Velázquez FMÁ, Chan TR, Ruiz EGR

Language: Spanish
References: 46
Page: 72-80
PDF size: 680.79 Kb.

ABSTRACT

Calreticulin is a multifunctional protein that was initially identified and characterized in the endoplasmic reticulum, and further identified in different subcellular compartments to regulate a variety of cellular processes. Interestingly, this protein is the only chaperone that has been identified in the cell surface and which is secreted to the extracellular space. Since the amino-terminal region of the calreticulin is part of the antibodies signature to detect the hepatocellular carcinoma, it could also be useful for the detection and/or diagnosis of other types of cancer. Besides, recent studies showed that calreticulin interacted with the 3´-UTR regions of the Angiotensin Receptor Type I and glucose Transporter 1 messenger RNAs to regulate their expression levels.

REFERENCES

1. Michalak M, Groenendyk J, Szabo E, Gold LI, Opas M (2009) Calreticulin, a multiprocess calcium-buffering chaperone of the endoplasmic reticulum. Biochem J 417: 651–666.

2. Baksh S, Michalak M (1991) Expression of calreticulin in Escherichia coli and identification of its Ca2+ binding domains. J Biol Chem 266(32):21458-65.

3. Nakamura K, Zuppini A, Arnaudeau S, Lynch J, Ahsan I, Krause R, Papp S, De Smedt H, Parys JB, Muller-Esterl W, Lew DP, Krause KH, Demaurex N, Opas M, Michalak M (2001) Functional specialization of calreticulin domains. J Cell Biol 154: 961–972.

4. Bastianutto C, Clementi E, Codazzi F, Podini P, De Giorgi F, Rizzuto R, Meldolesi J, Pozzan T (1995) Overexpression of calreticulin increases the Ca2+ capacity of rapidly exchanging Ca2+ stores and reveals aspects of their lumenal microenvironment and function. J Cell Biol 130: 847–855.

5. Mery L, Mesaeli N, Michalak M, Opas M, Lew DP, Krause KH (1996) Overexpression of calreticulin increases intracellular Ca2+storage and decreases store-operated Ca2+ influx. J Biol Chem 271: 9332–9339.

6. Lynch J, Guo L, Gelebart P, Chilibeck K, Xu J, Molkentin JD, Agellon LB, Michalak M (2005) Calreticulin signals upstream of calcineurin and MEF2C in a critical Ca2+-dependent signaling cascade. J Cell Biol 170: 37–47.

7. Guo L, Nakamura K, Lynch J, Opas M, Olson EN, Agellon LB, Michalak M (2002) Cardiacspecific expression of calcineurin reverses embryonic lethality in calreticulin-deficient mouse. J Biol Chem 277: 50776–50779.

8. Obeid M, Tesniere A, Ghiringhelli F, Fimia GM, Apetoh L, Perfettini JL, Castedo M, Mignot G, Panaretakis T, Casares N, Metivier D, Larochette N, van Endert P, Ciccosanti F, Piacentini M, Zitvogel L, Kroemer G (2007) Calreticulin exposure dictates the immunogenicity of cancer cell death. Nat Med 13: 54–61.

9. Tesniere A, Panaretakis T, Kepp O, Apetoh L, Ghiringhelli F, Zitvogel L, Kroemer G (2008) Molecular characteristics of immunogenic cancer cell death. Cell Death Differ 15: 3-12.

10. Gardai SJ, McPhillips KA, Frasch SC, Janssen WJ, Starefeldt A, Murphy-Ullrich JA, Bratton DL, Oldenborg PA, Michalak M, Henson PM (2005) Cell-surface calreticulin initiates clearance of viable or apoptotic cells through trans-activation of LRP on the phagocyte. Cell 123: 321-334.

11. Orr AW, Pallero MA, Xiong WC, Murphy-Ullrich, JE (2004) Thrombospondin induces RhoA inactivation through FAK-dependent signaling to stimulate focal adhesion disassembly. J Biol Chem 279: 48983–48992.

12. Nanney LB, Woodrell CD, Greives MR, Cardwell NL, Pollins AC, Bancroft TA, Chesser A, Michalak M, Rahman M, Siebert JW, Gold LI (2008) Calreticulin enhances porcine wound repair by diverse biological effects. Am J Pathol 173: 610–630.

13. Goicoechea S, Pallero MA, Eggleton P, Michalak M, Murphy-Ullrich JE (2002) The anti-adhesive activity of thrombospondin is mediated by the N-terminal domain of cell surface calreticulin. J Biol Chem 277: 37219–37228.

14. Pallero MA, Elzie CA, Chen J, Mosher DF, Murphy-Ullrich JE (2008) Thrombospondin 1 binding to calreticulin-LRP1 signals resistance to anoikis. FASEB J 22: 3968–3979.

15. Somogyi E, Petersson U, Hultenby K, Wendel M (2003) Calreticulin—an endoplasmic reticulum protein with calcium-binding activity is also found in the extracellular matrix. Matrix Biol 22: 179–191.

16. Kypreou KP, Kavvadas P, Karamessinis P, Peroulis M, Alberti A, Sideras P, Psarras S, Capetanaki Y, Politis PK, Charonis AS (2008) Altered expression of calreticulin during the development of fibrosis. Proteomics 8: 2407– 2419.

17. E g g l e t o n P, L l e w e l l y n D H ( 1 9 9 9 ) Pathophysiological roles of calreticulin in autoimmune disease. Scand J Immunol 49: 466–473.

18. Coppolino M, Leung-Hagesteijn C, Dedhar S, Wilkins J (1995) Inducible interaction of integrin alpha 2 beta 1 with calreticulin. Dependence on the activation state of the integrin. J Biol Chem 270: 23132–23138.

19. Tran H, Pankov R, Tran SD, Hampton B, Burgess WH, Yamada KM (2002) Integrin clustering induces kinectin accumulation. J Cell Sci 115: 2031–2040.

20. Bedard K, Szabo E, Michalak M, Opas M (2005) Cellular functions of endoplasmic reticulum chaperones calreticulin, calnexin, and ERp57. Int Rev Cytol 245: 91–121.

21. White TK, Zhu Q, Tanzer ML (1995) Cell surface calreticulin is a putative mannoside lectin which triggers mouse melanoma cell spreading. J Biol Chem 270: 15926–15929.

22. Orr AW, Elzie CA, Kucik DF, Murphy-Ullrich JE (2003) Thrombospondin signaling through the calreticulin/ LDL receptor-related protein co-complex stimulates random and directed cell migration. J Cell Sci 116: 2917–2927.

23. Tufi R, Panaretakis T, Bianchi K, Criollo A, Fazi B, Di Sano F, Tesniere A, Kepp O, Paterlini-Brechot P, Zitvogel L, Piacentini M, Szabadkai G, Kroemer G (2008) Reduction of endoplasmic reticulum Ca2_ levels favors plasma membrane surface exposure of calreticulin. Cell Death Differ 15: 274–282.

24. Viaud S, Terme M, Flament C, Taieb J, Andre F, Novault S, Escudier B, Robert C, Caillat- Zucman S, Tursz T, Zitvogel L, Chaput N (2009) Dendritic cell-derived exosomes promote natural killer cell activation and proliferation: a role for NKG2D ligands and IL-15Ralpha. PLoS One 4: e4942.

25. Panaretakis T., Joza N, Modjtahedi N, Tesniere A, Vitale I, Durchschlag M, Fimia, GM, Kepp O, Piacentini M, Froehlich KU, van Endert P, Zitvogel L, Madeo F, Kroemer G (2008) The co-translocation of ERp57 and calreticulin determines the immunogenicity of cell death. Cell Death Differ 15: 1499–1509.

26. Gehrmann M, Radons J, Molls M, and Multhoff G (2008) The therapeutic implications of clinically applied modifiers of heat shock protein 70 (Hsp70) expression by tumor cells. Cell Stress Chaperones 13: 1–10.

27. Forslow A, Liu Z, Sundqvist KG (2007) Receptor communication within the lymphocyte plasma membrane: a role for the thrombospondin family of matricellular proteins. Cell Mol Life Sci 64: 66–76.

28. Sipione S, Ewen C, Shostak I, Michalak M, Bleackley RC (2005) Impaired cytolytic activity in calreticulin-deficient CTLs. J Immunol 174: 3212–3219.

29. Obeid M (2009) Anticancer activity of targeted proapoptotic peptides and chemotherapy is highly improved by targeted cell surface calreticulin-inducer peptides. Mol Cancer Ther 8: 2693–2707.

30. Lu YC, Weng WC, Lee H (2015) Functional roles of calreticulin in cancer biology. Biomed Res Int 2015;2015:526524.

31. Armenian M, Veerakumarasivam A, Abdullah S, Rosli R (2013) Calreticulin and cancer. Pathol Oncol Res 19:149–154.

32. Ruiz Esparza-Garrido R, Velázquez-Flores MÁ, Diegopérez-Ramírez J, López-Aguilar E, Siordia-Reyes G, Hernández-Ortiz M, Martínez-Batallar AG, Encarnación-Guevara S, Salamanca-Gómez F, Arenas-Aranda DJ (2013) A proteomic approach of pediatric astrocytomas: MiRNAs and network insight. J Proteomics 94: 162-75.

33. Chen CN, Chang CC, Su TE, Hsu WM, Jeng YM, Ho MC, Hsieh FJ, Lee PH, Kuo ML, Lee H, Chang KJ (2009) Identification of calreticulin as a prognosis marker and angiogenic regulator in human gastric cancer. Ann Surg Oncol 16: 524–533.

34. Lwin ZM, Guo C, Salim A, Yip GW, Chew FT, Nan J, Thike AA, Tan PH, Bay BH (2010) Clinicopathological significance of calreticulin in breast invasive ductal carcinoma. Mod Pathol 23: 1559–1566.

35. Du XL, Hu H, Lin DC, Xia SH, Shen XM, Zhang Y, Luo ML, Feng YB, Cai Y, Xu X, Han YL, Zhan QM, Wang MR (2007) Proteomic profiling of proteins dysregulted in Chinese esophageal squamous cell carcinoma. J Mol Med (Berl) 85: 863–875.

36. Sheng W, Chen C, Dong M, Zhou J, Liu Q, Dong Q, Li F (2014) Overexpression of calreticulin contributes to the development and progression of pancreatic cancer. J Cell Physiol 229: 887–897.

37. Kageyama S, Isono T, Iwaki H, Wakabayashi Y, Okada Y, Kontani K, Yoshimura K, Terai A, Arai Y, Yoshiki T (2004) Identification by proteomic analysis of calreticulin as a marker for bladder cancer and evaluation of the diagnostic accuracy of its detection in urine. Clin Chem 50: 857–866.

38. Kageyama S, Isono T, Matsuda S, Ushio Y, Satomura S, Terai A, Arai Y, Kawakita M, Okada Y, Yoshiki T (2009) Urinary calreticulin in the diagnosis of bladder urothelial carcinoma. Int J Urol 16: 481–486.

39. Vaksman O, Davidson B, Tropé C, Reich R (2013) Calreticulin expression is reduced in high-grade ovarian serous carcinoma effusions compared with primary tumors and solid metastases. Hum Pathol 44: 2677–2683.

40. Chang HH, Lee H, Hu MK, Tsao PN, Juan HF, Huang MC, Shih YY, Wang BJ, Jeng YM, Chang CL, Huang SF, Tsay YG, Hsieh FJ, Lin KH, Hsu WM, Liao YF (2010) Notch1 expression predicts an unfavorable prognosis and serves as a therapeutic target of patients with neuroblastoma. Clin Cancer Res 16: 4411– 4420.

41. Klampfl T, Gisslinger H, Harutyunyan AS, Nivarthi H, Rumi E, Milosevic JD, Them NC, Berg T, Gisslinger B, Pietra D, Chen D, Vladimer GI, Bagienski K, Milanesi C, Casetti IC, Sant’Antonio E, Ferretti V, Elena C, Schischlik F, Cleary C, Six M, Schalling M, Schönegger A, Bock C, Malcovati L, Pascutto C, Superti-Furga G, Cazzola M, Kralovics R (2013) Somatic mutations of calreticulin in myeloproliferative neoplasms. N Engl J Med 369: 2379–2390.

42. Nangalia J, Massie CE, Baxter EJ, Nice FL, Gundem G, Wedge DC, Avezov E, Li J, Kollmann K, Kent DG, Aziz A, Godfrey AL, Hinton J, Martincorena I, Van Loo P, Jones AV, Guglielmelli P, Tarpey P, Harding HP, Fitzpatrick JD, Goudie CT, Ortmann CA, Loughran SJ, Raine K, Jones DR, Butler AP, Teague JW, O’Meara S, McLaren S, Bianchi M, Silber Y, Dimitropoulou D, Bloxham D, Mudie L, Maddison M, Robinson B, Keohane C, Maclean C, Hill K, Orchard K, Tauro S, Du MQ, Greaves M, Bowen D, Huntly BJ, Harrison CN, Cross NC, Ron D, Vannucchi AM, Papaemmanuil E, Campbell PJ, Green AR (2013) Somatic CALR mutations in myeloproliferative neoplasms with nonmutated JAK2. N Engl J Med 369: 2391–2405.

43. James C, Ugo V, Le Couédic JP, Staerk J, Delhommeau F, Lacout C, Garçon L, Raslova H, Berger R, Bennaceur-Griscelli A, Villeval JL, Constantinescu SN, Casadevall N, Vainchenker W (2005) A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera. Nature 434: 1144–1148.

44. Kralovics R, Passamonti F, Buser AS, Teo SS, Tiedt R, Passweg JR, Tichelli A, Cazzola M, Skoda RC (2005) A gain-of-function mutation of JAK2 in myeloproliferative disorders. N Engl J Med 352: 1779–1790.

45. Sun C, Zhang S, Li J (2015) Calreticulin gene mutations in myeloproliferative neoplasms without Janus kinase 2 mutations. Leuk Lymphoma 56: 1593-1598.

46. Nickenig G, Michaelsen F, Müller C, Berger A, Vogel T, Sachinidis A, Vetter H, Böhm M (2002) Destabilization of AT1 receptor mRNA by calreticulin. Circ Res 90: 53–58.