К ВОПРОСУ О РОЛИ МАГНИЯ В ФОРМИРОВАНИИ ДИСПЛАЗИИ

реклама
:
.,
.,
.
.,
.,
.,
.
.
,
.
.
,
,
(
.
) —
,
,
,
,
[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.
Скачать