Core tip: Diabetes mellitus and related metabolic disorders like . Adiponectin has negative correlation with insulin resistance, along with it. There was a significant inverse correlation between the HOMA–IR and adiponectin/leptin ratio. The adiponectin/leptin ratio was inversely correlated with BMI. Anah tar ke li me ler: Adiponektin, egzersiz, leptin, SF, tip 2 diyabet In this study, the relationship between aerobic exercise and. QOL as.
Epicardial, subcutaneous, and visceral fat can be measured using simple echocardiography, magnetic resonance imaging MRIand multi-slice computed tomography MSCT [ 910 ].
There have been several reports of its clinical associations, especially with CAD [ 11 ]. Similarly, an inverse relationship between adiponectin level and visceral adipose volume measured by computed tomography CT has been reported [ 13 ], while Harada et al.
On the other hand, irisin is a novel hormone secreted by myocytes a myokinethat has been proposed to mediate the beneficial effects of exercise on metabolism.
In human adipocytes, Huh et al. In fact, it has been reported that exercises such as aerobic or resistance exercise increase circulating irisin and decrease fat volume in humans [ 21 — 23 ].
However, there have been conflicting results showing a lack of effect of exercise on circulating irisin [ 24 ].
Furthermore, in contrast with the anti-obesity and metabolic effects of irisin [ 21 — 23 ], irisin has been reported to be involved in the pathogenesis of various complications of obesity, including dyslipidemia, type 2 DM, and metabolic syndrome [ 2526 ].
We have also reported that the circulating irisin concentration is significantly correlated with HOMA-IR in Japanese obese patients [ 27 ]. Thus, it remains uncertain whether irisin exerts anti-obesity effects and decreases adiposity in humans. Therefore, we investigated the relationship between serum irisin concentration and body fat including epicardial fat in patients undergoing cardiovascular surgery, and compared it with adiponectin and leptin, originally known as adipokines [ 2829 ].
Materials and methods Participants From October to Decemberwe evaluated 93 patients undergoing cardiovascular surgery at Dokkyo Medical Hospital. The baseline characteristics of the patients are summarized in Table 1. The mean age was We assessed the co-incidence of conventional risk factors such as hypertension HTdiabetes DMhyperlipidemia HLcurrent smoking, and hemodialysis HD.
Eleven patients were current smokers, and eleven received HD. Forty-two had coronary artery disease 9 patients, one-vessel disease; 4, two-vessel disease, and 29, three-vessel disease. Eleven patients had other valve replacement or repair mitral valve replacement or repair, tricuspid valve repair, replacement or repair.
Fourteen patients received the combination of CABG and valve replacement or repair. Twelve patients had aortic surgery, such as endovascular aneurysm repair EVAR and artificial blood vessel replacement. Three monomers 30 kDa associate together at the globular domain to form the adiponectin trimer, where four to six trimers associate through their collagenous domains to form the high order structure.
Monomeric adiponectin has not been observed in the plasma and it is believed to remain within adipocyte[ 28 ]. Human adiponectin is encoded by the ADIPOQ gene on the chromosomal locus 3q27 consisting three exons and two introns[ 29 ], involved in regulating glucose levels as well as fatty acid breakdown[ 1 ].
Mouse adiponectin is a amino acid long protein where human adiponectin is a protein product of amino acids consisting of four domains, an amino-terminal signal sequence, a variable region, a collagenous domain cAd consisting of 22 Gly-X-Y repeats, and a carboxy-terminal globular domain gAd [ 27 ].
Structure of single-chain globular domain adiponectin sc-gAd is reported Figure 2where globular domain is composed of three part A, B and C respectively[ 30 ]. The adiponectin protein can undergo proteolytic cleavage and can form the globular form of adiponectin, where the globular head domain has been reported to increase the fatty acid oxidation[ 33 ]. Acrp30 is found in two forms in serum; one is low molecular weight LMW trimer-dimer where the other one is high molecular weight complex.
Oligomer formation of Acrp30 depends on the formation of disulfide bond mediated by Cys Mutation of Cys results in the trimers which can easily undergo proteolytic cleavage in the collagenous domain[ 34 ]. Base region of mouse gAd structure where blue arrow determines the N terminus and red arrow determines the C terminus; B: Domain organization of human adiponectin and the sc-gAd, where there are three domains A, B and C respectively.
Adapted from Min et al[ 30 ]. Yamauchi et al[ 35 ] reported for the first time about the two adiponectin receptors which can successfully increase AMP kinase and PPAR-alpha ligand activities as well as can accelerate fatty acid oxidation and glucose uptake by adiponectin.
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These receptors are named as AdipoR1 which is abundantly expressed in skeletal muscle and AdipoR2 which is mainly expressed in the liver Figure 3 [ 3536 ]. They first successfully performed the cloning of complementary DNAs encoding adiponectin receptors 1 and 2 AdipoR1 and AdipoR2 by expression cloning[ 35 ].Boost weight loss success by reseting adiponectin, grhelin, leptin, melatonin - Dr. David Duizer ND
AdipoR1 and AdipoR2 mRNA expression in the liver and skeletal muscle increases after fasting and re-feeding can rapidly restore these to levels equal to the original fed state Figure 4 [ 3536 ]. Both of these receptors contain seven transmembrane domains but they are structurally and functionally completely distinct from G-protein-coupled receptors.
Wild type; AdipoR 2: Apart from negative correlations with measures of adiposity, adiponectin levels are also reduced in association with insulin resistance and type 2 diabetes[ 40 ]. Epidemiological studies in different ethnic groups revealed that low level of plasma adiponectin, especially its HMW form can be an important key factor for type 2 diabetes, hypertension, atherosclerosis and myocardial infarction[ 41 ]. Other than preventing insulin resistance and adipose tissue inflammation, adiponectin has been associated to exert several cardioprotective roles through direct actions on heart as well as on other vascular cells Figure 6 [ 42 ].
Adiponectin has negative correlation with insulin resistance, along with it maintains negative correlation with plasma triglyceride and low density lipoproteins LDLs where it has positive correlation with high density lipoproteins HDLs [ 43 ].
In this review we will try to elucidate the role of adiponectin in acquiring adiposity in various aspects, i. Endothelial progenitor cells; VSMC: Vascular smooth muscles; eNOS: Endothelial nitric oxide synthase.
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Adipocyte derived adiponectin can modulate the functions of cardiomyocytes, endothelial cells, endothelial progenitor cells, macrophages, leukocytes, and vascular smooth muscles in both endocrine and paracrine manner Figure 6. Here we will discuss the possible roles of this adipokine in type 2 diabetes mellitus, obesity and dyslipidemia.
Studies in Japan showed that hypertension has a major effect on atherosclerosis and CVD events in persons with high body mass index with T2DM[ 16 ].
Adiponectin and its association with lipid metabolism and increased obesity are studied well in many populations. Mode of actions of this potential biomarker Adiponectin serves as a central regulatory protein in many metabolic pathways playing crucial role in many metabolic disorders.
Its importance as a potential biomarker in type 2 diabetes is increasing rapidly. As a key factor of the metabolic pathway: Adiponectin has multifunctional roles in metabolic synchronization Figure 7. APPL1 works on Akt which increases Glut4 translocation ultimately elevating glucose uptake of the cell[ 42 ] Figure 7.
Plasma and hemolysate of patients of type 2 diabetes contains elevated level of protein carbonyl content, which indicates increased oxidative stress[ 44 ]. High molecular weight; LMW: Low molecular weight AdipoR1: Peroxisome proliferator-activated receptor gamma; Glut4: Glucose transporter type 4; APPL1: Adaptor protein, phosphotyrosine interaction, pH domain and leucine zipper containing 1; Akt: Protein kinase B; COX2: Adenosine monophosphate-activated protein kinase; PI3K: Tumor necrosis factor alpha; IL: Heat shock protein 90; eNOS: Vascular cell adhesion protein; ICAM: T-cadherin CDH13 localizes adiponectin to the vascular endothelium.
It has been reported that T-cadherin deficiency by siRNA knockdown prevented the ability of adiponectin to promote cellular migration and proliferation[ 45 ]. T-cadherin protects from stress-induced pathological cardiac remodeling by binding with adiponectin and activating its cardioprotective functions in mice[ 46 ].
Adiponectin exhibits two major mechanisms of action by which it inhibits obesity and type 2 diabetes, one by increasing insulin sensitivity and the other way is to increase fatty acid oxidation.
APPL1, stimulated by adiponectin can interact with both adiponectin receptors and can mediate the down-stream events such as lipid oxidation and membrane translocation of glucose transport 4 GLUT4thus increasing glucose uptake Figure 7providing a platform for increased insulin sensitization[ 47 ]. The major form of storing and transporting fatty acids is triglycerides. Adiponectin has been reported to decrease tissue triglyceride content by increasing the expression of CD36, a fatty acid transporter[ 50 ].
Thus, lowering of tissue triglyceride content promotes insulin sensitivity. It has been established that adiponectin enhances insulin-stimulated IRS-1 tyrosine and Akt phosphorylation.
Other than playing a crucial role as an insulin sensitizer, adiponectin also defeats obesity and obesity onset type 2 diabetes by increasing fatty acid oxidation.
Increased fatty acid oxidation in turn also elevates insulin sensitivity. As stated earlier, adiponectin associated activation of AMPK phosphorylation which in turn implements major role in fatty acid oxidation. It has been studied in humans that LDL activity is correlated positively with plasma adiponectin level, thus LPL may represent a link between low adiponectin levels and dyslipidemia in both nondiabetic individuals and patients with type 2 diabetes[ 55 ] where plasma TGs is negatively correlated with LDL activity and positively with diabetic state[ 56 ].