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ISSN 2522-9028 (Print)
ISSN 2522-9036 (Online)
DOI: https://doi.org/10.15407/fz

Fiziologichnyi Zhurnal

is a scientific journal issued by the

Bogomoletz Institute of Physiology
National Academy of Sciences of Ukraine

Editor-in-chief: V.F. Sagach

The journal was founded in 1955 as
1955 – 1977 "Fiziolohichnyi zhurnal" (ISSN 0015 – 3311)
1978 – 1993 "Fiziologicheskii zhurnal" (ISSN 0201 – 8489)
1994 – 2016 "Fiziolohichnyi zhurnal" (ISSN 0201 – 8489)
2017 – "Fiziolohichnyi zhurnal" (ISSN 2522-9028)

Fiziol. Zh. 2011; 57(3): 62-68


Altered collagene properties and lysyl oxidase activity during lathyrism

T.T. Volodina, N.D. Dzvonkevich, L.M. Petrun, I.P. Krisuk, N.M. Popova, S.G. Shandrenko,M.P. Dmytrenko.

    Ін-т біохімії ім. А.В. Палладіна НАН України, Київ


Abstract

Experiments were carried out on rats with lathyrism, which was induced by adding semicarbazide (0.075%) into drinking water for 45 days. The data obtained show a 30% reduction in the body weight and an increase in.organ weight coefficients. Semicarbazide intake led to the pelvic limb paralysis, scolio-sis, bone tissue degradation, cartilage growth, 46% decrease of the calcium level in the femur. It has been detected essential structural changes in extracellular matrix based on the collagen cross-links reduction. The activity of lysyl oxidase, a key enzyme for the collagen development, showed 5-fold decrease in the aorta tissues. The level of formaldehyde, a nonenzymic cross-links developer, has been measured in the liver tissue by the aldehyde trap (5,5-dimethylcyclohexane-1,3-dione) admin­istration and then fluorimetric determination of formal-dimedone. Under semicarbazide load, the formaldehyde level in the liver tissue was reduced by 47%. Therefore, semicarbazide influences not only the enzymic development of aldehyde groups in collagen, but the level of other alde­hydes, which can cause cross-links. This experimental model of lathyrism is appropriate for investigation of the lysyl oxi-dase inhibitors effect on extracellular matrix.

Keywords: lathyrism, semicarbazide, collagen, lysyl oxidase,cross-links, formaldehyde

References

  1. Володіна Т.Т., Печенова Т.М., Дзвонкевич Н.Д., Попова Н.М., Силонова Н.В., Астахова B.C., Панченко Л.М., Михайловський В.О., Гулий М.Ф. Модифікуюча дія низькомолекулярних метаболітів на стан позаклітинного матриксу тварин// Укр. біохім. журн. - 2007. - 79, №6. - С 52-65.
  2. Дмитренко М.П., Шандренко С.Г., Петрунь Л.М., Кішко Т.О., Сілонова Н.В., Латишко Н.В., Гудкова О.О., Сушкова В.В. Обмін формальдегіду за семікарбозид-ної інтоксикації // Там само. - 2010. - 82. - С 39-44.
  3. Зайдес А.Л., Михайлов А.Н., .Пушенко О.И. Модифицированный метод определения оксипро-лина// Биохимия. - 1964. - 29, №1. - C. 5-7.
  4. Меркурьева Р.В. Метод электрофоретического разделения гликозаминогликанов различных видов соединительной ткани и биологических жидкостей// Вопр. мед. химии. - 1975. - 21(4). –С. 423-428.
  5. Abe M., Takahashi M., Horiuchi K., Nagano A. The changes in crosslink contents in tissues after formalin fixation// Anal. Biochem. - 2003. - 318(1). - P.118-123.
  6. Barrow M.V., Simpson C.F., Miller E.J. Lathyrism: A Review //Quart. Rev. Biol. - 1974. - 49. - P. 101-128.
  7. Bondareva A., Downey Ch. M., Ayres F., Liu W., Boyd
  8. S. K., Hallgrimsson B., Jirik F.R. The lysyl oxidase inhibitor, beta-aminopropionitrile, diminishes the meta­static colonization potential of circulating breast cancer Cells//PLoS ONE. - 2009. - 4(5). - 5620. - P.1-10.
  9. El Rouby D.H., Bashir M.H., Korany N.S. Ultrastructural and histomorphometric alterations of rat jaw bones after experimental induction of lathyrism //Arch. Oral Biol. - 2008. - 53(10). - P. 916-923.
  10. 9. Erler J.T., Kevin L., Bennewith K.L., Nicolau M., Dornhofer N., Kong C, Le Q.T. Lysyl oxidase is es­sential for hypoxia-induced metastasis // Nature. -2006. - 440. - P.1222-1226.
  11. 10. Giampuzzi M., Oleggini R., Di Donato A. Altered adhe­sion features and signal transduction in NRK-49F cells transformed by down-regulation of lysyl oxidase // Biochim. Biophys. Acta. - 2003. - 1647. - P. 239-244.
  12. Harris E.D., Gonnerman W.A., Savage J.T. Connective tissue amine oxydase. Purification and partial characte­rization of lysyl oxydase from chick aorta // Ibid. - 1974. -341. - P. 332-344.
  13. Li W., Liu G., Chou I.N., Kagan H.M. Hydrogen per­oxide-mediated, lysyl oxidase-dependent chemotaxis of vascular smooth muscle cells // J. Cell Biochem. -2000. -78. - P. 550-557.
  14. Maki J.M, Sormunen R., Lippo S., Kaarteenaho-Wiik R., Soininen R., Myllyharju J. Lysyl Oxidase Is Essential for Normal Development and Function of the Respiratory System and for the Integrity of Elastic and Collagen Fi­bers in Various Tissues // Amer. J. Pathol. - 2005. - 167, № 4. - P.927-936.
  15. Maki J.M. Lysyl oxidases in mammalian development and certain pathological conditions // Histol Histo-pathol. - 2009. - 24(5). -P.651-660.
  16. Maranghi F., Tassinari R., Lagatta V. Effects of the food contaminant semicarbazide following oral admin­istration in juvenile Sprague-Dawley rats // Food and Chem.Tox. - 2009. - 47. - P.472-479.
  17. Kusama-Eguchi K.., Ikegami F., Kusama T., Suda A., Ogawa Y., Igarashi K., Watanabe K. A rat model of neurolathyrism: repeated injection of beta-ODAP in­duces the paraparesis of the hind legs // Amino Acids. -2005. - 28(2). - P.139-143.
  18. Palamakumbura A.H., Trackman PC. A Fluorometric as­say for detection of lysyl oxidase enzyme activity in biological samples // Anal. Biochem. - 2002. - 300. - P.245-251.
  19. Postovit L.M., Abbott D.E., Payne S.L., Wheaton W.W., Margaryan V. Hypoxia/reoxygenation: a dynamic regulator of lysyl oxidase-facilitated breast cancer migration // J. Cell Biochem. - 2008. - 103. - P.1369-1378.
  20. 19. Szarvas T., Szatloczky E., Volford J. Determination of endogenous formaldehyde level in human blood and urine by dimedone-14C radiometric // J. Radioanal. and Nucl. Chem. -1986. - 106(6). - P. 357-367.

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