약학회지 (YAKHAK HOEJI)

  • 제56권6호
  • /
  • Pages.377-381
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  • 2012
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  • 0377-9556(pISSN)
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  • 2383-9457(eISSN)
대한약학회 (The Pharmaceutical Society of Korea)
권호 표지

히스티딘-리치 $Ca^{2+}$ 결합 단백질에 의한 심실근세포 수축 및 $Ca^{2+}$ Transient의 조절

Regulation of Contraction and $Ca^{2+}$ Transient by Histidine-rich $Ca^{2+}$-binding Protein in Ventricular Myocytes

  • Son, Min-Jeong (College of Pharmacy, IDRD, Chungnam National University) ;
  • Kim, Joon-Chul (College of Pharmacy, IDRD, Chungnam National University) ;
  • Kim, Seong-Woo (College of Pharmacy, IDRD, Chungnam National University) ;
  • Ahn, Jong-Real (BK21 Physics Research Division, Sungkyunkwan University) ;
  • Woo, Sun-Hee (College of Pharmacy, IDRD, Chungnam National University)
  • 투고 : 2012.10.04
  • 심사 : 2012.11.23
  • 발행 : 2012.12.31
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초록

The histidine-rich $Ca^{2+}$ binding protein (HRC) is a $Ca^{2+}$ binding protein in the sarcoplasmic reticulum (SR). In this study, we examined whether the HRC is involved in the regulation of cardiac contraction and $Ca^{2+}$ signaling using HRC knock-out (KO) mouse ventricular myocytes. In field-stimulated single mouse ventricular myocytes, cell shortenings and $Ca^{2+}$ transients were measured using a video edge detection and a confocal $Ca^{2+}$ imaging, respectively. Compared with the wide-type (WT) myocytes, the magnitudes of cell shortenings were significantly larger in HRC KO cells (P<0.01, WT vs. KO). The rate of contraction and relaxation was significantly accelerated in HRC KO myocytes (P<0.05 and P<0.01, respectively, WT vs. KO). The magnitudes of $Ca^{2+}$ transients were increased by HRC KO (P<0.01, WT vs. KO). In addition, the decay of the $Ca^{2+}$ transient was faster in HRC KO cells than in wild-type cells P<0.01, WT vs. KO). These results suggest that HRC may suppress SR $Ca^{2+}$ releases and decay of $Ca^{2+}$ transients during action potentials, thereby attenuating ventricular contraction and relaxation.

키워드

과제정보

연구 과제 주관 기관 : 한국연구재단

참고문헌

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