Структурно-функциональные особенности тромбоцитарных интегринов

  • Д.Д. ЖЕРНОСЕКОВ (D.D. ZHERNOSSEKOV), д-р биол. наук, доцент Полесский государственный университет, г. Пинск, Республика Беларусь
Ключевые слова: тромбоциты, интегрины, плазминоген/плазминовая система

Аннотация

В обзоре описаны структурно-функциональные особенности адгезивных белков интегринового семейства, принимающих участие в установлении адгезивных связей тромбоцитов между собой и с другими клетками. Показано модулирующее действие компонентов плазминоген/плазминовой системы на эффективность адгезивного взаимодействия, опосредованнного интегриновыми белками. Рассмотрено действие препаратов, направленных на блокирование интегриновой адгезии.

Литература

1. Cell adhesion molecules and ubiquitinationfunctions and significance. / M. Homrich [et al.] // Biology – 2016. – Vol. 5 N. 1, P. 1-41.

2. Талаева, Т. В. Механизмы взаимодействия клеток крови и сосудистой стенки в реализации воспалительного и иммунного ответов./ Т. В Талаева // Укр. Ревматологічний журнал. – 2001– 3-4 (5-6). – C. 45-52.

3. Hynes, R.O. Integrins: bidirectional, allosteric signaling machines./ Hynes, R.O. // Cell – 2002. – Vol. 110, P. 673–687.

4. Activated human platelets express beta2 integrin. / M. M. Philippeaux [et al.] // Eur J Haematol, – 1996. – Vol. 56, P. 130–137.

5. The I domainis a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands. / M. S. Diamond [et al.] // J. Cell Biol, – 1993. – Vol. 120, P. 1031–1043.

6. Travis, M. A., An unraveling tale of how integrins areactivated from within. / M. A. Travis, J. D. Humphries, M. J. Humphries // Trends Pharmacol Sci – 2003. – Vol. 24, P. 192–197.

7. Liu, S, Integrin cytoplasmic domain-binding proteins. / S. Liu, D. A. Calderwood, M. H. Ginsberg // J Cell Sci – 2000. – Vol. 113, P. 3563–3571.

8. New fundamentals in hemostasis. / H. H. Versteeg [et al.] // Physiological reviews – 2013. – Vol. 93, N. 1, P. 327-358.

9. Plow, E.F. The role of RIAM in platelets put to a test. / E.F. // Blood – 2015. – Vol. 125, N. 2, P. 207-208.

10. Talin binding to integrin beta tails: a final common step in integrin activation / Tadokoro S. [et al.] // Science – 2003. – Vol. 302. – N. 5642. – P. 103–106.

11. Shattil, S. J. The final steps of integrin activation: the end game. / S. J. Shattil, C. Kim, M. H. Ginsberg // Nature reviews Molecular cell biology – 2010. – Vol. 11 N. 4, P. 288–300.

12. Analysis of GPIIb/IIIa receptor number by quantification of 7E3 binding to human platelets / Wagner C. L. [et al.] // Blood – 1996. – Vol. 88, P. 907–914.

13. Kamata, T Platelet integrin alphaIIbbeta3-ligand interactions: what canwe learn from the structure? / T. Kamata, Y. Takada // Int J Hematol, – 2001. – Vol. 74, P. 382–389.

14. Yousuf, O. The evolution of antiplatelet therapy in cardiovascular disease. / O. Yousuf, D.L. Bhatt // Nat. Rev. Cardiol. – 2011. – Vol. 8, P. 547–559.

15. Nieswandt, B Platelet-collagen interaction: is GPVI the central receptor? / B. Nieswandt, S. P. Watson // Blood, – 2003. – Vol. 102, P. 449–461.

16. Platelet adhesionto laminin: role of Ca2+ and Mg2+ ions, shear rate, and platelet-membrane glycoproteins. / G. Hindriks [et al.] // Blood – 1992. – Vol. 79, P. 928–935.

17. Piguet, P. F Beta2 integrin modulates platelet caspase activationand life span in mice. / P. F. Piguet, C. Vesin, A. Rochat // Eur J Cell Biol – 2001. – Vol. 80, P. 171–177.

18. Characterization of plasminogen as an adhesive ligand for integrins αM β2 (Mac-1) and α5 β1 (VLA-5). / V. K. Lishko // Blood – 2004. – Vol. 104, N. 3, P. 719-726.

19. Miles, L. A. Binding and activation of plasminogen on the platelet surface. / L. A. Miles, & E. F. Plow // The Journal of Biological Chemistry. – 1985. – Vol. 260, N. 7, P. 4303–4311.

20. Лысова Е.И. Превращение GIu-плазминогега в Lys-плазминоген на поверхности / Е.И. Лысова, О.В., Савчук, В.Н. Рубашик // Современные проблемы биохимии. – Гродно, 2016. – С. 105-111.

21. Roka-Moya, Y. M. Plasminogen/plasmin influence on platelet aggregation. / Y. M. Roka-Moya, D. D. Zhernossekov, T. V. Grinenko // Biopolymers and Cell. – 2012. – Vol. 28. – N. 5. – P. 352-356.

22. Schafer, A. I. Plasmin inhibition of platelet function and of arachidonic acid metabolism. / A. I. Schafer, B. Adelman // J.Clin. Invest., – 1985. – Vol. 75, N. 2, P. 456-461.

23. Ervin A. L. Platelet activation by sustained exposure to low-dose plasmin. / A. L. Ervin, E. I. Peerschke // Blood Coagul.Fibrinolysis. – 2001. – Vol. 12, N. 6, P. 415-425.

24. Platelet protein phosphorylation, elevation of cytosolic calcium, and inositol phospholipid breakdown in platelet activation induced by plasmin. / Schafer A. I. [et al.] // J.Clin. Invest. – 1986. – Vol. 78 – N. 1. – P. 73-79.

25. Rabhi-Sabile , S. Exposure of human platelets to plasmin results in the expression of irreversibly active fibrinogen receptors. / S. Rabhi-Sabile, D. Pidard // Thromb. Haemost., – 1995. – Vol. 73. – N. 4. – P. 693–701.

26. Pasche, B. Structural changes in platelet glycoprotein IIb/IIIa by plasmin: determinants and functional consequences. / B. Pasche // Blood. – 1994. – Vol. 83. – N. 2. – P. 404–414.

27. Limited plasmin proteolysis of vitronectin. Characterization of the adhesion protein as morpho-regulatory and angiostatin-binding factor. / C. Kost [et al.] // Eur. J. Biochem. – 1996. – Vol. 236. – P. 682-688.

28. Plasma osteopontin. Associations with survival and metastasis to bone in men with hormone-refractory prostate carcinoma. / S. J. Hotte [et al.] // Cancer. – 2002. – Vol. 95. – N. 3. – P. 506-512.

29. Osteopontin plasma levels and accelerated atherosclerosis in patients with CAD undergoing PCI: a prospective clinical study. / A. Mazzone [et al.] // Coron. Arter. Dis. – 2011. – Vol. 22. – N. 3. – P. 179-187.

30. Tesfamariam, B. Involvement of platelets in tumor cell metastasis. / B. Tesfamariam // Pharmacol. Ther. – 2016. – Vol. 157. – P. 112–119.

31. Expression and function of the high affinity αIIbβ3 integrin in murine melanoma cells. / J. Timar [et al.] // Clin. Exp. Metastasis. – 1998. – Vol. 16. – P. 437–445.

32. Placke, T. The wolf in sheep’s clothing: Platelet-derived “pseudo self” impairs cancer cell “missing self” recognition by NK cells. / T. Placke, H.G. Kopp, H.R. Salih // Oncoimmunology – 2012. – Vol. 1, P. 557–559.

33. Platelets mediate tumor cell adhesion to the subendothelium under flow conditions: Involvement of platelet GPIIb-IIIa and tumor cell α(v) integrins. / R. Dardik [et al.] // Int. J. Cancer. – 1997. – Vol. 70. – P. 201–207.

34. The disintegrin domain of ADAM9: A ligand for multiple beta1 renal integrins. / R.M. Mahimkar [et al.] // Biochem. J. – 2005. – Vol. 385. – P. 461–468.

35. Platelet integrin in tumor metastasis: do they represent a therapeutic target? / Lavergne M. [et al.] // Cancers (Basel) – 2017. – Vol. 9, N 10, Е133.

References

1. Homrich M., Gotthard I., Wokst H., & Diestel S. (2016). Cell adhesion molecules and ubiquitination-functions and significance. Biology, 2016, Vol. 5, no. 1, pp. 1-41.

2. Talaeva T.V. Mekhanizmy vzaimodeystviya kletok krovi i sosudistoy stenki v realizatsii vospalitel’nogo i immunnogo otvetov [The mechanisms of blood cells and vascular wall interaction in realization of inflammatory and
immune responses]. Ukr. Revmatologíchniy zhurnal. [Ukr. Rheumatology magazine.], 2001, Vol. 3-4, no. 5-6, pp. 45-52 (In Russian)

3. Hynes RO. Integrins: bidirectional, allosteric signaling machines. Cell, 2002, Vol. 110, pp. 673–687.

4. Philippeaux M. M, Vesin C, Tacchini-Cottier F, & Piguet P. F. Activated human platelets express beta2 integrin. Eur J Haematol, 1996, Vol. 56, pp. 130–137.

5. Diamond M. S., Garcia-Aguilar J, Bickford J. K, Corbi A. L, & Springer T. A. (1993). The I domainis a major recognition site on the leukocyte integrin Mac-1 (CD11b/CD18) for four distinct adhesion ligands. J. Cell Biol,
1993, Vol. 120, pp. 1031–1043.

6. Travis M. A., Humphries J. D., & Humphries M. J. An unraveling tale of how integrins areactivated from within. Trends Pharmacol Sci, 2003, Vol. 24, pp. 192–197.

7. Liu S, Calderwood D. A., & Ginsberg M. H. Integrin cytoplasmic domain-binding proteins. J Cell Sci, 2000, Vol. 113, pp. 3563–3571.

8. Versteeg H. H. New fundamentals in hemostasis. [et al.] Physiological reviews, Vol. 93, no. 1, pp. 327-358.

9. Plow EF, Qin J. The role of RIAM in platelets put to a test. Blood, 2015, Vol. 93, no. 1, pp. 327-358.

10. Tadokoro S. (2003). Talin binding to integrin beta tails: a final common step in integrin activation [Tadokoro S. et al.] Science, 2003, Vol. 125, no. 2, pp. 207-208.

11. Shattil S. J., Kim C., & Ginsberg M. H. The final steps of integrin activation: the end game. Nature reviews Molecular cell biology, 2010, Vol. 11, no. 4, pp. 288–300.

12. Wagner C. L., Mascelli M. A., Neblock D. S., Weisman H. F., Coller B. S., & Jordan R. E. Analysis of GPIIb/IIIa receptor number by quantification of 7E3 binding to human platelets. Blood, 1996, Vol. 88, pp. 907–914.

13. Kamata T, & Takada Y. Platelet integrin alphaIIbbeta3-ligand interactions: what canwe learn from the structure? Int J Hematol, 2001, Vol. 74, pp. 382–389.

14. Yousuf O., Bhatt D.L. The evolution of antiplatelet therapy in cardiovascular disease. Nat. Rev. Cardiol. 2011, Vol. 8 pp. 547–559.

15. Nieswandt B, & Watson S. P. Platelet-collagen interaction: is GPVI the central receptor? Blood, 2003, Vol. 102, pp. 449–461.

16. Hindriks G, Ijsseldijk M. J., Sonnenberg A, Sixma J. J., & de Groot P. G. Platelet adhesionto laminin: role of Ca2+ and Mg2+ ions, shear rate, and platelet-membrane glycoproteins. Blood, 1992, Vol. 79, pp. 928–935.

17. Piguet P. F, Vesin C, & Rochat A. Beta2 integrin modulates platelet caspase activationand life span in mice. Eur J Cell Biol, 2001, Vol. 80, pp. 171–177.

18. Lishko V. K., Novokhatny V. V., Yakubenko V. P., Skomorovska-Prokvolit H. V., & Ugarova T. P. Characterization of plasminogen as an adhesive ligand for integrins αM β2 (Mac-1) and α5 β1 (VLA-5). Blood, 2004, Vol. 104, no. 3, pp. 719-726.

19. Miles L. A., & Plow E. F. (1985). Binding and activation of plasminogen on the platelet surface. The Journal of Biological Chemistry, 1985, Vol. 260, no. 7, pp. 4303–4311.

20. Iusova E. I., Savchuk О. V., Rybachuk V. N. Prevrashchenie Glu-plazminogena v Lys-plasminogen na poverkhnosti trombotsitov. [Conversation of Ghu-plasminogen into Lys-plasminogen on the platelet cell surface].
Sovremennye problemy biokhimii [Modern problems of Biochemistry]. Eds. L.I. Nadol’nik et al. Grodno, 2016, pp.105-111. (In Russian)

21. Roka-Moya Y. M. Zhernossekov D. D, Grinenko T. V. Plasminogen/plasmin influence on platelet aggregation. Biopolymers and Cell. 2012, Vol. 28, no.5, pp.352-356.

22. Schafer A. I., & Adelman B. Plasmin inhibition of platelet function and of arachidonic acid metabolism. J.Clin. Invest. 1985, Vol. 75, no. 2, pp. 456-461.

23. Ervin A. L., & Peerschke E. I. Platelet activation by sustained exposure to low-dose plasmin. Blood Coagul.Fibrinolysis. 2001, Vol. 12, no. 6, pp. 415-425.

24. Schafer A. I., Maas A. K., Ware J. A., Johnson P. C., Rittenhouse S. E., & Salzman W. Platelet protein phosphorylation, elevation of cytosolic calcium, and inositol phospholipid breakdown in platelet activation induced by plasmin. J.Clin. Invest. 1986, Vol. 78, no. 1, pp. 73-79.

25. Rabhi-Sabile S., & Pidard D. Exposure of human platelets to plasmin results in the expression of irreversibly active fibrinogen receptors. Thromb. Haemost. 1995, Vol. 73, no. 4, pp. 693–701.

26. Pasche B. Structural changes in platelet glycoprotein IIb/IIIa by plasmin: determinants and functional consequences. Blood. 1994, Vol. 83, no. 2, pp. 404–414.

27. Kost C., Benner K., Stockmann A, Linder D., & Preissner K. T. Limited plasmin proteolysis of vitronectin. Characterization of the adhesion protein as morpho-regulatory and angiostatin-binding factor. Eur. J. Biochem. 1996, Vol. 236, pp. 682-688.

28. Hotte S. J., Winquist E. W., Stitt L., Wilson S., & Chambers A. F. Plasma osteopontin. Associations with survival and metastasis to bone in men with hormone-refractory prostate carcinoma. Cancer. 2002, Vol. 95, no. 3, pp. 506-512.

29. Mazzone A., Parri M. S., Giannesi D., Ravani M., Vagnetti M., Altieri P., Casalino L., Maltinti M., Balbi M., Barsotti A., & Berti S. (2011). Osteopontin plasma levels and accelerated atherosclerosis in patients with CAD undergoing PCI: a prospective clinical study. Coron. Arter. Dis. 2011, Vol. 22, no. 3, pp. 179-187.

30. Tesfamariam B. Involvement of platelets in tumor cell metastasis. Pharmacol. Ther. 2016, Vol. 157, pp. 112–119.

31. Timar J., Trikha M., Szekeres K., Bazaz R., Honn K. Expression and function of the high affinity αIIbβ3 integrin in murine melanoma cells. Clin. Exp. Metastasis. 1998, Vol. 16, pp. 437–445.

32. Placke T., Kopp H.G., Salih H.R. The wolf in sheep’s clothing: Platelet-derived “pseudo self” impairs cancer cell “missing self” recognition by NK cells. Oncoimmunology. 2012, Vol. 1, pp. 557–559.

33. Dardik R., Kaufmann Y., Savion N., Rosenberg N., Shenkman B., Varon D. Platelets mediate tumor cell adhesion to the subendothelium under flow conditions: Involvement of platelet GPIIb-IIIa and tumor cell α(v) integrins. Int. J. Cancer. 1997, Vol. 70, pp. 201–207.

34. Mahimkar R.M., Visaya O., Pollock A.S., Lovett D.H. The disintegrin domain of ADAM9: A ligand for multiple beta1 renal integrins. Biochem. J. 2005, Vol. 385, pp. 461–468.

35. Lavergne M., Janus-Bell E., Schaff M., Gachet C., Mangin P.H. Platelet integrin in tumor metastasis: do they represent a therapeutic target? Cancers (Basel). 2017, Vol. 9, no. 10, Е133.
Опубликован
2019-06-13
Выпуск
Раздел
Биологические науки