본문 바로가기
KERD
논문KCI 등재

Involvement of protein tyrosine phosphatases in adipogenesis: New anti-obesity targets?

이상철|김원곤|배광희
생화학분자생물학회 (Korean Society Of Biochemistry And Molecular Biology)|2012.12|BMB Reports|제45권 제12호|pp. 700-706

2

조회

0

다운로드

3

인용

0

참고문헌

키워드

ObesityAdipogenesisAdipocytePhosphorylationProtein tyrosine phosphatase
주제분류화학

초록

Obesity is a worldwide epidemic as well as being a major risk factor for diabetes, cardiovascular diseases and several types of cancers. Obesity is mainly due to the overgrowth of adipose tissue arising from an imbalance between energy intake and energy expenditure. Adipose tissue, primarily composed of adipocytes, plays a key role in maintaining whole body energy homeostasis. In view of the treatment of obesity and obesity-related diseases, it is critical to understand the detailed signal transduction mechanisms of adipogenic differentiation. Adipogenic differentiation is tightly regulated by many key signal cascades, including insulin signaling. These signal cascades generally transfer or amplify the signal by using serial tyrosine phosphorylations. Thus, protein tyrosine kinases and protein tyrosine phosphatases are closely related to adipogenic differentiation. Compared to protein tyrosine kinases, protein tyrosine phosphatases have received little attention in adipogenic differentiation. This review aims to highlight the involvement of protein tyrosine phosphatases in adipogenic differentiation and the possibility of protein tyrosine phosphatases as drugs to target obesity. [BMB Reports 2012;45(12): 700-706]

Abstract

Obesity is a worldwide epidemic as well as being a major risk factor for diabetes, cardiovascular diseases and several types of cancers. Obesity is mainly due to the overgrowth of adipose tissue arising from an imbalance between energy intake and energy expenditure. Adipose tissue, primarily composed of adipocytes, plays a key role in maintaining whole body energy homeostasis. In view of the treatment of obesity and obesity-related diseases, it is critical to understand the detailed signal transduction mechanisms of adipogenic differentiation. Adipogenic differentiation is tightly regulated by many key signal cascades, including insulin signaling. These signal cascades generally transfer or amplify the signal by using serial tyrosine phosphorylations. Thus, protein tyrosine kinases and protein tyrosine phosphatases are closely related to adipogenic differentiation. Compared to protein tyrosine kinases, protein tyrosine phosphatases have received little attention in adipogenic differentiation. This review aims to highlight the involvement of protein tyrosine phosphatases in adipogenic differentiation and the possibility of protein tyrosine phosphatases as drugs to target obesity. [BMB Reports 2012;45(12): 700-706]

참고문헌 (56)

  1. O’Rahilly, S., "Human genetics illuminates the paths to metabolic disease", Nature, 462, pp.307~314 (2009)
  2. Hursting, S. D., "Obesity, metabolic dysregulation, and cancer: a growing concern and an inflammatory (and microenvironmental) issue", Ann. N. Y. Acad. Sci., 1271, pp.82~87 (2012)
  3. Kim, E. Y., "Acetylation of malate dehydrogenase 1 promotes adipogenic differentiation via activating its enzymatic activity", J. Lipid Res., 53, pp.1864~1876 (2012)
  4. Cawthorn, W. P., "Adipose tissue stem cells meet preadipocyte commitment:going back to the future", J. Lipid Res., 53, pp.227~246 (2012)
  5. Koren, S., "Inhibition of the protein tyrosine phosphatase PTP1B: potential therapy for obesity, insulin resistance and type-2 diabetes mellitus", Best Prac. Res. Clin. Endocrinol. Met., 21, pp.621~640 (2007)
  6. Mustelin, T., "Protein tyrosine phosphatases", Front Biosci., 7, pp.d85~d142 (2002)
  7. Mustelin, T., "Positive and negative regulation of T-cell activation through kinases and phosphatases", Biochem. J., 371, pp.15~27 (2003)
  8. Hunter, T., "Signaling-2000 and beyond", Cell, 100, pp.113~127 (2000)
  9. Mustelin, T., "Protein tyrosine phosphatases in human disease. Lymphocyte Signal Transduction", Adv. Exp. Med. Biol., 584, pp.53~72 (2006)
  10. Julien, S. G., "Inside the human cancer tyrosine phosphatome", Nature Rev. Cancer, 11, pp.35~49 (2011)
  11. Goldstein, B. J., "Regulation of insulin receptor signaling by protein-tyrosine dephosphorylation", Receptor, 3, pp.1~15 (1993)
  12. Tonks, N. K., "From form to function: signaling by protein tyrosine phosphatases", Cell, 87, pp.365~368 (1996)
  13. Tabernero, L., "Protein tyrosine phosphatases: structure- function relationships", FEBS J., 275, pp.867~882 (2008)
  14. Hwang, C. S., "Adipocyte differentiation and leptin expression", Annu. Rev. Cell Dev. Biol., 13, pp.231~259 (1997)
  15. Matsuo, K., "Regulation of brown fat adipogenesis by protein tyrosine phosphatase 1B", Plos One, 6, pp.e16446~ (2011)
  16. Choi, Hye-Ryung, "Protein Tyrosine Phosphatase Profiling Analysis of HIB-1B Cells during Brown Adipogenesis", Journal of Microbiology and Biotechnology, 22(7), pp.1029~1033 (2012), 한국미생물·생명공학회[DOI]
  17. Kim, W. K., "Myostatin inhibits brown adipocyte differentiation via regulation of Smad3-mediated beta-catenin stabilization", INTERNATIONAL JOURNAL OF BIOCHEMISTRY CELL BIOLOGY, 44(2), pp.327~334 (2012), PERGAMON-ELSEVIER SCIENCE LTD
  18. Cypess, A. M., "Identification and importance of brown adipose tissue in adult humans", N. Engl. J. Med., 360, pp.1509~1517 (2009)
  19. van Marken Lichtenbelt, W., "Cold-activated brown adipose tissue in healthy men", N. Engl. J. Med., 360, pp.1500~1508 (2009)
  20. Farmer, S. R., "Obesity: be cool, lose weight", Nature, 458, pp.839~840 (2009)
  21. Poulos, S. P., "Cell line models for differentiation: preadipocytes and adipocytes", Exp. Biol. Med., 235, pp.1185~1193 (2010)
  22. Ntambi, J. M., "Adipocyte differentiation and gene expression", J. Nutr., 130, pp.3122S~3126S (2000)
  23. Gregoire, F., "Adipocyte differentiation: from fibroblast to endocrine cell", Exp. Biol. Med., 226, pp.997~1002 (2012)
  24. Hong, J. H., "TAZ, a transcriptional modulator of mesenchymal stem cell differentiation", SCIENCE, 309(5737), pp.1074~1078, AMER ASSOC ADVANCEMENT SCIENCE
  25. Jeon, M. J., "Activation of peroxisome proliferator-activated receptor gamma inhibits the Runx2-mediated transcription of osteocalcin in osteoblasts", J. Biol. Chem., 278, pp.23270~23277 (2003)
  26. Tang, Q. Q., "Adipogenesis: From stem cell to adipocyte", Annu. Rev. Biochem., 81, pp.715~736 (2012)
  27. White, M. F., "The insulin signaling system", J. Biol. Chem., 269, pp.1~4 (1994)
  28. White, M. F., "The IRS-signaling system: a network of docking proteins that mediate insulin and cytokine action", Curr. Top. Microbiol. Immunol., 228, pp.179~208 (1998)
  29. Czech, M. P., "Signaling mechanisms that regulate glucose transport", J. Biol. Chem., 274, pp.1865~1868 (1999)
  30. Rosen, E. D., "Molecular regulation of adipogenesis", Annu. Rev. Cell Dev. Biol., 16, pp.145~171 (2000)
  31. Laustsen, P. G., "Lipoatrophic diabetes in Irs1(-", -), -) double knockout mice, pp.Genes Dev., 2002[DOI]
  32. Tseng, Y. H., "Differential roles of insulin receptor substrates in brown adipocyte differentiation", Mol. Cell Biol., 24, pp.1918~1929 (2004)
  33. Rosen, E. D., "Adipocyte differentiation from the inside out", Nat. Rev. Mol. Cell Biol., 7, pp.885~896 (2006)
  34. Garofalo, R. S., "Severe diabetes, age-dependent loss of adipose tissue, and mild growth deficiency in mice lacking Akt2", PKBβ, 2003, pp.112, 197~208
  35. Menghini, R., "Phosphorylation of GATA2 by Akt increases adipose tissue differentiation and reduces adipose tissue-related inflammation: a novel pathway linking obesity to atherosclerosis", Circulation, 111, pp.1946~1953 (2005)
  36. Wolfrum, C., "Role of Foxa-2 in adipocyte metabolism and differentiation", J. Clin. Invest., 112, pp.345~356 (2003)
  37. Meng, T. C., "Regulation of insulin signaling through reversible oxidation of the protein-tyrosine phosphatases TC45 and PTP1B", J. Biol. Chem., 279, pp.37716~37725 (2004)
  38. Niu, X. L., "Leukocyte antigen-related deficiency enhances insulin-like growth factor-1 signaling in vascular smooth muscle cells and promotes neointima formation in response to vascular injury", J. Biol. Chem., 282, pp.19808~19819 (2007)
  39. Goldstein, B. J., "Regulation of insulin receptor signaling by protein-tyrosine dephosphorylation", Receptor, 3, pp.1~15 (1993)
  40. Denu, J. M., "Form and function in protein dephosphorylation", Cell, 87, pp.361~364 (1996)
  41. Jung, H., "Involvement of PTP-RQ in differentiation during adipogenesis of human mesenchymal stem cells", BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 383, pp.252~257 (2009), ELSEVIER
  42. Kim, W. K., "Regulation of adipocyte differentiation by LAR tyrosine phosphatase in human mesenchymal stem cells and 3T3–L1 preadipocytes", J. Cell Sci., 122, pp.4160~4167 (2009)
  43. Kim, W. K., "RPTPμ tyrosine phosphatase promotes adipogenic differentiation via modulation of p120 catenin phosphorylation", Molecular Biology of the Cell, 22(24), pp.4883~4891 (2011), American Society for Cell Biology
  44. Ozawa, M., "The membrane-proximal region of the E-cadherin cytoplasmic domain prevents dimerization and negatively regulates adhesion activity", J. Cell Biol., 142, pp.1605~1613 (1998)
  45. Noren, N. K., "p120 catenin regulates the actin cytoskeleton via Rho family GTPases", J. Cell Biol., 150, pp.567~580 (2000)
  46. Saltiel, A. R., "Insulin signalling and the regulation of glucose and lipid metabolism", Nature, 414, pp.799~806 (2001)
  47. Uehara, T., "SHP-2 positively regulates adipogenic differentiation in 3T3-L1 cells", Int. J. Mol. Med., 19, pp.895~900 (2007)
  48. Hayashi, K., "Insulin receptor substrate-1", SHP-2 interaction, a phenotype-dependent switching machinery of insulin-like growth factor-I signaling in vascular smooth muscle cells, 2004, pp.279, 40807~40818
  49. Sakaue, H., "Role of MAPK phosphatase- 1 (MKP1) in adipocyte differentiation", J. Biol. Chem., 279, pp.39951~39957 (2004)
  50. Glondu-Lassis, M., "Downregulation of protein tyrosine phosphatase PTP-BL repress adipogenesis", Int. J. Biochem. Cell Biol., 41, pp.2173~2180 (2009)
  51. Owen, C., "Adipocyte-specific protein tyrosine phosphatase 1B deletion increases lipogenesis, adipocyte cell size and is a minor regulator of glucose homeostasis", Plos One, 7, pp.e32700~ (2012)
  52. Lee, K., "Recent advances in protein Tyrosine phosphatase detection using chemical probes", Anti-Cancer Agents in Medicinal Chemistry, 11(1), pp.54~63 (2011), Bentham Science Publishers B.V.
  53. Jiang, Z. -X., "Targeting PTPs with small molecule inhibitors in cancer treatment", Cancer Meta. Rev., 27, pp.263~272 (2008)
  54. Blaskovich, M. A. T., "Drug discovery and protein tyrosine phosphatases", Curr. Med. Chem., 16, pp.2095~2176 (2009)
  55. Scott, L. M., "Targeting protein tyrosine phosphatases for anticancer drug discovery", Curr. Pharm. Des., 16, pp.1843~1862 (2010)
  56. Woojung Lee, "Anti-obesity and hypolipidemic effects of Rheum undulatum in high-fat diet-fed C57BL", 6 mice through protein tyrosine phosphatase 1B inhibition, 2012, pp.45(3), 141~146[DOI]

관련 논문AI추천

Protein tyrosine phosphatase profiling studies during brown adipogenic differentiation of mouse primary brown preadipocytes김원곤, 박안나, 배광희, 이상철, 정혜연, 최혜령, 한백수생화학분자생물학회 · BMB Reports2013 · 제46권 제11호Anti-obesity and hypolipidemic effects of Rheum undulatum in high-fat diet-fed C57BL/6 mice through protein tyrosine phosphatase 1B inhibition윤구, 김수남, 김용기, 황예란, Woojung Lee생화학분자생물학회 · BMB Reports2012 · 제45권 제3호Myonectin inhibits adipogenesis in 3T3-L1 preadipocytes by regulating p38 MAPK pathway김원곤, 오경진, 이상철, Anna Park, Baek Soo Han, Eun Woo Lee, Jaehoon Kim, Jeong-Yoon Kim, Kwang-Hee Bae, Tae-Jun Park생화학분자생물학회 · BMB Reports2021 · 제54권 제2호Emerging roles of PHLPP phosphatases in metabolism오아름, Jong-Ho Cha, KyeongJin Kim, Sang Bae Lee, Soon-Sun Hong, Yelin Jeong생화학분자생물학회 · BMB Reports2021 · 제54권 제9호Structure and catalytic mechanism of human protein tyrosine phosphatome김승준, 류성언생화학분자생물학회 · BMB Reports2012 · 제45권 제12호Roots Extract of Adenophora triphylla var. japonica Inhibits Adipogenesis in 3T3-L1 Cells through the Downregulation of IRS1김혜림, 박성범, 우성민, 이동령, 이해진, 최봉근한의병리학회 · 동의생리병리학회지2020 · 제34권 제3호

이 간행물의 다른 논문 (11건)

Tumor-associated autoantibodies as diagnostic and prognostic biomarkersChang-Kyu Heo, 조은위, 박영일pp. 677-685Mouse genetics: Catalogue and scissors김진수, 성제경, 이한웅, Young Hoon Sung, 백인정pp. 686-692Structure and catalytic mechanism of human protein tyrosine phosphatome류성언, 김승준pp. 693-699Roles of cysteine residues in the inhibition of human glutamate dehydrogenase by palmitoyl-CoAHyo Jeong Son, Seung Cheol Ha, Eun Young Hwang, 조성우, 안지인, 김은아, 최수영pp. 707-712Ganglioside GM1 influences the proliferation rate of mouse induced pluripotent stem cellsGislain Moussavou, 김지수, 김선욱, 장규태, 이정웅, 추영국, 고기성, 고기남, Kyung-A Hwang, 임맑음, 유재성, Ju-Taek Lee, Hyun-Ki Min, Yoon-Ju Na, Su-Bin Lee, Eun-Jeong Jeongpp. 713-718
원문 보기