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    Adropin as a potential marker of enzyme-positive acute coronary syndrome
    (Clinics Cardive Publ Pty Ltd, 2017) Aydin, Suna; Eren, Mehmet Nesimi; Yilmaz, Musa; Kalayci, Mehmet; Yardim, Meltem; Alatas, Omer Dogan; Kuloglu, Tuncay
    Aim: Enzyme-positive acute coronary syndrome (EPACS) can cause injury to or death of the heart muscle owing to prolonged ischaemia. Recent research has indicated that in addition to liver and brain cells, cardiomyocytes also produce adropin. We hypothesised that adropin is released into the bloodstream during myocardial injury caused by acute coronary syndrome (ACS), so serum and saliva levels rise as the myocytes die. Therefore, it could be useful to investigate how ACS affects the timing and significance of adropin release in human subjects. Methods: Samples were taken over three days after admission, from 22 EPACS patients and 24 age-and gendermatched controls. The three major salivary glands (submandibular, sublingual and parotid) were immunohistochemically screened for adropin production, and serum and saliva adropin levels were measured by an enzyme-linked immuno-sorbent wassay (ELISA). Salivary gland cells produce and secrete adropin locally. Results: Serum adropin, troponin I, CK and CK-MB concentrations in the EPACS group became gradually higher than those in the control group up to six hours (p < 0.05), and troponin I continued to rise up to 12 hours after EPACS. The same relative increase in adropin level was observed in the saliva. Troponin I, CK and CK-MB levels started to decrease after 12 hours, while saliva and serum adropin levels started to decrease at six hours after EPACS. In samples taken four hours after EPACS, when the serum adropin value averaged 4.43 ng/ml, the receiver operating characteristic curve showed that the serum adropin concentration indicated EPACS with 91.7% sensitivity and 50% specificity, while when the cut-off adropin value in saliva was 4.12 ng/ml, the saliva adropin concentration indicated EPACS with 91.7% sensitivity and 57% specificity. Conclusion: In addition to cardiac troponin and CK-MB assays, measurement of adropin level in saliva and serum samples is a potential marker for diagnosing EPACS.
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    Cardiac, skeletal muscle and serum irisin responses to with or without water exercise in young and old male rats: Cardiac muscle produces more irisin than skeletal muscle
    (Elsevier Science Inc, 2014) Aydin, Suna; Kuloglu, Tuncay; Aydin, Suleyman; Eren, Mehmet Nesimi; Celik, Ahmet; Yilmaz, Musa; Kalayci, Mehmet
    Irisin converts white adipose tissue (WAT) into brown adipose tissue (BAT), as regulated by energy expenditure. The relationship between irisin concentrations after exercise in rats compared humans after exercise remains controversial. We therefore: (1) measured irisin expression in cardiac and skeletal muscle, liver, kidney, peripheral nerve sheath and skin tissues, as also serum irisin level in 10 week-old rats without exercise, and (2) measured tissue supernatant irisin levels in cardiac and skeletal muscle, and in response to exercise in young and old rats to establishing which tissues produced most irisin. Young (12 months) and old rats (24 months) with or without 10min exercise (water floating) and healthy 10 week-old Sprague-Dawley rats without exercise were used. Irisin was absent from sections of skeletal muscle of unexercised rats, the only part being stained being the perimysium. In contrast, cardiac muscle tissue, peripheral myelin sheath, liver, kidneys, and skin dermis and hypodermis were strongly immunoreactivity. No irisin was seen in skeletal muscle of unexercised young and old rats, but a slight amount was detected after exercise. Strong immunoreactivity occurred in cardiac muscle of young and old rats with or without exercise, notably in pericardial connective tissue. Serum irisin increased after exercise, being higher in younger than older rats. Irisin in tissue supernatants (cardiac and skeletal muscle) was high with or without exercise. High supernatant irisin could come from connective tissues around skeletal muscle, especially nerve sheaths located within it. Skeletal muscle is probably not a main irisin source. Copyright (C) 2013 Elsevier Inc. All rights reserved.
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    The cardiovascular system and the biochemistry of grafts used in heart surgery
    (Springer International Publishing Ag, 2013) Aydin, Suna; Aydin, Suleyman; Eren, Mehmet Nesimi; Sahin, Ibrahim; Yilmaz, Musa; Kalayci, Mehmet; Gungor, Orhan
    Blood is pumped into the cardiac muscle through arteries called the coronary arteries. Over time, the accumulation of cholesterol, coagulation factors, and cells on the walls of these arteries causes the walls to thicken and lose their elasticity, resulting in the development of atherosclerosis. When the blood supply of the heart is diminished by atherosclerosis, it can be restored by bypass surgery, in which atherosclerosis-free vein and/ or artery grafts taken from another area of the body are used to replace the atherosclerotic vessels. These biological grafts used in surgery differ in biochemical composition and long-term patency. Although the great saphenous vein (GSV) has been the most popular graft material in revascularization for years, it has recently been superseded by the internal mammarian artery (IMA), which has a lower incidence of recurrence of atherosclerosis. The aim of the present review is briefly to address the structure of the cardiovascular system and blood vessels, and then, in the light recent data, to present the biochemical compositions and individual advantages of the graft materials used to restore an impaired blood supply to the heart.
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    Decreased saliva/serum irisin concentrations in the acute myocardial infarction promising for being a new candidate biomarker for diagnosis of this pathology
    (Elsevier Science Inc, 2014) Aydin, Suna; Aydin, Suleyman; Kobat, Mehmet Ali; Kalayci, Mehmet; Eren, Mehmet Nesimi; Yilmaz, Musa; Kuloglu, Tuncay
    Irisin is a muscle-secreted protein. Cardiac muscle produces more irisin than skeletal muscle in response to acute exercise, and is associated with myocardial infarction (MI) in an experimental model induced by isoproterenol in rats. The timing and significance of its release in patients with acute myocardial infarction (AMI) needs further investigation. We have studied the relationship between serum/saliva irisin concentration and AMI in humans. Serum and saliva samples were taken within 3 days of admission in 11 patients with AMI and in 14 matched controls. Salivary gland irisin was detected immunohistochemically, and serum and saliva levels were measured by ELISA. The three major paired salivary glands (submandibular, sublingual and parotid) produce and release irisin into saliva. Troponin-I, CK, CK-MB concentrations in the AMI group gradually increased from up to 12 h, while saliva and serum irisin gradually decreased from up to 48 h, compared with the control group (P < 0.05). After 12 h, troponin-I, CK, CK-MB started to decrease, while saliva and serum irisin started to increase at 72 h. Serum irisin levels correlated with age, while troponin I, CK-MB, and CK were correlated and with saliva irisin in AMI patients. Besides cardiac troponin and CK-MB, irisin adds new diagnostic information in AMI patients, and the gradual decrease of saliva/serum irisin over 48 h could be a useful biomarker. (c) 2014 Elsevier Inc. All rights reserved.
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    Elevated adropin: A candidate diagnostic marker for myocardial infarction in conjunction with troponin-I
    (Elsevier Science Inc, 2014) Aydin, Suna; Kuloglu, Tuncay; Aydin, Suleyman; Kalayci, Mehmet; Yilmaz, Musa; Cakmak, Tolga; Eren, Mehmet Nesimi
    Myocardial infarction (MI; heart attack) can cause injury to or death of heart muscle tissue (myocardium) owing to prolonged ischemia and hypoxia. Troponins and CK-MB are released from heart muscle cells during MI. It has been demonstrated that energy expenditure is regulated by adropin expressed in the endocardium, myocardium, and epicardium. We hypothesized that adropin is released into the bloodstream during myocardial muscle injury caused by MI, so the serum level rises as myocytes die. Therefore, we examined the association between adropin expression and myocardial infarction in isoproterenol-induced myocardial infarction. Rats were randomly allocated to six groups. After treatment they were decapitated and their blood and tissues were collected for adropin measurement. Changes in adropin synthesis in rat heart, kidney and liver tissues in isoproterenol (ISO)-induced MI were demonstrated immunohistochemically. Serum adropin concentrations were measured by ELISA, and troponin-I, CK and CK-MB concentrations by autoanalysis. The results demonstrated that cardiac muscle cells, glomerular, peritubular and renal cortical interstitial cells, hepatocytes and liver sinusoidal cells all synthesize adropin, and synthesis increased 1-24 h after MI except in the liver cells. The findings elucidate the pathogenesis of MI, and the gradual increase in serum adropin could be a novel diagnostic marker and serve as an alternative to troponin-I measurement for diagnosing MI. (C) 2014 Elsevier Inc. All rights reserved.
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    Expression of adropin in rat brain, cerebellum, kidneys, heart, liver, and pancreas in streptozotocin-induced diabetes
    (Springer, 2013) Aydin, Suleyman; Kuloglu, Tuncay; Aydin, Suna; Eren, Mehmet Nesimi; Yilmaz, Musa; Kalayci, Mehmet; Sahin, Ibrahim
    We have investigated how diabetes affects the expression of adropin (ADR) in rat brain, cerebellum, kidneys, heart, liver, and pancreas tissues. The rats in the diabetic group were administered an intraperitoneal (i.p.) injection of a single dose of 60 mg/kg streptozotocin (STZ) dissolved in a 0.1 M phosphate-citrate buffer (pH 4.5). The rats were maintained in standard laboratory conditions in a temperature between 21 and 23 A degrees C and a relative humidity of 70 %, under a 12-h light/dark cycle. The animals were fed a standard commercial pellet diet. After 10 weeks, the animals were sacrified. ADR concentrations in the serum and tissue supernatants were measured by ELISA, and immunohistochemical staining was used to follow the expression of the hormones in the brain, cerebellum, kidneys, heart, liver, and pancreas tissues. The quantities were then compared. Increased ADR immunoreaction was seen in the brain, cerebellum, kidneys, heart, liver, and pancreas in the diabetes-induced rats compared to control subjects. ADR was detected in the brain (vascular area, pia mater, neuroglial cell, and neurons), cerebellum (neuroglial cells, Purkinje cells, vascular areas, and granular layer), kidneys (glomerulus, peritubular interstitial cells, and peritubular capillary endothelial cells), heart (endocardium, myocardium, and epicardium), liver (sinusoidal cells), and pancreas (serous acini). Its concentrations (based on mg/wet weight tissues) in these tissues were measured by using ELISA showed that the levels of ADR were higher in the diabetic rats compared to the control rats. Tissue ADR levels based on mg/wet weight tissues were as follows: Pancreas > liver > kidney > heart > brain > cerebellar tissues. Evidence is presented that shows ADR is expressed in various tissues in the rats and its levels increased in STZ-induced diabetes; however, this effect on the pathophysiology of the disorder remains to be understood.
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    Irisin: A potentially candidate marker for myocardial infarction
    (Elsevier Science Inc, 2014) Kuloglu, Tuncay; Aydin, Suna; Eren, Mehmet Nesimi; Yilmaz, Musa; Sahin, Ibrahim; Kalayci, Mehmet; Sarman, Emine
    Myocardial infarction (MI) causes energy depletion through imbalance between coronary blood supply and myocardial demand. Irisin produced by the heart reduces ATP production by increasing heat generation. Energy depletion affects irisin concentration in circulation and cardiac tissues, suggesting an association with MI. We examined: (1) irisin expression immunohistochemically in rat heart, skeletal muscle, kidney and liver in isoproterenol (ISO)-induced MI, and (2) serum irisin concentration by ELISA. Rats were randomly allocated into 6 groups (n=6), (i) control, (ii) ISO (1 h), (iii) ISO (2 h), (iv) ISO (4 h), (v) ISO (6 h), and (vi) ISO (24 h), 200 mg ISO in each case. Rats were decapitated and the blood and tissues collected for irisin analysis. Blood was centrifuged at 1792 g for 5 min. Tissues were washed with saline and fixed in 10% formalin for histology. Serum irisin levels gradually decreased from 1 h to 24h in MI rats compared with controls, the minimum being at 2 h, increasing again after 6 h. Cardiac muscle cells, glomerular, peritubular renal cortical interstitial cells, hepatocytes and liver sinusoidal cells and perimysium, endomysium and nucleoi of skeletal muscle were irisin positive, but its synthesis decreased 1-4 h after MI. At all time-points, irisin increased near myocardial connective tissue, with production in skeletal muscle, liver and kidney recovering after 6 h, although slower than controls. Unique insight into the pathogenesis of MI is shown, and the gradually decrease of serum irisin might be a diagnostic marker for MI. (C) 2014 Elsevier Inc. All rights reserved.