Optimal concentration of cellular free calcium for AVP-induced cAMP in collecting tubules
作者： San-e Ishikawa , Toshikazu Saito
DOI: 10.1038/KI.1990.86
关键词: Kidney 、 Calcium 、 Renal papilla 、 Ionomycin 、 Endocrinology 、 Vasopressin 、 Arginine 、 Internal medicine 、 Chemistry 、 Fluorescence spectrometry 、 EGTA 、 Nephrology
摘要: Optimal concentration of cellular free calcium for AVP-induced cAMP in collecting tubules. The role Ca 2+ the action arginine vasopressin (AVP) has been demonstrated renal papillary tubule. We further examined whether an optimal ([Ca ]i) exists production rat tubule cells culture. [Ca ]i was measured using fura-2. When were exposed one hour to media supplemented with 0mM (containing 1mM EGTA), 1, 2, 3, 4, 6.4, or 8mM , basal ranged as below: 24.9 ± 5.6, 90.7 7.4, 107.4 9.8, 146.1 13.7, 162.0 14.6, 241.5 32.8, and 234.9 29.6 nM, respectively. medium 1 mM, × 10 −7 M AVP increased 181.5 13.2nM from 7.4nM (P obtained varying described above, though increases quantitatively variable. during three minute incubation period presence 5 −4 3-isobutyl-l-methylxanthine. Basal level 87.6 7.9 fmol/µg protein. After exposing containing levels −9 107.9 11.6 (0mM medium), 175.6 14.1 (1mM ), 198.8 9.8 (2mM 134.4 10.2 (3mM 175.3 21.1 (4mMCa 146.7 13.8 (6.4mM 59.5 9.5fmol/µtg protein (8mM between response maximal. Similar results AVP. Cells incubated 2 −6 ionophore ionomycin hour, then elevated 675.8 93.7nM. In this condition increase disappeared totally. Cellular 112.5 3.6 206.0 14.4 respectively, values significantly less than 215.0 9.3 506.3 33.5 control groups. These therefore indicate that there is cells.
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sci-hub.se 参考文章(28)
D.A. Ausiello, D. Hall, Regulation of vasopressin-sensitive adenylate cyclase by calmodulin. Journal of Biological Chemistry. ,vol. 256, pp. 9796- 9798 ,(1981) , 10.1016/S0021-9258(19)68693-X
Benedict J. Campbell, Gerald Woodward, Victoria Borberg, Calcium-mediated Interactions between the Antidiuretic Hormone and Renal Plasma Membranes Journal of Biological Chemistry. ,vol. 247, pp. 6167- 6175 ,(1972) , 10.1016/S0021-9258(19)44778-9
A. Lewis Farr, Oliver H. Lowry, Rose J. Randall, Nira J. Rosebrough, Protein Measurement with the Folin Phenol Reagent Journal of Biological Chemistry. ,vol. 193, pp. 265- 275 ,(1951)
P. J. BENTLEY, THE EFFECTS OF IONIC CHANGES ON WATER TRANSFER ACROSS THE ISOLATED URINARY BLADDER OF THE TOAD BUFO MARINUS Journal of Endocrinology. ,vol. 18, pp. 327- 333 ,(1959) , 10.1677/JOE.0.0180327
SAN-E ISHIKAWA, TOSHIKAZU SAITO, Enhancement by veratridine and 60 mM KCl of vasopressin-induced 3',5'-cyclic adenosine monophosphate production and cellular free calcium concentration in rat renal papillary collecting tubule cells in culture. Endocrinology. ,vol. 124, pp. 265- 271 ,(1989) , 10.1210/ENDO-124-1-265
Y Ando, H R Jacobson, M D Breyer, Phorbol ester and A23187 have additive but mechanistically separate effects on vasopressin action in rabbit collecting tubule. Journal of Clinical Investigation. ,vol. 81, pp. 1578- 1584 ,(1988) , 10.1172/JCI113491
San-e Ishikawa, Toshikazu Saito, Takeshi Kuzuya, Reversal of somatostatin inhibition of AVP-induced cAMP by pertussis toxin Kidney International. ,vol. 33, pp. 536- 542 ,(1988) , 10.1038/KI.1988.31
Dennis A. Ausiello, Karl L. Skorecki, Alan S. Verkman, Joseph V. Bonventre, Vasopressin signaling in kidney cells Kidney International. ,vol. 31, pp. 521- 529 ,(1987) , 10.1038/KI.1987.31
Holm Holmsen, Inger Holmsen, Arvid Bernhardsen, Microdetermination of adenosine diphosphate and adenosine triphosphate in plasma with the firefly luciferase system Analytical Biochemistry. ,vol. 17, pp. 456- 473 ,(1966) , 10.1016/0003-2697(66)90181-3
Katsuji Takeda, Shozo Torikai, Yasushi Asano, Masashi Imai, Modulation by verapamil of hormonal action on the Henle's loop of mice Kidney International. ,vol. 29, pp. 863- 869 ,(1986) , 10.1038/KI.1986.78