Immunohistochemical distribution of irisin in the lung and tongue of Porcupine (Hystrix cristata)

DOI: 10.18805/ijar.11473    | Article Id: B-525 | Page : 537-540
Citation :- Immunohistochemical distribution of irisin in the lungand tongue of Porcupine (Hystrix cristata) .Indian Journal Of Animal Research.2017.(51):537-540

F.M. Gur, S. Timurkaan*, M. H. Yalcin and B. Gencer Tarakci

histolog44@gmail.com
Address :

Department of Histology and Embryology, Faculty of Veterinary Medicine, Firat University, Elazig.

Submitted Date : 9-05-2016
Accepted Date : 2-07-2016

Abstract

Irisin, a novel peptide, was first identified in skeletal muscle cells. It is an exercise protein that is secreted into the bloodstream, through which it reached the white adipose tissue, and interacted with an unknown receptor and cause fat destruction by converting the white adipose tissue to brown adipose tissue. The presence of irisin immunoreactivity in porcupine lung and tongue was studied. In lung, irisin immunoreactivity was found in type II pneumocytes, bronchus, bronchioles and blood vessel. Positive irisin immunostaining was also detected in the lamina epithelialis, striated muscle cells and serous glands in porcupine’s tongue. The function of locally synthesized irisin is currently unknown. Therefore, further study is required to reveal the precise effect of irisin.

Keywords

Immunoreactivity Irisin Lung Porcupine Tongue.

References

  1. Affourtit, C., Quinlan, C.L., Brand, M.D. (2012) Measurement of proton leak and electron leak in isolated mitochondria. Methods. Mol. Biol., 810:165–82.
  2. Aydin, S. (2014) Three new players in energy regulation: preptin, adropin and irisin. Peptides, 56:94–110.
  3. Aydin, S., Aydin, S., Kuloglu, T., Yilmaz, M., Kalayci, M., Sahin, I., Cicek, D. (2013) Alterations of irisin concentrations in saliva and serum of obese and normal-weight subjects, before and after 45 min of a Turkish bath or running. Peptides, 50:13–18.
  4. Aydin, S., Kuloglu, T., Aydin, S., Eren, M.N., Celik, A., Yilmaz, M., Kalayci, M., Sahin, I., Gungor, O., Gurel, A., Ogeturk, M., Dabak, O. (2014a) 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. Peptides, 52:68–73.
  5. Aydin, S., Kuloglu, T., Aydin, S., Kalayci, M., Yilmaz, M., Cakmak, T., Albayrak, S., Gungor, S., Colakoglu, N., Ozercan, I.H. (2014b) A comprehensive immunohistochemical examination of the distribution of the fat-burning protein irisin in biological tissues. Peptides, 61:130-136.
  6. Aydin, S., Ogeturk, M., Kuloglu, T., Kavakli, A., Aydin, S. (2015). Effect of carnosine supplementation on apoptosis and irisin, total oxidant and antioxidants levels in the serum, liver and lung tissues in rats exposed to formaldehyde inhalation. Peptides, 64:14 –23.
  7. Boström, P., Wu, J., Jedrychowski, M.P., Korde, A., Ye, L., Lo, J.C., Rasbach, K.A., Boström, E.A., Choi, J.H., Long, J.Z., Kajimura, S., Zingaretti, M.C., Vind, B.F., Tu, H., Cinti, S., Højlund, K., Gygi, S.P., Spiegelman, B.M. (2012) A PGC1-b-dependent myokine that drives brown-fat-like development of white fat and thermogenesis. Nature, 481:463-468.
  8. Dun, S.L., Lyu, R.M., Chen, Y.H., Chang, J.K., Luo, J.J., Dun, N.J. (2013) Irisin-immunoreactivity in neural and non-    neural cells of the rodent. Neuroscience, 240:155-162.
  9. Gençer Tarakçi, B., Girgin, A., Gür, F.M., Timurkaan, S., Yalçin, M.H., Karan, M. (2016) Immunohistochemical localization of irisin in skin, eye, thyroid and pineal glands of crested porcupine (Hystrix cristata). Biotechnic&Histochemistry, Doi:10.1080/10520295.2016.1183820.
  10. Huh, J.Y., Panagiotou, G., Mougios, V., Brinkoetter, M., Vamvini, M.T., Schneider, B.E., Mantzoros, C.S. (2012) FNDC5 and irisin in humans: I. Predictors of circulating concentrations in serum and plasma and II. mRNA expression and circulating concentrations in response to weight loss and exercise. Metabolism, 61:1725-1738.
  11. Jastroch, M., Divakaruni, A.S., Mookerjee, S., Treberg, J.R., Brand, M.D. (2010) Mitochondrial proton and electron leaks. Essays. Biochem., 47:53–67.
  12. Kuloglu, T., Aydin, S., Eren, M.N., Yilmaz, M., Sahin, I., Kalayci, M., Sarman, E., Kaya, N., Yilmaz, O.F., Turk, A., Aydin, Y., Yalcin, M.H., Uras, N., Gurel, A., Ilhan, S., Gul, E. (2014) Irisin: a potentially candidate marker for myocardial infarction. Peptides, 55:85–91.
  13. Moreno-Navarrete, J.M., Ortega, F., Serrano, M., Guerra, E., Pardo, G., Tinahones, F., WifredoRicart, W., Fernández-Real, J.M. (2013) Irisin is expressed and produced by human muscle and adipose tissuein association with obesity and insulin resistance. J. Clin. Endocrinol. Metab., 98:E769–78.
  14. Pedersen, B.K., Steensberg, A., Fischer, C., Keller, C., Keller, P., Plomgaard, P., Febbraio, M. and Saltin, B. (2003) Searching for the exercise factor: is IL-6 a candidate? J. Muscle Res. Cell Motil., 24:113–119.
  15. Pekkala, S., Wiklund, P.K., Hulmi, J.J., Ahtiainen, J.P., Horttanainen, M., Pollanen, E., Makela, K.A., Kainulainen, H., Hakkinen, K., Nyman, K., Alen, M., Herzig, K.H. Cheng, S. (2013) Are skeletal muscle FNDC5 gene expression and irisin release regulated by exercise and related to health? J. Physiol., 591:5393–400.
  16. Polak, J.M., Van Noorden, S. (1997) Introduction to immunocytochemistry. Second edition. BIOS, Scientific Publishers, Oxford, UK. 137pp.
  17. Roca-Rivada, A., Castelao, C., Senin, L.L., Landrove, M.O., Baltar, J., Belén, C., Seoane, L.M., Casanueva, F.F., Pardo, M. (2013) FNDC5/irisin is not only a myokine but also an adipokine. PLoS ONE 8:e60563.
  18. Schumacher, M.A., Chinnam, N., Ohashi, T., Shah, R.S., Erickson, H. (2013) Structure of irisin reveals a novel intersubunit beta-sheet fibronectin (FNIII) dimer; implications for receptor activation. J. Biol.Chem., 288: 33738 – 33744.
  19. Zhang, Y., Li, R., Meng, Y., Li, S., Donelan, W., Zhao, Y., Qi, L., Zhang, M., Wang, X., Cui, T., Yang, L.J., Tang, D. (2014) Irisin stimulates browning of white adipocytes through mitogen-activated protein kinase p38 MAP kinase and ERK MAP kinase signaling. Diabetes, 63:514–25.

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