressure; • positive regulation of protein kinase activity; • negative regulation of transcription, DNA-dependent; • positive regulation of fatty acid metabolic process; • positive regulation of glucose import; • negative regulation of hormone secretion; • negative regulation of smooth muscle cell proliferation; • negative regulation of inflammatory response; • negative regulation of inflammatory response; • positive regulation of peptidyl-tyrosine phosphorylation; • negative regulation of phagocytosis; • negative regulation of synaptic transmission; • brown fat cell differentiation; • protein homooligomerization; • response to glucocorticoid stimulus; • membrane depolarization; • membrane hyperpolarization; • negative regulation of ERK1 and ERK2 cascade; • detection of oxidative stress; • positive regulation of monocyte chemotactic protein-1 production; • protein localization in plasma membrane; • negative regulation of intracellular protein transport; • negative regulation of DNA biosynthetic process; • negative regulation of eukaryotic cell surface binding; • positive regulation of glycogen (starch) synthase activity; • positive regulation of metanephric glomerular visceral epithelial cell development; • positive regulation of cAMP-dependent protein kinase activity; • positive regulation of renal albumin absorption;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	This box: view; talk; edit;

　　[★]

英: adiponectin
関: 脂肪細胞、アディポカイン

脂肪細胞から分泌されるホルモン。(DMR.112)
肝臓や骨格筋に作用してインスリン感受性を増強させる。(DMR.112)
肥満者は2型糖尿病患者では血中濃度が低下(DMR.112)

「adiponectin receptor」

　　[★]

アディ・ネクチン受容体、アディ・ネクチンレセプター

「hypoadiponectinemia」

　　[★]

低アディ・ネクチン血症

[pmid8619847-0] Maeda K, Okubo K, Shimomura I, Funahashi T, Matsuzawa Y, Matsubara K (April 1996). "cDNA cloning and expression of a novel adipose specific collagen-like factor, apM1 (AdiPose Most abundant Gene transcript 1)". Biochem. Biophys. Res. Commun. 221 (2): 286–9. DOI:10.1006/bbrc.1996.0587. PMID 8619847.

[pmid9512423-1] Shapiro L, Scherer PE (March 1998). "The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor". Curr. Biol. 8 (6): 335–8. DOI:10.1016/S0960-9822(98)70133-2. PMID 9512423.

[pmid12611609-2] Díez JJ, Iglesias P (March 2003). "The role of the novel adipocyte-derived hormone adiponectin in human disease". Eur. J. Endocrinol. 148 (3): 293–300. DOI:10.1530/eje.0.1480293. PMID 12611609.

[pmid16570162-3] Chen J, et al. (June 2006). "Secretion of adiponectin by human placenta: differential modulation of adiponectin and its receptors by cytokines.". Diabetalogica 49 (6): 1292–302. PMID 16570162.

[pmid12436346-4] Ukkola O, Santaniemi M (November 2002). "Adiponectin: a link between excess adiposity and associated comorbidities?". J. Mol. Med. 80 (11): 696–702. DOI:10.1007/s00109-002-0378-7. PMID 12436346.

[pmid17204560-5] Bauche IB, El Mkadem SA, Pottier AM, Senou M, Many MC, Rezsohazy R, Penicaud L, Maeda N, Funahashi T, Brichard SM (April 2007). "Overexpression of adiponectin targeted to adipose tissue in transgenic mice: impaired adipocyte differentiation". Endocrinology 148 (4): 1539–49. DOI:10.1210/en.2006-0838. PMID 17204560.

[pmid19258676-6] Renaldi O, Pramono B, Sinorita H, Purnomo LB, Asdie RH, Asdie AH (January 2009). "Hypoadiponectinemia: a risk factor for metabolic syndrome". Acta Med Indones 41 (1): 20–4. PMID 19258676.

[pmid11479627-7] Yamauchi T, Kamon J, Waki H, Terauchi Y, Kubota N, Hara K, Mori Y, Ide T, Murakami K, Tsuboyama-Kasaoka N, Ezaki O, Akanuma Y, Gavrilova O, Vinson C, Reitman ML, Kagechika H, Shudo K, Yoda M, Nakano Y, Tobe K, Nagai R, Kimura S, Tomita M, Froguel P, Kadowaki T (August 2001). "The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity". Nat. Med. 7 (8): 941–6. DOI:10.1038/90984. PMID 11479627.

[pmid18378021-8] Coppola A, Marfella R, Coppola L, Tagliamonte E, Fontana D, Liguori E, Cirillo T, Cafiero M, Natale S, Astarita C (March 2008). "Effect of weight loss on coronary circulation and adiponectin levels in obese women". Int. J. Cardiol. 134 (3): 414–6. DOI:10.1016/j.ijcard.2007.12.087. PMID 18378021.

[9] Oh DK, Ciaraldi T, Henry RR Adiponectin in health and disease. Diabetes Obes Metab 2007:9:282–289

[pmid20719834-10] Zhu N, Pankow JS, Ballantyne CM, Couper D, Hoogeveen RC, Pereira M, Duncan BB, Schmidt MI (November 2010). "High-molecular-weight adiponectin and the risk of type 2 diabetes in the ARIC study". J. Clin. Endocrinol. Metab. 95 (11): 5097–104. DOI:10.1210/jc.2010-0716. PMC 2968724. PMID 20719834. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2968724.

[pmid15544426-11] ^ ^a ^b ^c ^d ^e ^f ^g Nedvídková J, Smitka K, Kopský V, Hainer V (2005). "Adiponectin, an adipocyte-derived protein". Physiol Res 54 (2): 133–40. PMID 15544426. http://www.biomed.cas.cz/physiolres/pdf/54/54_133.pdf.

[pmid12802337-12] Yamauchi T, Kamon J, Ito Y, Tsuchida A, Yokomizo T, Kita S, Sugiyama T, Miyagishi M, Hara K, Tsunoda M, Murakami K, Ohteki T, Uchida S, Takekawa S, Waki H, Tsuno NH, Shibata Y, Terauchi Y, Froguel P, Tobe K, Koyasu S, Taira K, Kitamura T, Shimizu T, Nagai R, Kadowaki T (June 2003). "Cloning of adiponectin receptors that mediate antidiabetic metabolic effects". Nature 423 (6941): 762–9. DOI:10.1038/nature01705. PMID 12802337.

[pmid15210937-13] Hug C, Wang J, Ahmad NS, Bogan JS, TSao TS, Lodish HF (2004). "T-cadherin is a receptor for hexameric and high-molecular-weight forms of Acrp30/adiponectin". Proc Natl Acad Sci U S A 101 (28): 10308–13. DOI:10.1073/pnas.0403382101. PMC 478568. PMID 15210937. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=478568.

[pmid17052201-14] Fang X, Sweeney G (November 2006). "Mechanisms regulating energy metabolism by adiponectin in obesity and diabetes". Biochem. Soc. Trans. 34 (Pt 5): 798–801. DOI:10.1042/BST0340798. PMID 17052201.

[pmid18222103-15] Bonnard C, Durand A, Vidal H, Rieusset J (February 2008). "Changes in adiponectin, its receptors and AMPK activity in tissues of diet-induced diabetic mice". Diabetes Metab. 34 (1): 52–61. DOI:10.1016/j.diabet.2007.09.006. PMID 18222103.

[pmid17495599-16] Lara-Castro C, Fu Y, Chung BH, Garvey WT (June 2007). "Adiponectin and the metabolic syndrome: mechanisms mediating risk for metabolic and cardiovascular disease". Curr. Opin. Lipidol. 18 (3): 263–70. DOI:10.1097/MOL.0b013e32814a645f. PMID 17495599.

[pmid14551151-17] Matsuzawa Y, Funahashi T, Kihara S, Shimomura I (January 2004). "Adiponectin and metabolic syndrome". Arterioscler. Thromb. Vasc. Biol. 24 (1): 29–33. DOI:10.1161/01.ATV.0000099786.99623.EF. PMID 14551151.

[pmid15794918-18] Hara K, Yamauchi T, Kadowaki T (April 2005). "Adiponectin: an adipokine linking adipocytes and type 2 diabetes in humans". Curr. Diab. Rep. 5 (2): 136–40. DOI:10.1007/s11892-005-0041-0. PMID 15794918.

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adiponectin