Decreased protein and phosphorylation level of the protein phosphatase inhibitor-1 in failing human hearts.
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Decreased protein and phosphorylation level of the protein phosphatase inhibitor-1 in failing human hearts. / El-Armouche, Ali; Pamminger, Torsten; Ditz, Diana; Zolk, Oliver; Eschenhagen, Thomas.
in: CARDIOVASC RES, Jahrgang 61, Nr. 1, 1, 2004, S. 87-93.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Decreased protein and phosphorylation level of the protein phosphatase inhibitor-1 in failing human hearts.
AU - El-Armouche, Ali
AU - Pamminger, Torsten
AU - Ditz, Diana
AU - Zolk, Oliver
AU - Eschenhagen, Thomas
PY - 2004
Y1 - 2004
N2 - OBJECTIVE: The protein phosphatase inhibitor-1 (I-1) is a highly specific and potent inhibitor of type 1 phosphatases (PP1) that is active only in its protein kinase A (PKA)-phosphorylated form. I-1 ablation decreases, I-1 overexpression sensitizes beta-adrenergic signaling in the heart. It is controversial whether I-1 expression is altered in human heart failure (HF), likely because its detection in heart is difficult due to its low abundance. METHODS AND RESULTS: I-1 was >500-fold enriched from left ventricular myocardium (LVM) from patients with terminal HF (n=16) and non-failing controls (NF, n=5) and quantified with an affinity-purified I-1 and a I-1 phosphospecific antiserum. In non-failing I-1 protein levels amounted to 126 fmol/mg protein. In failing hearts, I-1 protein levels were reduced by 58% and I-1 phosphorylation by 77% (P
AB - OBJECTIVE: The protein phosphatase inhibitor-1 (I-1) is a highly specific and potent inhibitor of type 1 phosphatases (PP1) that is active only in its protein kinase A (PKA)-phosphorylated form. I-1 ablation decreases, I-1 overexpression sensitizes beta-adrenergic signaling in the heart. It is controversial whether I-1 expression is altered in human heart failure (HF), likely because its detection in heart is difficult due to its low abundance. METHODS AND RESULTS: I-1 was >500-fold enriched from left ventricular myocardium (LVM) from patients with terminal HF (n=16) and non-failing controls (NF, n=5) and quantified with an affinity-purified I-1 and a I-1 phosphospecific antiserum. In non-failing I-1 protein levels amounted to 126 fmol/mg protein. In failing hearts, I-1 protein levels were reduced by 58% and I-1 phosphorylation by 77% (P
M3 - SCORING: Zeitschriftenaufsatz
VL - 61
SP - 87
EP - 93
JO - CARDIOVASC RES
JF - CARDIOVASC RES
SN - 0008-6363
IS - 1
M1 - 1
ER -
