ProMMP-1 PRODUCTION BY CULTIVATED CELLS OF VASCULAR ENDОTHELIUM IN VITRO AND IN A HUMAN BODY

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Abstract. Matrix metalloproteinases (MMP) are structurally related endopeptidase composed of active sites which include ions Zn2+ and Ca2+. Cultured cells of human blood vessels produce MMP-1, proteolytic effect is aimed at splitting the collagen I and III types, and subsequent vascular remodeling. MMP-1 is synthesized as an inactive zymogen proMMP-1. It was shown that interferon alpha, beta and gamma inhibited production by culture of HUVEC proenzyme MMP-1, which seems to characterize their anti-angiogenic action. The effect of immunomodulators is more difficult to explain: perhaps inhibiting effect of imunofan and, as well as activating effect of cycloferon due to their internal structural peculiarities. The action of interferon alpha, beta and gamma, used as HUVEC before infection with HSV-1, and after it led to decrease in production proMMP-1. Apparently, the antiangiogenic effect of IFN is saved in the case of infection of cultures of vascular endothelium with HSV-1. Scatter in the content of proMMP-1 in the serum of blood donors was 1.625–11.8 ng/ml and in patients with chronic microbial-viral infections was 1.22–21.16 ng/ml. Higher rates of proMMP-1 were in older patients group. To estimate the system of MMP in vitro, and in the body a comprehensive study must be conducted, including proMMP-1, the active form of proenzyme and specific inhibitor of MMP-1.

About the authors

N. N. Scliankina

ФГБУ «НИИЭМ им. Н.Ф. Гамалеи» Минздравсоцразвития России

Email: scheglovitova@rambler.ru
Russian Federation

N. V. Boldyreva

ФГБУ «НИИЭМ им. Н.Ф. Гамалеи» Минздравсоцразвития России

Email: scheglovitova@rambler.ru
Russian Federation

A. A. Babayants

ФГБУ «НИИЭМ им. Н.Ф. Гамалеи» Минздравсоцразвития России

Email: scheglovitova@rambler.ru
Russian Federation

I. S. Frolova

ФГБУ «НИИЭМ им. Н.Ф. Гамалеи» Минздравсоцразвития России

Email: scheglovitova@rambler.ru
Russian Federation

D. L. Belyaev

ФГБУ «НИИЭМ им. Н.Ф. Гамалеи» Минздравсоцразвития России

Email: scheglovitova@rambler.ru
Russian Federation

Yu. A. Portnova

ФГБУ «НИИЭМ им. Н.Ф. Гамалеи» Минздравсоцразвития России

Email: scheglovitova@rambler.ru
Russian Federation

O. N. Scheglovitova

ФГБУ «НИИЭМ им. Н.Ф. Гамалеи» Минздравсоцразвития России

Author for correspondence.
Email: scheglovitova@rambler.ru

д.м.н., профессор, зав. лабораторией противовирусного иммунитета

123098, Москва, ул. Гамалеи, 18

Russian Federation

References

  1. Соловьева Н.И. Матриксные металлопротеиназы: регуляция активности и роль в процессе онкогенеза // Вопр. мед. химии. — 2000. — № 5. — С. 30–31.
  2. Bellon G., Martiny L., Robiner A. Matrix metalloproteinases and matrikines in angiogenesis // Crit. Rev. Oncol. Haemathol. — 2004. — Vol. 49, N 3. — P. 203–220.
  3. Birkedal-Hansen H., Moore W.G., Bodden M.K., Windsor L.J., Birkedal-Hansen B., DeCarlo A., Engler J.A. Matrix metalloproteinases: review // Crit. Rev. Oral. Biol. Med. — 1993. — Vol. 4, N 2. — P. 197–250.
  4. De Wever O., Derycke L., Hendrix A., De Meerleer G., Godeau F., Depypere H., Bracke M. Soluble cadherins as cancer biomarkers // Clin. Exp. Metastasis. — 2007. — Vol. 24, N 8. — P. 685–697.
  5. Egeblad M., Werb Z. New function for the matrix metalloproteinases in cancer progression // Nat. Rev. Cancer. — 2002. — N 2. — P. 161–174.
  6. Haas T.L. Endothelial cell regulation of matrix metalloproteinases // Can. J. Phisiol. Pharmacol. — 2005. — Vol. 83, N 1. — P. 1–7.
  7. Hayashida K., Bartlett A.H., Chen Y., Park P.W. Molecular and cellular machanisms of ectodomain shedding // Anat. Rec. — 2010. — Vol. 293, N 6. — P. 925–937.
  8. Heissig B., Hattori K., Friedrich M., Rafii S., Werb Z. Angiogenesis: vascular remodeling of the extracellular matrix involves metalloproteinases // Curr. Opin. Haemathol. — 2003. — Vol. 10, N 2. — P. 136–141.
  9. Malemud C.J. Matrix metalloproteinases (mmpS) in health and desease: overview // Front Biosci. — 2006. — N 11. — P. 1696–1701.
  10. Mott J.D., Werb Z. Regulation of matrix biology by matrix metalloproteinases // Curr. Opin. Cell Biol. — 2004. — Vol. 16, N 5. — P. 558–564.
  11. .Nagase H., Woessner J.F. Matrix metalloproteinases // J. Biol. Chem. — 1999. — Vol. 274, N 31. — P. 21491–21494.
  12. Ozato K., Taylor P., Kubota T. The interferon regulatory factor family in host defense: mechanism of action // J. Biol. Chem. — 2007. — Vol. 282, N 28. — P. 20065–20069.
  13. Parks W.S., Wilson C.L., Lopez-Boado Y.S. Matrix metalloproteinases as modulators of inflammation and innate immunity // Natl. Rev. Immunol. —2004. — Vol. 4, N 8. — P. 617–629.
  14. Scheglovitova O.N., Romanov Yu.A., Maksianina E.V., Kabaeva N.V., Pronin A.G. Herpes simplex type I virus infection of cultured human vascular endothelial cells: expression of cell adhesion molecules and induction of interferon and cytokine production by blood mononuclear cells // Russian J. Immunol. — 2001. — N 6. — P. 367–376.
  15. Woessner J. MMPs and TIMPs — an historical perspective // Mol. Biotechnol. — 2002. — Vol. 22, N 1. — P. 33–49.

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Copyright (c) 2014 Scliankina N.N., Boldyreva N.V., Babayants A.A., Frolova I.S., Belyaev D.L., Portnova Y.A., Scheglovitova O.N.

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