Yavuzkir, Seyda; Ugur, Kader; Deniz, Rulin; Ustebay, Dondu Ulker; Mirzaoglu, Miyase; Yardim, Meltem; Sahin, İbrahim; Baykus, Yakup; Karagoz, Zuhal Karaca; Aydin, Suleyman

Subfatin and spexin are two novel adipokines implicated in glucose homeostasis. This study was designed to investigate changes in blood subfatin and spexin levels during gestational diabetes mellitus (GDM) and childbirth, and define the mechanisms of these hormones in the physiopathology of GDM. A total of 60 pregnant women, comprising 30 diagnosed with GDM and 30 with normal gestation, were included in the study. The diagnosis of GDM was made through a 75-g oral glucose tolerance test (OGTT) administered between 24 and 28 weeks of pregnancy. The amounts of subfatin, spexin, and insulin were measured in blood samples by enzyme-linked immunosorbent assays; lipid profiles, glucose, and other biochemical parameters were measured by using an autoanalyzer. Levels of subfatin and spexin were significantly higher in blood samples drawn at baseline (before OGTT) in mothers with GDM compared to those with normal gestation. Similar observations were made in maternal and cord blood sampled at the end of pregnancy. However, at delivery, the increase in subfatin and spexin concentrations observed at baseline was abrogated in both groups of pregnant women, although levels in mothers with GDM were comparatively higher. These results show that levels of subfatin and spexin increased because of GDM and suggest that these hormones could be potential biomarkers for the diagnosis and management of GDM.

Aydin, Suleyman; Kuloglu, Tuncay; Aydin, Suna; Eren, Mehmet Nesimi; Yilmaz, Musa; Sahin, Ibrahim; Kalayci, Mehmet; Sarman, Emine; Kaya, Nalan; Yilmaz, Osman Fatih

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 24 h 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.

Aydin, Suna; Kuloglu, Tuncay; Aydin, Suleyman; Eren, Mehmet Nesimi; Celik, Ahmet; Yilmaz, Musa; Kalayci, Mehmet; Sahin, Ibrahim; Gungor, Orhan; Gurel, Ali

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 10 min 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.

Aydin, Suleyman; Aydin, Suna; Kuloglu, Tuncay; Yilmaz, Musa; Kalayci, Mehmet; Sahin, Ibrahim; Cicek, Demet

The purpose of this study was to ascertain (1) whether human saliva contains irisin and whether its level correlates with serum irisin concentration, (2) whether salivary glands, eccrine glands and sebaceous glands in human skin produce irisin, (3) how the changes in saliva and serum irisin concentrations after the Turkish bath at 47 ± 3 C compare with the changes caused by moderate exercise in obese and normal weight subjects. Seven obese male subjects and seven normal weight subjects were enrolled for Turkish bath. Seven obese male subjects and seven normal weight subjects were also enrolled for moderate outdoor exercise, and thirteen male normal weight subjects neither exercised nor showered at the Turkish bath. From each participant, 1.5 ml of saliva and 5 ml blood were collected simultaneously before and after the moderate exercise and Turkish bath. Salivary glands and eccrine and sebaceous glands in the skin were screened immunohistochemically for irisin while serum and saliva irisin were measured with an ELISA. Submandibular glands, eccrine glands and sebaceous glands in the human skin showed strong irisin immunoreactivity. Human saliva contained irisin and its level was significantly higher than the serum levels in both obese and normal weight subjects. However, irisin concentrations were more markedly increased in both saliva and serum samples from subjects who had showered at a Turkish bath than in obese subjects who had exercised or in normal weight subjects. Human submandibular glands, eccrine sweat glands and sebaceous glands synthesize irisin.

Aydin, Suleyman; Celik, Onder; Gurates, Bilgin; Sahin, Ibrahim; Ulas, Mustafa; Yilmaz, Musa; Kalayci, Mehmet; Kuloglu, Tuncay; Catak, Zekiye; Aksoy, Aziz

This study was undertaken to ascertain whether human milk contains preptin, salusin-alpha (salusin-α) and -beta (salusin-β) and pro-hepcidin and hepcidin-25, and whether there are relationships between plasma and milk preptin, salusin-α and -β and pro-hepcidin and hepcidin-25 concentrations in lactating mothers with and without gestational diabetes mellitus (GDM). Blood was obtained from non-lactating women (n = 12), non-diabetic lactating women (n = 12), and GDM lactating women (n = 12). Colostrum, transitional milk, and mature milk samples were collected just before suckling from healthy and GDM lactating women. Peptides concentrations were determined by ELISA and EIA. Mammary gland tissues were screened immunohistochemically for these peptides. Women with GDM had significantly higher plasma and colostum preptin concentrations than healthy lactating women during the colostral and transitional milk period. Salusin-alpha and -beta levels in milk and plasma were lower in women with GDM. Salusin-α and -β were significantly lower in both plasma and colostrums of GDM than of healthy lactating women. Women with GDM had significantly higher colostum prohepcidin and hepcidin-25 concentrations than healthy lactating women during the colostral period. Plasma prohepcidin was also higher in women with GDM than in healthy lactating women during the colostral period, but plasma prohepcidin and hepcidin-25 levels decreased during mature milk period. Transitional milk pro-hepcidin and hepcidin-25 levels in women with GDM were higher than in healthy lactating women. All these results revealed that the mammary gland produces those peptides, which were present in milk at levels correlating with plasma concentrations.