: ., ., . ., ., ., . . , . . , , ( . ) — , , , , [1, 2]. , , , [2, 9, 10]. (2000), . — , [3]. 200 , [1]. , , . . ( ), , , 50 % , , , , , , . , , [3]. , , . , . . , . . , , [4]. , , . ( , , ) , , , ( ) , , , , , (Mg, Ca, K, Na). , — , . 20 ( [5]. 50) [6]. — , . — — . , , [1]. — , ( ) ) 200 . , ( ( ). (25 ). — (T ). . T , , , « , - , » [7, 8]. , — . . . . , , ( (Mg2+) , , ). , , , . . % ( Mg2+-AT , , , , , 90 % , 50 % (30 % 53 20 % — , ). , 10 % 10 % ) [9–11]. . , , ( ) , , [12]. , . transient receptor potential cation channel 6) . TRPM6 — TRPM7, [13]. TRPM6 , TRPM7. TRPM6 TRPM6 ( [14]. TRPM7 , TRPM6/TRPM7 [15]. SLC41A1 ( SLC41A1 41.1): , [16]. ( CASR), . CASR ( ), , [17]. , . , . snRNA) [18]. ( , ( , , ). , , , , . . HAS1, HAS2 HAS3 ( , [19]. . , ) ( ). , . , , . , . ( ) . MMP2 MMP9 [20]. MMP2 [21]. , , , ( , ( ), ) . . — . ( 2–3 ) [22]. . — , , [23, 24]. M , (LOX) [25], . , , , , , », « , . , , : 1) — , 2) , 3) , 4) . , , . , , , , . , . ; , [1–3]: , , , , , , , ; ( ; « , » , ), II, , , , - » 1- , II ; V ; ; ; , IV I, « , , , , , ; , I , 90°, 10°, , 45°, ; , , , - , , , , , ; . [1–3]: 1) : ) — , 10 , , , , ; ) — 10 ; ) , ; , , , , — — , ) , , ; ) — , , , , ; ) — , , , , , , ; 2) , : , , ; 3) , : ; 4) . , : , , 200 , . : . , , ( — .). « »( . ). [7], ( ) , . [1–3]. . , . . , . 1. . 2. ., 3. 4. 5. 6. 7. 8. 44-47. . ? // . . . — 2008. — 1. — . 67-74. // Doctor. — 2004. — 1. — C. . , , , . — .: , 2000. — 270 . . .— — : , 2000. — 507 . Simon D.B., Lu Y., Choate K.A. et al. Paracellin-1, a renal tight junction protein required for paracellular Mg2+ resorption // Science. — 1999. — Vol. 285, 5424. — P. 103-106. Meij I.C., Koenderink J.B., Van Bokhoven H. et al. Dominant isolated renal magnesium loss is caused by misrouting of the Na(+), K(+)-ATPase gamma-subunit // Nat. Genet. — 2000. — V. 26, 3. — P. 265-266. Cauwe B., Van den Steen P.E., Opdenakker G. The biochemical, biological, and pathological kaleidoscope of cell surface substrates processed by matrix metalloproteinases // Crit. Rev. Biochem. Mol. Biol. — 2007. — Vol. 42, 3. — P. 113-185. Malemud C.J. Matrix metalloproteinases (MMPs) in health and disease: an overview // Front Biosci. — 2006. — Vol. 11, 1696. — P. 1696-1701. 9. . .— , 2000. — 272 . 10. Senni K., Foucault-Bertaud A., Godeau G. Magnesium and connective tissue // Magnes Res. — 2003. — Vol. 16, 1. — P. 70-74. 11. . : . — .: , 2006. — 234 . 12. Quamme G.A., de Rouffignac C. Epithelial magnesium transport and regulation by the kidney // Front Biosci. — 2000. — 5. — P. D694-D711. 13. Chubanov V., Waldegger S., Mederos y Schnitzler M. Disruption of TRPM6/TRPM7 complex formation by a mutation in the TRPM6 gene causes hypomagnesemia with secondary hypocalcemia // Proc. Natl. Acad Sci USA. — 2004. — Vol. 101, 9. — P. 2894-9. 14. Schlingmann K.P., Weber S., Peters M. et l. Hypomagnesemia with secondary hypocalcemia is caused by mutations in TRPM6, a new member of the TRPM gene family // Nat. Genet. — 2002. — Vol. 31, 2. — P. 166-170. 15. Wang Z., Hu S.Y., Lei D.L. Effect of chronic stress on PKA and P-CREB expression in hippocampus of rats and the antagonism of antidepressors Zhong Nan Da Xue Xue Bao Yi Xue Ban // Nat. Genet. — 2006. — Vol. 31, 5. — P. 767-771. 16. Goytain A., Quamme G.A. Functional characterization of human SLC41A1, a Mg2+ transporter with similarity to prokaryotic MgtE Mg2+ transporters // Physiol. Genomics. — 2005. — Vol. 21, 3. — P. 337-342. 17. Nagase T., Murakami T., Tsukada T. et al. A family of autosomal dominant hypocalcemia with a positive correlation between serum calcium and magnesium: identification of a novel gain of function mutation (Ser(820)Phe) in the calcium-sensing receptor // J. Clin. Endocrinol. Metab. — 2002. — Vol. 87, 6. — P. 2681-2687. 18. Van Venrooij W.J. Autoantibodies against small nuclear ribonucleoprotein components // J. Rheumatol. Suppl. — 1987. — 14. — P. 78-82. 19. Mio K., Carrette O., Maibach H.I. et al. Evidence that the serum inhibitor of hyaluronidase may be a member of the inter-alpha-inhibitor family // J. Biol. Chem. — 2000. — Vol. 275, 42. — P. 32413-32421. 20. Pages N., Gogly B., Igondjo-Tchen S. et al. Structural alterations of the vascular wall in magnesium-deficient mice. A possible role of gelatinases A (MMP-2) and B (MMP-9) // Magnes Rus. — 2003. — Vol. 16, 1. — P. 43-48. 21. Yue H., Lee J.D., Shimizu H. et al. Effects of magnesium on the production of extracellular matrix metalloproteinases in cultured rat vascular smooth muscle cells // Atherosclerosis. — 2003. — Vol. 166, 2. — P. 271-277. 22. Lefebvre F., Graves P.V. et al. Magnesium enhances human pancreatic elastase digestion of 125I-labeled elastin // Experientia. — 1985. — Vol. 41, 5. — P. 628-631. 23. Ahvazi B., Boeshans K.M., Rastinejad F. The emerging structural understanding of transglutaminase 3 // J. Struct. Biol. — 2004. — Vol. 147, 2. — P. 200-207. 24. Ahvazi B., Boeshans K.M., Idler W. et al. Roles of calcium ions in the activation and activity of the transglutaminase 3 enzyme // J. Biol. Chem. — 2003. — Vol. 278, 26. — P. 23834-23841. 25. Gacheru S.N., Trackman P.C., Shah M.A. et al. Structural and catalytic properties of copper in lysyl oxidase // J. Biol. Chem. — 1990. — Vol. 265, 31. — P. 19022-19027.