Yıl 2018,
Cilt: 7 Sayı: 3, 102 - 107, 30.09.2018
Birgül Vanizör Kural
,
Sevil Kör
Öz
Lipin
proteinleri hem fosfatidik asidin diaçilgliserole defosforilasyonunu
kalatizleyen fosfatitat fosfataz enzimi olarak hem de DNA-bağımlı transkripsiyon faktörlerinin
koregülatörü olarak fonksiyon görürler. Bu fonksiyonları ile özellikle
triaçilgliserol ve fosfolipid metabolizmasında önemli rol üstlenirler. Lipin
protein genleri insan için LPIN geni
ve diğer memeliler için lpin geni
şeklinde ifade edilmektedir. Memelilerde doku spesifik ekspresyonlarına göre lipin-1, lipin-2 ve
lipin-3 olmak üç lipin paralogu vardır. Ayrıca lipin-1’in insanda a, β ve g izoformları mevcuttur. Lipin-1 en fazla adipoz doku ve
iskelet kasında; lipin-2 en fazla karaciğer ve beyinde; lipin-3 ise gastrointestinal sistemde
bulunur. Bu derlemenin amacı lipin proteinlerinin çeşitleri, yapıları ve genel
fonksiyonları hakkında bilgi vermektir.
Kaynakça
- 1. Chen, Y, Rui, BB, Tang, LY, Hu, CM.( 2015). “Lipin family proteins--key regulators in lipid metabolism”. Ann Nutr Metab., 66(1), 10-8.
- 2. Reue, K, Brindley, DN. (2008). “Thematic Review Series: Glycerolipids. Multipleroles for lipins/phosphatidate phosphatase enzymes in lipid metabolism”. J Lipid Res., 49(12), 2493-503.
- 3. Williams, JA, Manley, S, Ding, WX. (2014). “New advances in molecular mechanisms and emerging therapeutic targets in alcoholic liver diseases”. World J Gastroenterol., 20(36), 12908-33.
- 4. Li, YY, Zhou, JY.(2016). “Role of lipin-1 in the pathogenesis of alcoholic fatty liver disease”. Zhonghua Gan Zang Bing Za Zhi, 24(3), 237-40.
- 5. Siniossoglou, S. (2013). “Phospholipid metabolism and nuclear function: roles of the lipin family of phosphatidic acid phosphatases”. Biochim Biophys Acta, 1831(3), 575-81.
- 6. Csaki, LS, Reue, K. (2010). “Lipins: multifunctional lipid metabolism proteins”. Annu Rev Nutr., 30, 257-72.
- 7. Csaki, LS, Dwyer, JR, Fong, LG, Tontonoz, P, Young, SG, Reue, K. (2013). “Lipins, lipinopathies, and the modulation of cellular lipid storage and signaling”. Prog Lipid Res., 52(3), 305-16.
- 8. Harris, TE, Finck, BN. (2011). “Dual function lipin proteins and glycerolipid metabolism”. Trends Endocrinol Metab., 22(6), 226-33.
- 9. Bou Khalil, M, Blais, A, Figeys, D, Yao, Z. (2010).“Lipin - The bridge between hepatic glycerolipid biosynthesis and lipoprotein metabolism”. Biochim Biophys Acta., 1801(12), 1249-59.
- 10. Kim, HE, Bae, E, Jeong, DY, Kim, MJ, Jin, WJ, Park, SW, Han, GS, Carman, GM, Koh, E, Kim, KS. (2013). “Lipin1 regulates PPARγ transcriptional activity”. Biochem J., 453(1), 49-60.
- 11. Sasser, T, Qiu, QS, Karunakaran, S, Padolina, M, Reyes, A, Flood, B, Smith, S, Gonzales, C, Fratti, RA. (2012). “Yeast lipin 1 orthologue pah1p regulates vacuole homeostasis and membrane fusion”. J Biol Chem., 287(3), 2221-36.
- 12. Péterfy, M, Phan, J, Xu, P, Reue, K. (2001). “Lipodystrophy in the fld mouse results from mutation of a new gene encoding a nuclear protein, lipin”. Nat Genet, 27(1), 121-4.
- 13. Phan, J, Reue, K. (2005). “Lipin, a lipodystrophy and obesity gene”. Cell Metab., 1(1), 73-83.
- 14. Michot, C, Hubert, L, Romero, NB, Gouda, A, Mamoune, A, Mathew, S, et al. (2012). “Study of LPIN1, LPIN2 and LPIN3 in rhabdomyolysis and exercise-induced myalgia”. J Inherit Metab Dis., 35(6), 1119-28.
- 15. Vanizor Kural, B, Alver, A, Canpolat, S, Kahraman, C, Us Altay, D, Kara, H, Akcan, B. (2014). “The Effects of high fat diets with and without N-Acetylcysteine supplementation on the lipin-1 levels of serum and various tissues in rats”. Turk J Biochem, 39(1), 19–24.
- 16. Donkor, J, Sparks, LM, Xie, H, Smith, SR, Reue, K. (2008). “Adipose tissue lipin-1 expression is correlated with peroxisome proliferator-activated receptor alpha gene expression and insulin sensitivity in healthy young men". J Clin Endocrinol Metab., 93(1), 233-9.
- 17. Zeharia, A, Shaag, A, Houtkooper, RH, Hindi, T, de Lonlay, P, Erez, G, Hubert, L, Saada, A, de Keyzer, Y, Eshel, G, Vaz, FM, Pines, O, Elpeleg, O. (2008). “Mutations in LPIN1 cause recurrent acute myoglobinuria in childhood”. Am J Hum Genet, 83(4), 489-94.
- 18. Wang, H, Zhang, J, Qiu, W, Han, GS, Carman, GM, Adeli, K. (2011). “Lipin-1 gamma isoform is a novel lipid droplet-associated protein highly expressed in the brain”. FEBS Lett., 585(12), 1979-84.
- 19. Sembongi, H, Miranda, M, Han, GS, Fakas, S, Grimsey, N, Vendrell, J, Carman, GM, Siniossoglou, S. (2013). “Distinct roles of the phosphatidate phosphatases lipin 1 and 2 during adipogenesis and lipid droplet biogenesis in 3T3-L1 cells”. J Biol Chem., 288(48), 34502-13.
- 20. Péterfy, M, Harris, TE, Fujita, N, Reue, K. (2010). “Insulin-stimulated interaction with 14-3-3 promotes cytoplasmic localization of lipin-1 in adipocytes”. J Biol Chem., 285(6), 3857-64.
- 21. Bi, L, Jiang, Z, Zhou, J. (2015). “The role of lipin-1 in the pathogenesis of alcoholic fatty liver”. Alcohol Alcohol., 50(2), 146-51.
- 22. Eaton, JM, Mullins, GR, Brindley, DN, Harris, TE. (2013). “Phosphorylation of lipin 1 and charge on the phosphatidic acid head group control its phosphatidic acid phosphatase activity and membrane association”. J Biol Chem., 288(14), 9933-45.
- 23. Csaki, LS, Dwyer, JR, Li, X, Nguyen, MH, Dewald, J, Brindley, DN, Lusis, AJ, Yoshinaga, Y, de Jong, P, Fong, L, Young, SG, Reue, K. (2014). “Lipin-1 and lipin-3 together determine adiposity in vivo”. Mol Metab., 3(2), 145-54.
- 24. Valdearcos, M, Esquinas, E, Meana, C, Peña, L, Gil-de-Gómez, L, Balsinde, J, Balboa, MA. (2012). “Lipin-2 reduces proinflammatory signaling induced by saturated fatty acids in macrophages”. J Biol Chem., 287(14), 10894-904.
- 25. Lordén, G, Sanjuán-García, I, de Pablo, N, Meana, C, Alvarez-Miguel, I, Pérez-García, MT, Pelegrín, P, Balsinde, J, Balboa, MA. (2017). “Lipin-2 regulates NLRP3 inflammasome by affecting P2X7 receptor activation”. J Exp Med., 214(2), 511-528.
- 26. Obama, T, Nagaoka, S, Akagi, K, Kato, R, Horiuchi, N, Horai, Y, Aiuchi, T, Arata, S, Yamaguchi, T, Watanabe, M, Itabe, H. (2011). “Dietary cholesterol reduces plasma triacylglycerol in apolipoprotein E-null mice: suppression of lipin-1 and -2 in the glycerol-3-phosphate pathway”. Plos One, 6(8), 22917.
- 27. Ryu, D, Seo, WY, Yoon, YS, Kim, YN, Kim, SS, Kim, HJ, Park, TS, Choi, CS, Koo, SH. (2011). “Endoplasmic reticulum stress promotes LIPIN2-dependent hepatic insulin resistance”. Diabetes, 60(4), 1072-81.
- 28. Dwyer, JR, Donkor, J, Zhang, P, Csaki, LS, Vergnes, L, Lee, JM, Dewald, J, Brindley, DN, Atti, E, Tetradis, S, Yoshinaga, Y, De Jong, PJ, Fong, LG, Young, SG, Reue, K. (2012). “Mouse lipin-1 and lipin-2 cooperate to maintain glycerolipid homeostasis in liver and aging cerebellum”. Proc Natl Acad Sci U S A., 109(37), E2486-95.
- 29. Gropler, MC, Harris, TE, Hall, AM, Wolins, NE, Gross, RW, Han, X, Chen Z, Finck BN. (2009). “Lipin 2 is a liver-enriched phosphatidate phosphohydrolase enzyme that is dynamically regulated by fasting and obesity in mice”. J Biol Chem., 284(11), 6763-72.
- 30. Kok, BP, Kienesberger, PC, Dyck, JR, Brindley, DN. (2012). “Relationship of glucose and oleate metabolism to cardiac function in lipin-1 deficient (fld) mice”. J Lipid Res., 53(1), 105-18.
Yıl 2018,
Cilt: 7 Sayı: 3, 102 - 107, 30.09.2018
Birgül Vanizör Kural
,
Sevil Kör
Kaynakça
- 1. Chen, Y, Rui, BB, Tang, LY, Hu, CM.( 2015). “Lipin family proteins--key regulators in lipid metabolism”. Ann Nutr Metab., 66(1), 10-8.
- 2. Reue, K, Brindley, DN. (2008). “Thematic Review Series: Glycerolipids. Multipleroles for lipins/phosphatidate phosphatase enzymes in lipid metabolism”. J Lipid Res., 49(12), 2493-503.
- 3. Williams, JA, Manley, S, Ding, WX. (2014). “New advances in molecular mechanisms and emerging therapeutic targets in alcoholic liver diseases”. World J Gastroenterol., 20(36), 12908-33.
- 4. Li, YY, Zhou, JY.(2016). “Role of lipin-1 in the pathogenesis of alcoholic fatty liver disease”. Zhonghua Gan Zang Bing Za Zhi, 24(3), 237-40.
- 5. Siniossoglou, S. (2013). “Phospholipid metabolism and nuclear function: roles of the lipin family of phosphatidic acid phosphatases”. Biochim Biophys Acta, 1831(3), 575-81.
- 6. Csaki, LS, Reue, K. (2010). “Lipins: multifunctional lipid metabolism proteins”. Annu Rev Nutr., 30, 257-72.
- 7. Csaki, LS, Dwyer, JR, Fong, LG, Tontonoz, P, Young, SG, Reue, K. (2013). “Lipins, lipinopathies, and the modulation of cellular lipid storage and signaling”. Prog Lipid Res., 52(3), 305-16.
- 8. Harris, TE, Finck, BN. (2011). “Dual function lipin proteins and glycerolipid metabolism”. Trends Endocrinol Metab., 22(6), 226-33.
- 9. Bou Khalil, M, Blais, A, Figeys, D, Yao, Z. (2010).“Lipin - The bridge between hepatic glycerolipid biosynthesis and lipoprotein metabolism”. Biochim Biophys Acta., 1801(12), 1249-59.
- 10. Kim, HE, Bae, E, Jeong, DY, Kim, MJ, Jin, WJ, Park, SW, Han, GS, Carman, GM, Koh, E, Kim, KS. (2013). “Lipin1 regulates PPARγ transcriptional activity”. Biochem J., 453(1), 49-60.
- 11. Sasser, T, Qiu, QS, Karunakaran, S, Padolina, M, Reyes, A, Flood, B, Smith, S, Gonzales, C, Fratti, RA. (2012). “Yeast lipin 1 orthologue pah1p regulates vacuole homeostasis and membrane fusion”. J Biol Chem., 287(3), 2221-36.
- 12. Péterfy, M, Phan, J, Xu, P, Reue, K. (2001). “Lipodystrophy in the fld mouse results from mutation of a new gene encoding a nuclear protein, lipin”. Nat Genet, 27(1), 121-4.
- 13. Phan, J, Reue, K. (2005). “Lipin, a lipodystrophy and obesity gene”. Cell Metab., 1(1), 73-83.
- 14. Michot, C, Hubert, L, Romero, NB, Gouda, A, Mamoune, A, Mathew, S, et al. (2012). “Study of LPIN1, LPIN2 and LPIN3 in rhabdomyolysis and exercise-induced myalgia”. J Inherit Metab Dis., 35(6), 1119-28.
- 15. Vanizor Kural, B, Alver, A, Canpolat, S, Kahraman, C, Us Altay, D, Kara, H, Akcan, B. (2014). “The Effects of high fat diets with and without N-Acetylcysteine supplementation on the lipin-1 levels of serum and various tissues in rats”. Turk J Biochem, 39(1), 19–24.
- 16. Donkor, J, Sparks, LM, Xie, H, Smith, SR, Reue, K. (2008). “Adipose tissue lipin-1 expression is correlated with peroxisome proliferator-activated receptor alpha gene expression and insulin sensitivity in healthy young men". J Clin Endocrinol Metab., 93(1), 233-9.
- 17. Zeharia, A, Shaag, A, Houtkooper, RH, Hindi, T, de Lonlay, P, Erez, G, Hubert, L, Saada, A, de Keyzer, Y, Eshel, G, Vaz, FM, Pines, O, Elpeleg, O. (2008). “Mutations in LPIN1 cause recurrent acute myoglobinuria in childhood”. Am J Hum Genet, 83(4), 489-94.
- 18. Wang, H, Zhang, J, Qiu, W, Han, GS, Carman, GM, Adeli, K. (2011). “Lipin-1 gamma isoform is a novel lipid droplet-associated protein highly expressed in the brain”. FEBS Lett., 585(12), 1979-84.
- 19. Sembongi, H, Miranda, M, Han, GS, Fakas, S, Grimsey, N, Vendrell, J, Carman, GM, Siniossoglou, S. (2013). “Distinct roles of the phosphatidate phosphatases lipin 1 and 2 during adipogenesis and lipid droplet biogenesis in 3T3-L1 cells”. J Biol Chem., 288(48), 34502-13.
- 20. Péterfy, M, Harris, TE, Fujita, N, Reue, K. (2010). “Insulin-stimulated interaction with 14-3-3 promotes cytoplasmic localization of lipin-1 in adipocytes”. J Biol Chem., 285(6), 3857-64.
- 21. Bi, L, Jiang, Z, Zhou, J. (2015). “The role of lipin-1 in the pathogenesis of alcoholic fatty liver”. Alcohol Alcohol., 50(2), 146-51.
- 22. Eaton, JM, Mullins, GR, Brindley, DN, Harris, TE. (2013). “Phosphorylation of lipin 1 and charge on the phosphatidic acid head group control its phosphatidic acid phosphatase activity and membrane association”. J Biol Chem., 288(14), 9933-45.
- 23. Csaki, LS, Dwyer, JR, Li, X, Nguyen, MH, Dewald, J, Brindley, DN, Lusis, AJ, Yoshinaga, Y, de Jong, P, Fong, L, Young, SG, Reue, K. (2014). “Lipin-1 and lipin-3 together determine adiposity in vivo”. Mol Metab., 3(2), 145-54.
- 24. Valdearcos, M, Esquinas, E, Meana, C, Peña, L, Gil-de-Gómez, L, Balsinde, J, Balboa, MA. (2012). “Lipin-2 reduces proinflammatory signaling induced by saturated fatty acids in macrophages”. J Biol Chem., 287(14), 10894-904.
- 25. Lordén, G, Sanjuán-García, I, de Pablo, N, Meana, C, Alvarez-Miguel, I, Pérez-García, MT, Pelegrín, P, Balsinde, J, Balboa, MA. (2017). “Lipin-2 regulates NLRP3 inflammasome by affecting P2X7 receptor activation”. J Exp Med., 214(2), 511-528.
- 26. Obama, T, Nagaoka, S, Akagi, K, Kato, R, Horiuchi, N, Horai, Y, Aiuchi, T, Arata, S, Yamaguchi, T, Watanabe, M, Itabe, H. (2011). “Dietary cholesterol reduces plasma triacylglycerol in apolipoprotein E-null mice: suppression of lipin-1 and -2 in the glycerol-3-phosphate pathway”. Plos One, 6(8), 22917.
- 27. Ryu, D, Seo, WY, Yoon, YS, Kim, YN, Kim, SS, Kim, HJ, Park, TS, Choi, CS, Koo, SH. (2011). “Endoplasmic reticulum stress promotes LIPIN2-dependent hepatic insulin resistance”. Diabetes, 60(4), 1072-81.
- 28. Dwyer, JR, Donkor, J, Zhang, P, Csaki, LS, Vergnes, L, Lee, JM, Dewald, J, Brindley, DN, Atti, E, Tetradis, S, Yoshinaga, Y, De Jong, PJ, Fong, LG, Young, SG, Reue, K. (2012). “Mouse lipin-1 and lipin-2 cooperate to maintain glycerolipid homeostasis in liver and aging cerebellum”. Proc Natl Acad Sci U S A., 109(37), E2486-95.
- 29. Gropler, MC, Harris, TE, Hall, AM, Wolins, NE, Gross, RW, Han, X, Chen Z, Finck BN. (2009). “Lipin 2 is a liver-enriched phosphatidate phosphohydrolase enzyme that is dynamically regulated by fasting and obesity in mice”. J Biol Chem., 284(11), 6763-72.
- 30. Kok, BP, Kienesberger, PC, Dyck, JR, Brindley, DN. (2012). “Relationship of glucose and oleate metabolism to cardiac function in lipin-1 deficient (fld) mice”. J Lipid Res., 53(1), 105-18.