Activity of MMP and content of TIMP and some proteoglycan components were measured in the liver, lungs, and spleen of BALB/c mice aging 2, 6, and 12 months. The increase in the content of proteoglycan components in mouse organs was associated with age-related changes in MMP activity and TIMP-1 and TIMP-2 levels. The ratio between MMP activity and content of TIMP-1 and TIMP-2 differed in the studied organs. The levels of TIMP-1 and TIMP-2 in mouse blood serum and their concentration in studied organs changed asynchronously with age. They are important regulators that determine MMP activity in the analyzed age periods in mice, which can be determined as periods of growth, development, and ageing.
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C. Y. Bae, Y. G. Kang, M. H. Piao, B. Cho, K. H. Cho, Y. K. Park, B. Y. Yu, S. W. Lee, M. J. Kim, S. H. Lee, Y. J. Kim, D. H. Kim, J. S. Kim, and J. E. Oh, Models for estimating the biological age of five organs using clinical biomarkers that are commonly measured in clinical practice settings. Maturitas, 75, No. 3, 253-260 (2013).
T. Bitter and H. M. Muir, A modified uronic acid carbazole reaction. Anal. Biochem., 4, 330-334 (1962).
J. C. de Grauw, C. H. van de Lest, and, R. van Weeren, Inflammatory mediators and cartilage biomarkers in synovial fluid after a single inflammatory insult: a longitudinal experimental study. Arthritis Res. Ther., 11, No. 2, R35 (2009).
S. Georges, D. Heymann, and M. Padrines, Modulatory effects of proteoglycans on proteinase activities. Methods Mol. Biol., 836, 307-322 (2012).
L. B. Kim, V. A. Shkurupy, and A. N. Putyatina, Serum, liver, and lung levels of the major extracellular matrix components at the early stage of BCG-induced granulomatosis depending on the infection route. Bull. Exp. Biol. Med., 158, No. 3, 322-325 (2015).
K. Komosinska-Vassev, P. Olczyk, K. Winsz-Szczotka, K. Klimek, and K. Olczyk, Age- and gender-dependent changes in circulating concentrations of tumor necrosis factor-α, soluble tumor necrosis factor receptor-1 and sulfated glycosaminoglycan in healthy people. Clin. Chem. Lab. Med., 49, No. 1, 121-127 (2011).
K. Komosinska-Vassev, P. Olczyk, K. Winsz-Szczotka, K. Kuznik-Trocha, K. Klimek, and K. Olczyk, Age- and genderdependent changes in connective tissue remodeling: physiological differences in circulating MMP-3, MMP-10, TIMP-1 and TIMP-2 level. Gerontologe, 57, No. 1, 44-52 (2011).
J. H. Roe, The determination of sugar in blood and spinal fluid with anthrone reagent. J. Biol. Chem., 212, No. 1, 335-343 (1955).
M. H. Tayebjee, G. Y. Lip, A. D. Blann, and R. J. Macfadyen, Effects of age, gender, ethnicity, diurnal variation and exercise on circulating levels of matrix metalloproteinases (MMP)-2 and -9, and their inhibitors, tissue inhibitors of matrix metalloproteinases (TIMP)-1 and -2. Thromb. Res., 115, No. 3, 205-210 (2005).
A. Tocchi, W. Parks, Functional interactions between matrix metalloproteinases and glycosaminoglycans. FEBS J., 280, No. 10, 2332-2341 (2013).
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Translated from Byulleten’ Eksperimental’noi Biologii i Meditsiny, Vol. 161, No. 1, pp. 40-45, January, 2016
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Kim, L.B., Shkurupy, V.A. & Putyatina, A.N. Age-Related Changes in the System Metalloproteinases/Tissue Metalloproteinase Inhibitors and Proteoglycan Components in Mouse Organs. Bull Exp Biol Med 161, 32–36 (2016). https://doi.org/10.1007/s10517-016-3338-x
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DOI: https://doi.org/10.1007/s10517-016-3338-x