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The effect of some transition metal ions (Mn+2, Co+2, Fe+2) on paraoxonase enzyme activity (E.C.3.1.8.1.) in bonito (Sarda sarda)

Yıl 2022, Cilt: 8 Sayı: 1, 23 - 30, 25.06.2022

Çiğdem Kırsüleymanoğlu , Dilek Çelikler

Öz

In this study, it was aimed to determine the effects of transition metal ions of manganese (Mn+2), cobalt (Co+2) and iron (Fe+2) on paraoxonase (PON) enzyme in the muscle tissue of bonito. Research is located in the north of Turkey from the Black Sea obtained 25 pieces of bonito derived from fish muscle tissue is used. Solutions of Mn, Co and Fe transition metals as MnCl2, CoCl2 and FeCl2 were prepared to be used in analysis. PON enzyme activity was determined by taking different volumes of these solutions. As a result of the obtained data, the enzyme activities of Mn+2, Co+2 and Fe+2 transition metal ions were calculated and percentage activity graphs were drawn. As a result of the research, it was determined that transition metal ions Mn+2, Co+2 and Fe+2 decreased PON enzyme activity in bonito fish. In addition, One Way Analysis of Variance (One-Way Anova) was performed to statistically demonstrate the effect of different concentrations of MnCl2, CoCl2 and FeCl2 solutions on the PON enzyme activity. As a result of the analysis, it was determined that the effects of different concentrations of each solution on PON enzyme activity did not show a statistically significant difference.

Anahtar Kelimeler

bonito cobalt iron manganese heavy metal ion Paraoxonase

Destekleyen Kurum

BAP

Proje Numarası

PYO.EGF.1904.19.006.

Kaynakça

  • Aksun, F.Y. (1986). Heavy metal accumulation in pike fish (Esox lucius, 1758) living in Karamık Lake. VIII. National Biology Congress, İzmir 2: 454-461. Doi.org/10.29048/makufebed.411888
  • Beyaztaş, S., Türker, D., Sinan, S., and Arslan, O. (2007). Investigation of the inhibition effect of Cyprinus carpio paraoxonase enzyme with some heavy metals, 21st National Chemistry Congress, Malatya, 23-27. https://dergipark.org.tr/tr/pub/fufbd/issue/39198/461290
  • Carey, J., Diana, M., Shih, S., et al. (2005). The paraoxonase gene family and atherosclerosis. Free Radic Biol Med, 38(2):153–163. Doi.10.1016/j.freeradbiomed.2004.09.035.
  • Costa, L.G., Li, W.F., Richter, R.J., et al. (1999). Shih DM, Lusis A, Furlong CE. The role of paraoxonase (PON 1) in the detoxication of organophosphates and its human polymorphism. Chem Biol Int, 119-120:429. Doi: 10.1016/s0009-2797(99)00055-1.
  • Chemnitus, J.M., Losch, H., Losch, K., et al. (1983). Organophasphate detoxicating hydrolases in different vertebrate species. Com Biochem Physiol, 6C:85. doi: 10.1016/0742-8413(83)90048-8.
  • Clendenning, J.B., Humbert, R., Green, E.D., et al. (1996). Structural organization of the human PON1 gene. Genom, 35:586. Doi: 10.1006/geno.1996.0401 .
  • Çelik, N. (2012). Anova models of robust statistical inference and applications using skew distributions, Ankara University, Graduate School of Science, Ankara, Master Thesis.
  • Çiftçi, M., Küfrevioğlu, Ö.İ., Gündoğdu, M., Özmen, İ. (2000). Effects of some antibiotics on enzyme activity of glucose-6-phosphate dehydrogenase from human erythrocyte. Pharmacol Res, 41:109. https://www.agriculturejournals.cz/publicFiles/61658.pdf
  • Debord, J., Dantoine, T., Bollinger, J.C., Abraham, M.H., et al. (1998). Inhibition of aryesterase by aliphatic alcohols. Chem Biol Int, 113:105-115. Doi: 10.1007/s12041-017-0741-7.
  • Debord, J., Bollinger, J.C., Merle, L., Dantoine, T. (2003). Inhibition of human serumarylesterase by metal chlorides. J Inorg Biochem, 94:1-4. Doi: 10.1016/s0162-0134(02)00627-x.
  • Del Valls TA, Blasco J, Sarasquete M.C et al. (1998). Forja JM ve Gomez-Parra A. Evaluation of heavy metal sediment toxicity in littoral ecosystems using juveniles of the fish sparus aurata. Ecotoxicol Environ Saf, 41:157-167.
  • Dedeoğlu, N., Arslan, M., Erzengin, M. (2014). Purification of Holstein Bull Semen Paraoxonase 1 (PON1) by Hydrophobic Interaction Chromatography and Investigation of Its Inhibition Kinetics by Heavy Metals. Biol Trace Elem Res, 158:29–35 . Doi: 10.1007/s12011-014-9916-8
  • Deveci, H.A., Kaya, İ., Yılmaz, M and Karapehlivan, M. (2015). Effect of zinc sulphate on the levels of plasma paraoxonase activity, total oxidant and high density lipoprotein of transcaucasian barb (Capoeta capoeta Guldenstaedt, 1773). Fresen Environ Bull, 24(9):2732-2735.
  • Durrington, P.N., Mackness, B., Mackness, M.I. (2001). Paraoxonase and atherosclerosis. Arterioscler Thromb Vasc Biol, 21:473-80. Doi.org/10.1161/01.ATV.21.4.473
  • Elana, T., Elana, M., Magdalena, G., Isabel, L., Ana, M.P. (2006). Effects of caloric restriction and gender on rat serum paraoxonase1 activity. J Exerc Nutr Biochem, 17:197-203. Doi: 10.1016/j.jnutbio.2005.07.004
  • Erol, K., Gençer, N., Arslan, M., Arslan, O. (2012). Purification, characterization, and investigation of in vitro inhibition by metals of paraoxonase from different sheep breeds. Artificial Cells, Nanomedicine, and Biotechnology, 41(2):1255-130. Doi: 10.3109/10731199.2012.696065
  • Fuhrman, B., Khateeb, J., Nitzan, O., et al. (2008). Urokinase plasminogen activator upregulates paraoxonase2 expression in macrophages via an NADPH oxidase-dependent mechanism. Arterioscler Thromb Vasc Biol, 1361-1367.
  • Furlong, C.E., Richter, R.J., Chapline, C., et al.(1991). Purification of rabbit and human serum paraoxonase. Biochem, 30:10133. Doi: 10.1021/bi00106a009.
  • Gonzalvo, M.C., Gil, F., Hernandez, F., et al.(1997). Inhibition of paraoxonase activity in human liver microsomes by exposura to EDTA, metals and mercurials. Chem Biol Interact , 105:169-179. Doi: 10.1016/s0009-2797(97)00046-x.
  • Gülcü, F., Gürsu, M.F. (2003). Standardization of paraoxonase and arylesterase activity measurements. J Biochem, 28 (2): 45-49.
  • Güller, U., Taşer, P., Çiftci, M., Küfrevioğlu, Ö.İ. (2014). Purification of Glutathione S-Transferase From Bonito (Sarda Sarda) Liver And Investigation of Metal Ions Effects on Enzyme Activity. Hacettepe J Biol Chem, 42(3):435-442
  • Janka, Z., Juhász, A., Rimanóczy, A.A., et al. (2002). Codon 311 polymorphism of paraoxonase2 gene is associated with apolipoprotein E4 allele in both alzheimer's and vascular dementias. Mol Psychiatry, 7(1):110-2. Doi: 10.1038/sj.mp.4000916.
  • Köse, E., Uysal K. (2008). Comparison of heavy metal accumulation rates in the muscles, skin and gills of the scaled carp (Cyprinus carpio L., 1758), which has not reached maturity. Dumlupınar University Institute of Science, Kütahya, Master Thesis.
  • La, Du, B.N., Aviram, M., Billecke., S et al. (1999). Navab M, Primo-Parmo S, Sorenson RC, Standiford TJ. On the physioogical role(s) of the paraoxonases. Chem Biol Int, 379:119-120.
  • Mackness, B., Mackness, M. (2004). Paraoxonase 1: biochemistry and contribution to atherosclerosis. University International Congress Series, 1262:91– 94. Doi:10.1016/S0531-5131(03)01736-9
  • Pla, L., Rodrigo, A.F., Hernandez, F., et al. (2007). Effect of metal ions and calcium on purified PON1 and PON3 from rat liver. Chem Biol Interact, 167 63–70. Doi: 10.1016/j.cbi.2007.01.006.
  • Pellin, MC., Moretto, A., Lotti, M., et al. (1990). Distribution and biochemical properties of rat paraoxonase activity. Neurotoxicol Teratol, 12,611614. Doi: 10.1016/0892-0362(90)90071-j.
  • Roest, M. (2008). PON1 Genotypes and Coronary Heart Disease. Laboratory for Clinical Chemistry and Haematology. In: Mackness B, Mackness M, Aviram M, Paragh G (Eds.). The Paraoxonases: their role in disease development and xenobiotic metabolism. Netherlands: Springer, 139-147. Doi:10.1007/978-1-4020-6561-3_15.
  • Sayın D, Türker Çakır D, Gençer N, Arslan O.(2012). Effects of some metals on paraoxonase activity from shark (Scyliorhinuscanicula). J Enzyme Inhib Med Chem, 27(4):595-598. Doi: 10.3109/14756366.2011.604320.
  • Shiner, M., Fuhrman, B., Aviram, M. (2006). A biphasic U-shape effect of cellular oxidative stress on the macrophage antioxidant paraoxonase2 (PON2) enzymatic activity. Biochem Biophys Res Communat, 349:1094-1099. Doi: 10.1016/j.bbrc.2006.08.150.
  • Türkmen, M., Ciminli, C. (2007). Determination of metals in fish and mussel species by inductively coupled plasma-atomic emission spectrometry. Food Chem, 103:670-675.
  • Wildi, W., Domink, J., Thomas, RL., et al. (2004). River, reservoir and lake sediment contamination by heavy metals downstream from urban areas of switzerland. Lakes & Reservoirs: Res Manag, 9:75-87. Doi.org/10.1111/j.1440-1770.2004.00236.x

The Effect of Some Transition Metal Ions (Mn+2, Co+2, Fe+2) on Paraoxonase Enzyme Activity in Bonito (Sarda sarda)

Yıl 2022, Cilt: 8 Sayı: 1, 23 - 30, 25.06.2022

Çiğdem Kırsüleymanoğlu , Dilek Çelikler

Öz

Bu çalışmada, manganez (Mn+2), kobalt (Co+2) ve demir (Fe+2) geçiş metal iyonlarının palamut (S.Sarda) kas dokusundaki paraoksonaz (PON) enzimi üzerine etkilerinin belirlenmesi amaçlanmıştır. sarda). Araştırmada Türkiye'nin kuzeyinde Karadeniz'den elde edilen 25 adet palamut (S. sarda) balık kasından elde edilen doku kullanılıyor. Analizlerde kullanılmak üzere Mn, Co ve Fe geçiş metallerinin MnCl2, CoCl2 ve FeCl2 çözeltileri hazırlanmıştır. Bu çözeltilerin farklı hacimleri alınarak PON enzim aktivitesi belirlendi. Elde edilen veriler sonucunda Mn+2, Co+2 ve Fe+2 geçiş metal iyonlarının enzim aktiviteleri hesaplanmış ve yüzde aktivite grafikleri çizilmiştir. Araştırma sonucunda palamut (S. sarda) balıklarında geçiş metal iyonları Mn+2, Co+2 ve Fe+2'nin PON enzim aktivitesini azalttığı belirlendi. Ayrıca, farklı konsantrasyonlarda MnCl2, CoCl2 ve FeCl2 çözeltilerinin PON enzim aktivitesi üzerindeki etkisini istatistiksel olarak göstermek için Tek Yönlü Varyans Analizi (Tek Yönlü Anova) yapıldı. Analiz sonucunda her bir çözeltinin farklı konsantrasyonlarının PON enzim aktivitesi üzerindeki etkilerinin istatistiksel olarak anlamlı bir farklılık göstermediği belirlendi.

Anahtar Kelimeler

kobalt demir mangan paraoksonaz ağır metal iyon

Proje Numarası

PYO.EGF.1904.19.006.

Kaynakça

  • Aksun, F.Y. (1986). Heavy metal accumulation in pike fish (Esox lucius, 1758) living in Karamık Lake. VIII. National Biology Congress, İzmir 2: 454-461. Doi.org/10.29048/makufebed.411888
  • Beyaztaş, S., Türker, D., Sinan, S., and Arslan, O. (2007). Investigation of the inhibition effect of Cyprinus carpio paraoxonase enzyme with some heavy metals, 21st National Chemistry Congress, Malatya, 23-27. https://dergipark.org.tr/tr/pub/fufbd/issue/39198/461290
  • Carey, J., Diana, M., Shih, S., et al. (2005). The paraoxonase gene family and atherosclerosis. Free Radic Biol Med, 38(2):153–163. Doi.10.1016/j.freeradbiomed.2004.09.035.
  • Costa, L.G., Li, W.F., Richter, R.J., et al. (1999). Shih DM, Lusis A, Furlong CE. The role of paraoxonase (PON 1) in the detoxication of organophosphates and its human polymorphism. Chem Biol Int, 119-120:429. Doi: 10.1016/s0009-2797(99)00055-1.
  • Chemnitus, J.M., Losch, H., Losch, K., et al. (1983). Organophasphate detoxicating hydrolases in different vertebrate species. Com Biochem Physiol, 6C:85. doi: 10.1016/0742-8413(83)90048-8.
  • Clendenning, J.B., Humbert, R., Green, E.D., et al. (1996). Structural organization of the human PON1 gene. Genom, 35:586. Doi: 10.1006/geno.1996.0401 .
  • Çelik, N. (2012). Anova models of robust statistical inference and applications using skew distributions, Ankara University, Graduate School of Science, Ankara, Master Thesis.
  • Çiftçi, M., Küfrevioğlu, Ö.İ., Gündoğdu, M., Özmen, İ. (2000). Effects of some antibiotics on enzyme activity of glucose-6-phosphate dehydrogenase from human erythrocyte. Pharmacol Res, 41:109. https://www.agriculturejournals.cz/publicFiles/61658.pdf
  • Debord, J., Dantoine, T., Bollinger, J.C., Abraham, M.H., et al. (1998). Inhibition of aryesterase by aliphatic alcohols. Chem Biol Int, 113:105-115. Doi: 10.1007/s12041-017-0741-7.
  • Debord, J., Bollinger, J.C., Merle, L., Dantoine, T. (2003). Inhibition of human serumarylesterase by metal chlorides. J Inorg Biochem, 94:1-4. Doi: 10.1016/s0162-0134(02)00627-x.
  • Del Valls TA, Blasco J, Sarasquete M.C et al. (1998). Forja JM ve Gomez-Parra A. Evaluation of heavy metal sediment toxicity in littoral ecosystems using juveniles of the fish sparus aurata. Ecotoxicol Environ Saf, 41:157-167.
  • Dedeoğlu, N., Arslan, M., Erzengin, M. (2014). Purification of Holstein Bull Semen Paraoxonase 1 (PON1) by Hydrophobic Interaction Chromatography and Investigation of Its Inhibition Kinetics by Heavy Metals. Biol Trace Elem Res, 158:29–35 . Doi: 10.1007/s12011-014-9916-8
  • Deveci, H.A., Kaya, İ., Yılmaz, M and Karapehlivan, M. (2015). Effect of zinc sulphate on the levels of plasma paraoxonase activity, total oxidant and high density lipoprotein of transcaucasian barb (Capoeta capoeta Guldenstaedt, 1773). Fresen Environ Bull, 24(9):2732-2735.
  • Durrington, P.N., Mackness, B., Mackness, M.I. (2001). Paraoxonase and atherosclerosis. Arterioscler Thromb Vasc Biol, 21:473-80. Doi.org/10.1161/01.ATV.21.4.473
  • Elana, T., Elana, M., Magdalena, G., Isabel, L., Ana, M.P. (2006). Effects of caloric restriction and gender on rat serum paraoxonase1 activity. J Exerc Nutr Biochem, 17:197-203. Doi: 10.1016/j.jnutbio.2005.07.004
  • Erol, K., Gençer, N., Arslan, M., Arslan, O. (2012). Purification, characterization, and investigation of in vitro inhibition by metals of paraoxonase from different sheep breeds. Artificial Cells, Nanomedicine, and Biotechnology, 41(2):1255-130. Doi: 10.3109/10731199.2012.696065
  • Fuhrman, B., Khateeb, J., Nitzan, O., et al. (2008). Urokinase plasminogen activator upregulates paraoxonase2 expression in macrophages via an NADPH oxidase-dependent mechanism. Arterioscler Thromb Vasc Biol, 1361-1367.
  • Furlong, C.E., Richter, R.J., Chapline, C., et al.(1991). Purification of rabbit and human serum paraoxonase. Biochem, 30:10133. Doi: 10.1021/bi00106a009.
  • Gonzalvo, M.C., Gil, F., Hernandez, F., et al.(1997). Inhibition of paraoxonase activity in human liver microsomes by exposura to EDTA, metals and mercurials. Chem Biol Interact , 105:169-179. Doi: 10.1016/s0009-2797(97)00046-x.
  • Gülcü, F., Gürsu, M.F. (2003). Standardization of paraoxonase and arylesterase activity measurements. J Biochem, 28 (2): 45-49.
  • Güller, U., Taşer, P., Çiftci, M., Küfrevioğlu, Ö.İ. (2014). Purification of Glutathione S-Transferase From Bonito (Sarda Sarda) Liver And Investigation of Metal Ions Effects on Enzyme Activity. Hacettepe J Biol Chem, 42(3):435-442
  • Janka, Z., Juhász, A., Rimanóczy, A.A., et al. (2002). Codon 311 polymorphism of paraoxonase2 gene is associated with apolipoprotein E4 allele in both alzheimer's and vascular dementias. Mol Psychiatry, 7(1):110-2. Doi: 10.1038/sj.mp.4000916.
  • Köse, E., Uysal K. (2008). Comparison of heavy metal accumulation rates in the muscles, skin and gills of the scaled carp (Cyprinus carpio L., 1758), which has not reached maturity. Dumlupınar University Institute of Science, Kütahya, Master Thesis.
  • La, Du, B.N., Aviram, M., Billecke., S et al. (1999). Navab M, Primo-Parmo S, Sorenson RC, Standiford TJ. On the physioogical role(s) of the paraoxonases. Chem Biol Int, 379:119-120.
  • Mackness, B., Mackness, M. (2004). Paraoxonase 1: biochemistry and contribution to atherosclerosis. University International Congress Series, 1262:91– 94. Doi:10.1016/S0531-5131(03)01736-9
  • Pla, L., Rodrigo, A.F., Hernandez, F., et al. (2007). Effect of metal ions and calcium on purified PON1 and PON3 from rat liver. Chem Biol Interact, 167 63–70. Doi: 10.1016/j.cbi.2007.01.006.
  • Pellin, MC., Moretto, A., Lotti, M., et al. (1990). Distribution and biochemical properties of rat paraoxonase activity. Neurotoxicol Teratol, 12,611614. Doi: 10.1016/0892-0362(90)90071-j.
  • Roest, M. (2008). PON1 Genotypes and Coronary Heart Disease. Laboratory for Clinical Chemistry and Haematology. In: Mackness B, Mackness M, Aviram M, Paragh G (Eds.). The Paraoxonases: their role in disease development and xenobiotic metabolism. Netherlands: Springer, 139-147. Doi:10.1007/978-1-4020-6561-3_15.
  • Sayın D, Türker Çakır D, Gençer N, Arslan O.(2012). Effects of some metals on paraoxonase activity from shark (Scyliorhinuscanicula). J Enzyme Inhib Med Chem, 27(4):595-598. Doi: 10.3109/14756366.2011.604320.
  • Shiner, M., Fuhrman, B., Aviram, M. (2006). A biphasic U-shape effect of cellular oxidative stress on the macrophage antioxidant paraoxonase2 (PON2) enzymatic activity. Biochem Biophys Res Communat, 349:1094-1099. Doi: 10.1016/j.bbrc.2006.08.150.
  • Türkmen, M., Ciminli, C. (2007). Determination of metals in fish and mussel species by inductively coupled plasma-atomic emission spectrometry. Food Chem, 103:670-675.
  • Wildi, W., Domink, J., Thomas, RL., et al. (2004). River, reservoir and lake sediment contamination by heavy metals downstream from urban areas of switzerland. Lakes & Reservoirs: Res Manag, 9:75-87. Doi.org/10.1111/j.1440-1770.2004.00236.x
Toplam 32 adet kaynakça vardır.

Ayrıntılar

Birincil Dil İngilizce
Konular Hidrobiyoloji
Bölüm Araştırmalar
Yazarlar

Çiğdem Kırsüleymanoğlu 0000-0001-7262-1349

Dilek Çelikler 0000-0002-9945-7195

Proje Numarası PYO.EGF.1904.19.006.
Yayımlanma Tarihi 25 Haziran 2022
Kabul Tarihi 24 Haziran 2022
Yayımlandığı Sayı Yıl 2022 Cilt: 8 Sayı: 1

Kaynak Göster

APA Kırsüleymanoğlu, Ç., & Çelikler, D. (2022). The effect of some transition metal ions (Mn+2, Co+2, Fe+2) on paraoxonase enzyme activity (E.C.3.1.8.1.) in bonito (Sarda sarda). Menba Kastamonu Üniversitesi Su Ürünleri Fakültesi Dergisi, 8(1), 23-30.
AMA Kırsüleymanoğlu Ç, Çelikler D. The effect of some transition metal ions (Mn+2, Co+2, Fe+2) on paraoxonase enzyme activity (E.C.3.1.8.1.) in bonito (Sarda sarda). Menba Kastamonu Üniversitesi Su Ürünleri Fakültesi Dergisi. Haziran 2022;8(1):23-30.
Chicago Kırsüleymanoğlu, Çiğdem, ve Dilek Çelikler. “The Effect of Some Transition Metal Ions (Mn+2, Co+2, Fe+2) on Paraoxonase Enzyme Activity (E.C.3.1.8.1.) in Bonito (Sarda Sarda)”. Menba Kastamonu Üniversitesi Su Ürünleri Fakültesi Dergisi 8, sy. 1 (Haziran 2022): 23-30.
EndNote Kırsüleymanoğlu Ç, Çelikler D (01 Haziran 2022) The effect of some transition metal ions (Mn+2, Co+2, Fe+2) on paraoxonase enzyme activity (E.C.3.1.8.1.) in bonito (Sarda sarda). Menba Kastamonu Üniversitesi Su Ürünleri Fakültesi Dergisi 8 1 23–30.
IEEE Ç. Kırsüleymanoğlu ve D. Çelikler, “The effect of some transition metal ions (Mn+2, Co+2, Fe+2) on paraoxonase enzyme activity (E.C.3.1.8.1.) in bonito (Sarda sarda)”, Menba Kastamonu Üniversitesi Su Ürünleri Fakültesi Dergisi, c. 8, sy. 1, ss. 23–30, 2022.
ISNAD Kırsüleymanoğlu, Çiğdem - Çelikler, Dilek. “The Effect of Some Transition Metal Ions (Mn+2, Co+2, Fe+2) on Paraoxonase Enzyme Activity (E.C.3.1.8.1.) in Bonito (Sarda Sarda)”. Menba Kastamonu Üniversitesi Su Ürünleri Fakültesi Dergisi 8/1 (Haziran 2022), 23-30.
JAMA Kırsüleymanoğlu Ç, Çelikler D. The effect of some transition metal ions (Mn+2, Co+2, Fe+2) on paraoxonase enzyme activity (E.C.3.1.8.1.) in bonito (Sarda sarda). Menba Kastamonu Üniversitesi Su Ürünleri Fakültesi Dergisi. 2022;8:23–30.
MLA Kırsüleymanoğlu, Çiğdem ve Dilek Çelikler. “The Effect of Some Transition Metal Ions (Mn+2, Co+2, Fe+2) on Paraoxonase Enzyme Activity (E.C.3.1.8.1.) in Bonito (Sarda Sarda)”. Menba Kastamonu Üniversitesi Su Ürünleri Fakültesi Dergisi, c. 8, sy. 1, 2022, ss. 23-30.
Vancouver Kırsüleymanoğlu Ç, Çelikler D. The effect of some transition metal ions (Mn+2, Co+2, Fe+2) on paraoxonase enzyme activity (E.C.3.1.8.1.) in bonito (Sarda sarda). Menba Kastamonu Üniversitesi Su Ürünleri Fakültesi Dergisi. 2022;8(1):23-30.
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