Tarçının (Cinnamon) Yüksek Glukoz Konsantrasyonlarına Maruz Bırakılan İnsan Eritrositlerinde (in vitro) Protein Glikozilasyonu, Na+-K+ ATPaz, Ca++ ATPaz ve Lipid Peroksidasyonu Düzeylerine Etkisinin Araştırılması

Yıl 2017, Cilt: 12 Sayı: 3, 22 - 30, 27.12.2017

Nuri Güleşci Naciye Kurtul

https://doi.org/10.17517/ksutfd.350249

Öz

Bu çalışmada,
yüksek glukoz konsantrasyonuna maruz bırakılan insan eritrositlerinde in vitro
ortamda tarçının (Cinnamon) eritrosit membranı Na⁺-K⁺ ATPaz
ve Ca⁺⁺ ATPaz aktiviteleri ile glikozillenmiş hemoglobin (HbA_1c)
ve MDA düzeylerine etkisi araştırılmıştır. Sağlıklı bireylerden toplanan kan
örneklerinden elde edilen eritrositler normal ve yüksek glukoz
konsantrasyonlarına maruz bırakılarak farklı konsantrasyonlardaki tarçın ile
bir saat süresince inkübe edilmiştir. Sadece normal glukoza maruz bırakılan eritrositler
kontrol grubu olarak kullanılmıştır. Yüksek glukoza maruz bırakılan
eritrositlerde Na⁺-K⁺ ATPaz ve Ca⁺⁺ ATPaz
aktiviteleri normal glukoza maruz bırakılan kontrol grubuna göre istatistiki
olarak önemli düzeyde düşük bulunmuştur (p<0.001). Tarçın uygulanan
gruplarda tarçın konsantrasyonlarına da bağlı olarak bu enzimlerin
aktivitelerinin istatistiki olarak önemli düzeyde arttığı saptanmıştır. Yüksek
konsantrasyondaki glukozun etkisi ile MDA ve HbA_1c değerlerinin
normal konsantrasyonda glukoz uygulanan kontrol grubuna göre istatistiki olarak
önemli düzeyde arttığı, tarçının etkisi ile tarçının konsantrasyonlarına da
bağlı olarak MDA ve HbA_1c değerlerinin azaldığı saptanmıştır. Sonuçta,
tarçının eritrositlerde normal glukoz konsantrasyonlarında olduğu gibi yüksek
glukoz konsantrasyonlarında da Na⁺-K⁺ ATPaz ve Ca⁺⁺
ATPaz aktivitelerini artırıcı ve lipid peroksidasyonu ile protein
glikozilasyonunu azaltıcı etkiye sahip olduğu görülmüş, bunun ise yüksek kan
glukozu ile karakterize ve bütün dünyada yaygın bir hastalık olan diabetes
mellitusta özel bir önem arz edebileceği düşünülmüştür.

Anahtar Kelimeler

Tarçın(cinnamon), Na+-K+ ATPaz, Ca++ ATPaz, Lipid Peroksidasyonu, Eritrosit Membranı

In vitro Investigation of the Effect of Cinnamon on Protein Glycosylation, Na+-K+ ATPase, Ca++ ATPase and Lipid Peroxidation in Human Erythrocytes Exposed to High Glucose Concentration

Öz

In this study, the effect of cinnamon on protein
glycosylation, Na⁺-K⁺ ATPase, Ca⁺⁺ ATPase
activities and lipid peroxidation levels in human erythrocytes which exposed to
high glucose concentration in vitro is investigated. For this purpose, the
blood samples obtained from healthy individuals have been exposed to normal
glucose and high glucose concentrations and then incubated with cinnamon at
different concentrations. The samples which exposed to normal glucose
concentration only, are used as a control group. In erythrocyte samples which
have been exposed to high glucose concentration, Na⁺-K⁺
ATPase, Ca⁺⁺ ATPase activities are found lower than those of control
group and the differences between these two groups are statistically
significant (p<0.001). In the groups which have been exposed to cinnamon,
the activities of these two membrane enzymes are increased at a statistically
significant level due to the increase of cinnamon concentrations. It has also
been detected that MDA and HbA_1c levels increase more in high
glucose group than normal glucose group, and they also decrease under the effect
of cinnamon, directly depending on the concentration of applied cinnamon. As a result, cinnamon increase the activities of Na⁺-K⁺
ATPase and Ca⁺⁺ ATPase and decrease the level of lipid peroxidation
in high glucose concentration in erythrocytes, so do in normal glucose
concentrations. It is concluded that the effects of cinnamon on these
parameters have a special importance on diabetes mellitus, a disease known
commonly all over the world, which is characterized by high blood glucose
level.

Anahtar Kelimeler

Cinnamon, Na+-K+ ATPase, Ca++ ATPase, Lipid Peroxidation

Kaynakça

• King GL, Banskota NK. Mechanisms of diabetic microvascular complications. In: Kahn, C.R, Weir GC. eds, Joslin's Diabetes Mellitus. (International Ed. Thirteenth Ed. Companv). 1994; 634-648.
• Maxwell SRJ, Thomason H, Sandler D, Leguen C, Baxter MA, Thorpe GHG, Jones AF, Barnett AH. Poor glycaemic control is associated with reduced serum free radical scavenging (antioxidant) activity in non-insulin-dependent diabetes mellitus. Ann Clin Biochem. 1997; 34:638-644.
• Orei NN, Zidek W, Tepel M. Increased intracellular generation of reactive oxygen species in mononuclear leukocytes from patients with diabetes mellitus type 2. Exp Clin Endocrinol Diabetes. 2000; 108(3):175-80.
• Jain SK, Lim G. Lipoicacid decreases lipid peroxidation and protein glycosylation and increases (Na+, K+ ) and Ca+2 ATPase activities in high glucose-treated human erythrocytes. Free Radical Biology & Medicine. 2000; 11:1122-1128.
• Jain SK, Lim G. Pyridoxine and pyridoxamine inhibits superoxide radicals and prevents lipid peroxidation, protein glycosylation, and Na+, K+ -ATPase activity reduction in high glucose-treated human erythrocytes. Free Radical Biology & Medicine. 2001; 12:595-604.
• Davis FB, Davis PJ, Nat G, Blas SD, Macgillivra M, Gutman S, Feldman MJ. The effect of in vivo glucose administration on human erythrocyte Ca++-ATPase activity and on enzyme responsiveness in vitro to thyroid hormone and calmodulin. Diabetes. 1985; 34(7):639-646.
• Bilgin R. Glukozun Eritrosit Zarlarında Bulunan Na+- K+ ATPaz ve Ca+2 ATPaz Enzim Aktivitelerine Etkisinin İn Vitro ve İn Vivo Koşullarda Araştırılması. Çukurova Üniversitesi Doktora Tezi, Adana. 1995; 100p.
• Kızıltunç A, Akçay F, Polat F, Kuşkay S, Şahin YN. Reduced lecithin: Cholesterol acyltransferase (LCAT) and Na+, K+ -ATPase activity in diabetic patients. Clinical Biochemistry. 1997; 2:177-182.
• Gürbilek M, Dağlar C, Aköz C. The effect of disease duration on of erythrocyte membrane Na+, K+ -ATPase enzyme activity, lipid peroxidation, and DHEA(S), glucose and lipid levels in the diabets mellitus patients. Turk J. of Biochem. 2004; 29(39); 237-242. Khan A, Safdar M, Khan MMA, Khattak KN, Anderson RA. Cinnamon Improves Glucose and Lipids of People With Type 2 Diabetes. Diabetes Care. 2003; 26:3215–3218.
• Bruneton J. Pharmacognosy, Phytochemistry, Medicinal Plants. Lavoisier printing press, Paris. 1995; 509.
• Karnick CR. Pharmacopoeial Standards of Herbal Plants. Sri Satguru printing press, Delhi. 1994; 1138p.
• Kim SH, Hyun SH, Choung SY. Anti-diabetic effect of cinnamon extract on blood glucose in db/db mice. Journal of Ethnopharmacology. 2005; 18:3953-3958
• Kitazuru ER, Moreira AVB, Mancini-Filho J, Delince´e H, Villavicencio ALCH. Effects of irradiation on natural antioxidants of cinnamon (Cinnamomum zeylanicum N.). Radiation Physics and Chemistry. 2004; 71; 37–39.
• Shan B, Cai YZ, Sun M, Corke H. Antioxidant capacity of 26 spices extracts and characterization of their phenolic constituents. J. Agric Food Chem. 2005; 53(20):7749-59.
• Blomhoff R. Antioxidants and oxidative stres. Tidsskr Nor Laegeforen. 2004; 124(12): 1643-5.
• Lopez P, Sanchez C, Batlle R, Nerin C. Solid- and vapour-phase antimicrobial activities of six essential oils: Susceptibility of selected food bourne bacterial and fungal strains. J. Agri Food Chem. 2005; 53(17):6939-46.
• Wichtl M, Bisset, NG. Herbal Drugs and Phytopharmaceuticals. Medpharm Scientific printing press. Stuttgart. 1994; 386p.
• Moretti N, Rabini RA, Nanetti L, Grechi G, Curzi MC, Cester N, Tranquilli LA, Mazzanti L. Sialic acid content in erythrocyte membranes from pregnant women affected by gestational diabetes. Metabolism. 2002; 51(5):605-608.
• Mazzanti L, Rabini RA, Testa I, Bertoli E. Modifications induceed by diabetes on the physicochemical and functional properties of erythrocyte plasma membrane. European J. Clin. Invest. 1989; 19:84-89.
• Flecha FG, Bermudez MC, Cedola NN, Gagliardino JJ, Rossi JP. Febs. Lett. 1990; 244(2):484-486.
• Ames BN. Asay of inorganic phosphate. Methods in Enzymology. Academic Press. 1966; 8:115. Yagi K. Assay for blood plasma or serum. Methods in Enzymolgy. 1984; 105:328-337.
• Jain SK. Hyperglycemia Can Cause Membrane Lipid Peroxidation and Osmatic Fragility in Human Red Blood Cells. Journal of Biological Chemistry. 1989; 264(35):21340-21345.
• Lowry O, Rosenbraugh N, Farr L, Randall R. Protein measurement with theophilin-phenol reagent. J. Biol. Chem. 1951; 183:265–275.