Investigation of angiogenic factors in obese rats exposed to low oxygen pressure

Main Article Content

Meral Dağ
Muhittin Yürekli


Objective: Obesity, which is one of the most important health problems of today's people, remains current due to the risks of illness it brings due to the increase rate in the world.

Material and Methods: Male Sprague Dawley rats were used in our study of obesity. Rats were divided into four groups as standard diet/ normal oxygen, standard diet/low oxygen, high-fat diet/normal oxygen and high-fat diet / low oxygen. For the study, a special cage with a low oxygen level of 17-18% was made in a closed system. After achieving the desired 25% weight increase in obese group rats, blood, liver, lung, white adipose tissue and brown adipose tissue were obtained from the rats. In these tissues, adrenomedullin, hypoxic inducible factor 1-α (HIF1-α) and matrix metalloproteinase-II (MMP-II) levels were measured by ELISA.

Results: According to our results, there was a significant increase in adrenomedullin, HIF1-α and MMP-II in white adipose tissue, and adrenomedullin and MMP-II in brown adipose tissue. It was found that the amount of HIF1-α increased significantly in liver and lung tissues.

Conclusion: According to the metabolic status of adipose tissue, it is thought that the effect of adrenomedullin, HIF1-α and MMP-II can increase vascularization of brown adipose tissue and provide energy consumption.


Download data is not yet available.

Article Details

How to Cite
Dağ, M., & Yürekli, M. (2020). Investigation of angiogenic factors in obese rats exposed to low oxygen pressure . Medical Science and Discovery, 7(3), 426–430.
Research Article
Received 2020-02-13
Accepted 2020-03-13
Published 2020-03-21


Stoll, BJ, Kliegman RM. Hypoxia-Ischemia, In: RE. Behrman, RM. Kliegman, HB. Jenson, Nelson Textbook of Pediatrics, 17th ed. Philadelphia WB Saunders Co; 2004; 566.

World Health Organisation. Obesity: Preventing and Managing the Global Epidemic, Report of a WHO Consultation on Obesity. Geneva, World Health Organ Techn Rep Ser. 2000; 894: 1-253.

Raine JE, Donaldson MDC, Gregory JW, et al. Obesity, In: J.E. Raine, M. D. C. Donaldson, J. W. Gregory, M. O. Savage (eds), Practical Endocrinology and Diabetes in Children. United Kingdom: Blackwell Science. 2001; 161-171.

Blüher M. Professor in Molecular Endocrinology, Adipose tissue dysfunction contributes to obesity related metabolic diseases. Best Practice & Research Clinical Endocrinology & Metabolism. 2013; 27: 168-177.

Donohoue PA. Obesity. In: Behrman RE, Kliegman RM, Jenson HB, Nelson Textbook of Pediatrics 17 th ed. Philadelphia: W.B. Saunders. 2004; 173-177.

National Institutes of Health, National Heart, Lung. And Blood Institute. Clinical guidelines on the idendification, evaluation, and treatment of overweight and obesity in adults-in evidence report. Obes Res. 1998; 51-209.

Christiaens V, Lijnen HR. Angiogenesis and development of Adipose tissue. Mol Cell Endocrinol. 2010; 318: 2-9.

Dahlman I, Elsen M, Tennagels N. 2012. Functional annotation of the human fat cell secretome. Arch Physiol Biochem. 2012; 118: 84-91.

van Gaal LFV, Mertens IL, De Block CE. Mechanisms linking obesity with cardiovascular disease. Nature. 2006; 444: 875-880.

Blüher M. Adipose tissue dysfunction in obesity. Exp Clin Endocrinol Diabetes. 2009; 117: 241-250.

Blüher M. Clinical relevance of adipokines. Diabetes Metab J. 2012; 36: 317-327.

Folkman J, Klagsbrun M. Angiogenic factors. Science. 1987; 235: 442-447.

Yin L, Changtao J, Xian W, et al. 2007. Adrenomedullin is a novel adipokine: Adrenomedullin in adipocytes and Adipose tissues. Peptides. 2007; 28: 1129-1143.

Paulmyer-Lacroix O, Desbriere R, Poggi M, et al. Expression of adrenomedullin adipose tissue of lean and obese women. Eur J Endocrinol. 2006; 155:177-185.

Oliver KR, Kane SA, Salvatore CA, et al. Cloning, characterization and central nervous system distribution of receptor activity modifying proteins in the rat. Eur J Neurosci. 2001; 14: 618-628.

Berra E, Benizri E, Ginouves A, et al. HIF prolylhydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia. EMBO J 2003; 22: 4082-4090.

Schofield CJ, Ratcliffe PJ. Oxygen sensing by HIF hydroxylases. Nat Rev Mol Cell Biol. 2004; 5: 343-354.

Magnus B, Daniel FJK, Stefan A. Matrix Metalloproteinases in Atherothrombosis, Prog Cardiovasc Dis. 2010; 52: 410-428.

Hopps E, Caimi G. Matrix Metalloproteinases in metabolic syndrome. Eur J Intern Med. 2012; 23: 99-104.

Shibasaki I, Nishikimi T, Mochizuki Y, et al. Greater expression of inflammatory cytokines, adrenomedullin, and natriuretic peptide receptor-C in epicardial adipose tissue in coronary artery disease. Regulatory Peptids. 2010; 165 (2,3): 210-217.

Chakravarty P, Suthar TP, Coppcok HA, et al. CGRP and adrenomedullin binding correlates with transcript levels for Calcitonin Receptor-Like Receptor (CRLR) and Receptor Activity Modifying Proteins (RAMPs) in rat tissues. British Journal of Pharmacology. 2000; 130 (1): 189-195.

Peter J. The etiology and pharmacologic approach to hypoxic-ischemic encephalopathy in the newborn. Neo Rewiews. 2002;3(6): 99-106.