• Title/Summary/Keyword: Physiology

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Identification of a Marker Protein for Cardiac Ischemia and Reperfusion Injury by Two-Dimensional Gel Electrophoresis and Matrix-Assisted Laser Desorption Ionization Mass Spectrometry

  • Lee, Young-Suk;Kim, Na-Ri;Kim, Hyun-Ju;Joo, Hyun;Kim, Young-Nam;Jeong, Dae-Hoon;Cuong, Dang Van;Kim, Eui-Yong;Hur, Dae-Young;Park, Young-Shik;Hong, Yong-Geun;Lee, Sang-Kyung;Chung, Joon-Yong;Seog, Dae-Hyun;Han, Jin
    • The Korean Journal of Physiology and Pharmacology
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    • v.8 no.4
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    • pp.207-211
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    • 2004

  • The purpose of the present study was to evaluate the expression of cardiac marker protein in rabbit cardiac tissue that was exposed to ischemic preconditioning (IPC), or ischemiareperfusion injury (IR) using two-dimensional gel electrophoresis (2DE) and matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS). We compared 2DE gels of control (uninjured) cardiac tissue with those of IPC and IR cardiac tissue. Expression of one protein was detected in IR heart tissue, however the protein was not detected in the samples of control and IPC tissue. To further characterize the detected protein molecule, the protein in the 2D gel was isolated and subjected to trypsin digestion, followed by MALDI-MS. The protein was identified as myoglobin, which was confirmed also by Western blot analysis. These results are consistent with previous studies of cardiac markers in ischemic hearts, indicating myoglobin as a suitable marker of myocardial injury. In addition, the present use of multiple techniques indicates that proteomic analysis is an appropriate means to identify cardiac markers in studies of IPC and IR.

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Interaction between Cholecystokinin and Secretin in Isolated Rat Pancreatic Acini

  • Yoon, Shin-Hee;Hahn, Sang-June;Sim, Sang-Soo;Rhie, Duck-Joo;Song, In-Young;Baek, Hye-Jung;Kim, Myung-Suk;Jo, Yang-Hyeok
    • The Korean Journal of Physiology
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    • v.29 no.2
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    • pp.243-250
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    • 1995

  • A possible potentiation between cholecystokinin (CCK) and secretin in amylase secretion from isolated rat pancreatic acini was investigated. Combined treatment of acini with secretin and CCK at low concentrations, which are known to be physiological, resulted in enzyme secretion larger than the arithmetic sum of their separate effects. Such a potentiating effect also occurred between secretin and A23187 (Ca ionophore), between forskolin (adenylate cyclase activator) and CCK, and between forskolin and A23187. Staurosporin (protein kinase C inhibitor) and W7 (calmodulin antagonist) inhibited markedly the potentiated amylase release induced by the agonists, but KT5720 (protein kinase A inhibitor) did not affect the potentiated amylase release. Therefore, we concluded that the action of CCK in a physiological concentration is potentiated by secretin in a physiological concentration range and vice versa, and that the intracellular mechanism necessary for the potentiation is associated with $Ca^{2+}$. However, it is uncertain what mechanisms are involved in potentiation of amylase release after CAMP and $Ca^{2+}$.

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