UDC 61

CLEARANCE OF CARBONYL-MODIFIED LIPOPROTEINS FROM THE BLOODSTREAM OF RABBITS

Published в Acta biomedica scientifica · Volume 1, Issue 3, p. 2, 2017 · Pages 104–108 · Rubrics: Experimental Study in biology and medicine
DOI 10.12737/article_590823a4b59f98.13160142
Received: 27.04.2017 Accepted: 02.05.2017 Published: 02.05.2017
Authors
1 Russian Cardiology Research and Production Complex (laborant-issledovatel')
Moskv, Moscow, Russian Federation
2 Russian Cardiology Research and Production Complex (zaveduyuschiy laboratoriey)
Moskva, Moscow, Russian Federation
3 Russian Cardiology Research and Production Complex (starshiy nauchnyy sotrudnik)
Moskva, Moscow, Russian Federation
4 Institute of Clinical Cardiology (laboratoriya biohimii svobodnoradikal'nyh processov, veduschiy nauchnyy sotrudnik)
Moskva, Moscow, Russian Federation
5 E.I. Chazov National Medical Research Centre of Cardiology (otdel biohimii svobodnoradikal'nyh processov)
Moscow, Moscow, Russian Federation
Issledovali klirens al'degid-modificirovannyh lipoproteidov nizkoy plotnosti (LNP) u krolikov s ispol'zovaniem izolirovannyh pri pomoschi preparativnogo ul'tracentrifugirovaniya biotinilirovannyh LNP krolikov i FITC-mechenyh LNP cheloveka. Glioksal'- i metilglioksal'-modificirovannye LNP krolikov i cheloveka cirkuliruyut v krovotoke takoe zhe vremya, chto i nativnye LNP. MDA-modificirovannye LNP bystro eliminiruyutsya iz krovotoka. Veroyatno, glioksal'- i metilglioksal'-modificirovannye LNP bolee aterogenny, v to vremya kak MDA-modificirovannye LNP mogut podvergat'sya usilennoy utilizacii.
okislitel'nyy stress modificirovannye lipoproteidy nizkoy plotnosti malonovyy dial'degid glioksal' metilglioksal' ateroskleroz saharnyy diabet
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References

1. Lankin VZ, Tikhaze AK, Kapelko VI, Shepelkova GS, Shumaev KB, Panasenko OM, Konovalova GG, Belenkov YN (2007). The mechanisms of oxidative modification of LDL under oxidative and carbonyl stress [Mekhanizmy okislitel’noy modifikatsii lipoproteidov nizkoy plotnosti pri okislitel’nom i karbonil’nom stresse]. Biokhimiya, 72 (10), 1330-1341.

2. Bayer EA, Wilchek M (1990). Protein biotinylation. Meth. Enzymol., (184), 138-160.

3. Cartun RW, Pedersen CA (1989). An immunocytochemical technique offering increased sensitivity and lowered cost with a streptavidin-horseradish peroxidase conjugate. J. Histotechnol., 12 (4), 273-277.

4. Goldstein JL, Brown MS (2009). History of discovery: the LDL receptor. Arterioscler. Thromb. Vasc. Biol., 29 (4), 431-438.

5. Gylling H, Kontula K, Miettinen TA (1995). Cholesterol absorption and metabolism and LDL kinetics in healthy men with different apoprotein E phenotypes and apoprotein B Xba I and LDL receptor Pvu II genotypes. Arterioscler. Thromb. Vasc. Biol., (15), 208-213.

6. Jomova K, Valko M (2011). Advances in metalinduced oxidative stress and human disease. Toxicology, 283 (2-3), 65-87.

7. Lankin VZ, Tikhaze AK (2003). Free radical lipoperoxidation during atherosclerosis and antioxidative therapy of this disease. Free Radicals, Nitric Oxide, and Inflammation: Molecular, Biochemical, and Clinical Aspects (Tomasi A (eds.) et al.). NATO Science Series, (344), 218-231.

8. Lankin VZ, Konovalova GG, Tikhaze AK, Shumaev KB, Kumskova EM, Viigmaa M (2014). The initiation of free radical peroxidation of low-density lipoproteins by glucose and its metabolite methylglyoxal: a common molecular mechanism of vascular wall injure in atherosclerosis and diabetes. Mol. Cell. Biochem., 395 (1-2), 241-252.

9. Lankin VZ, Tikhaze AK, Konovalova GG, Kumskova EM, Shumaev KB (2010). Aldehyde-dependent modification of low-density lipoproteins. Handbook of lipoprotein research (Rathbound JE (ed.)), 85-107.

10. Lankin VZ, Tikhaze AK, Kumskova EM (2012). Macrophages actively accumulate malonyldialdehydemodified but not enzymatically oxidized low-density lipoprotein. Mol. Cell. Biochem., 365 (1-2), 93-98.

11. Lindgren FT (1975). Preparative ultracentrifugal laboratory procedures and suggestions for lipoprotein analysis. Analysis of lipids and lipoproteins (Perkins EG (ed.)). Amer. Oil. Chemists’ Soc., 204-224.

12. Miettinen TA, Gylling H, Vanhanen H, Ollus A (1992). Cholesterol absorption, elimination, and synthesis related to LDL kinetics during varying fat intake in men with different apoprotein E phenotypes. Arteriosclerosis Arterioscler. Thromb. Vasc. Biol., (12), 1044-1052.

13. Niedowicz DM, Daleke DL (2005). The role of oxidative stress in diabetic complications. Cell. Biochem. Biophys., 43 (2), 289-330.

14. Requena JR, Fu MX, Ahmed MU, Jenkins AJ, Lyons TJ, Baynes JW, Thorpe SR (1997). Quantification of malondialdehyde and 4-hydroxynonenal adducts to lysine residues in native and oxidized human low-density lipoprotein. Biochem. J., 322, 317-325.

15. Staines WA, Meister B, Melander T, Nagy JI, Hokfelt TJ (1988). Three-color immunofluorescence histochemistry allowing triple labeling within a single section. Histochem. Cytochem, (36), 145-151.

16. Tertov VV, Kaplun VV, Dvoryantsev SN, Orechov AN (1995). Apolipoprotein B-bound lipids as a marker for evaluation of low-density lipoprotein oxidation in vivo. Biochem. Biophys. Res. Commun., (214), 608-613.

17. Witz G (1989). Biological interactions of α,β-unsaturated aldehydes. Free Rad. Biol. Med., (7), 333-349.

18. Yla-Herttuala S (1991). Macrophages and oxidized low-density lipoproteins in the pathogenesis of atherosclerosis. Ann. Med., 23 (5), 561-567.

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