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OtherRENAL PHARMACOLOGY

Regulation of Renin Secretion Through Reversible Phosphorylation of Myosin by Myosin Light Chain Kinase and Protein Phosphatase Type 1

Mi Hyun Kim, Sun-Hee Kim, Hyun Sook Kim, Jai Won Chang, Yoo Sun Hong, Hae Won Kim and Chun Sik Park
Journal of Pharmacology and Experimental Therapeutics June 1998, 285 (3) 968-974;
Mi Hyun Kim
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Sun-Hee Kim
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Hyun Sook Kim
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Jai Won Chang
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Yoo Sun Hong
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Hae Won Kim
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Chun Sik Park
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Abstract

Possible involvement of reversible phosphorylation and dephosphorylation of myosin light chain (MLC) by myosin light chain kinase (MLCK) and protein phosphatases (PPases), respectively, in the Ca++-calmodulin-dependent inhibition of renin secretion was investigated with the use of putative MLCK inhibitor ML-7 [1-(5-iodonaphthalene-1-sulfonyl)-1H-hexahydro-1,4-diazepine] and PPase type1 (PPase-1) and type 2A (PPase-2A) inhibitor calyculin A. ML-7 (1 × 10−6 to 3 × 10−5 M) increased renin secretion in vitro from rat renal cortical slices under “resting” conditions in a concentration-dependent manner with maximal 2.5-fold stimulation. Furthermore, Ca++-induced inhibition of renin secretion in depolarizing K+-rich Krebs-Ringer bicarbonate not only was prevented completely but also reversed by ML-7 in a concentration-dependent and reversible manner. On the other hand, calyculin A (3 × 10−6 M) blocked both effects of ML-7 on stimulation and reversal of renin secretion independently of intracellular Ca++ concentrations. Such antagonistic effects of ML-7 and calyculin A on renin secretion most likely resulted from their respective effects on the level of MLC phosphorylation: ML-7 stimulates renin secretion by decreasing phosphorylation of MLC through its inhibition of MLCK, whereas calyculin A inhibits secretion by increasing phosphorylation of MLC through its inhibition of PPase-1. By inference from these results, MLC may be the target protein involved in regulation of the renin secretory process by Ca++: Ca++-calmodulin phosphorylates MLC via activating MLCK and thereby inhibits renin secretion, whereas dephosphorylation of phosphorylated MLC by PPase-1 reverses the inhibited secretion. We therefore conclude that reversible phosphorylation of MLC may be an important biochemical step determining the rate of renin secretion from the juxtaglomerular cell.

Footnotes

  • Send reprint requests to: Chun Sik Park, M.D., Ph.D., Department of Physiology, University of Ulsan College of Medicine, 388–1 Poongnap Dong, Songpa Ku, Seoul 138–736, Korea.

  • ↵1 This work was supported by grants from the Korea Science and Engineering Foundation (961–0701-002–2), the Academic Research Fund to the Ministry of Education, Republic of Korea (BM96–197), and the Asan Social Welfare Foundation, Seoul, Korea

  • ↵2 Present address: Department of Physiology, Jeonbuk National University Medical School, Jeonju, Korea.

  • ↵3 Present address: Department of Thoracic Surgery, Cardiovascular Center, Yeonsei University College of Medicine, Seoul, Korea.

  • Abbreviations:
    JG cell
    juxtaglomerular cell
    ML-7
    1-(5-iodonaphthalene-1-sulfonyl)-1H-hexahydro-1,4-diazepine
    ML-9
    1-(5-chloronaphthalene-1-sulfonyl)-1H-hexahydro-1,4-diazepine
    MLC20
    20-kdalton myosin light chain
    MLCK
    myosin light chain kinase
    PPase-1
    protein phosphatase type 1
    PPase-2A
    protein phosphatase type 2A
    KRB
    Krebs-Ringer bicarbonate
    ANG I
    angiotensin I
    • Received September 2, 1997.
    • Accepted February 23, 1998.
  • The American Society for Pharmacology and Experimental Therapeutics
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Journal of Pharmacology and Experimental Therapeutics
Vol. 285, Issue 3
1 Jun 1998
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OtherRENAL PHARMACOLOGY

Regulation of Renin Secretion Through Reversible Phosphorylation of Myosin by Myosin Light Chain Kinase and Protein Phosphatase Type 1

Mi Hyun Kim, Sun-Hee Kim, Hyun Sook Kim, Jai Won Chang, Yoo Sun Hong, Hae Won Kim and Chun Sik Park
Journal of Pharmacology and Experimental Therapeutics June 1, 1998, 285 (3) 968-974;

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OtherRENAL PHARMACOLOGY

Regulation of Renin Secretion Through Reversible Phosphorylation of Myosin by Myosin Light Chain Kinase and Protein Phosphatase Type 1

Mi Hyun Kim, Sun-Hee Kim, Hyun Sook Kim, Jai Won Chang, Yoo Sun Hong, Hae Won Kim and Chun Sik Park
Journal of Pharmacology and Experimental Therapeutics June 1, 1998, 285 (3) 968-974;
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