Transduction of the N-Terminal Fragments of MYPT1 Enhances Myofilament Ca 2+ Sensitivity in an Intact Coronary Artery

Katsuya Hirano, Dmitry N. Derkach, Mayumi Hirano, Junji Nishimura, Shosuke Takahashi, Hideo Kanaide

研究成果: ジャーナルへの寄稿記事

10 引用 (Scopus)

抄録

Objective - The region of the 110 kDa regulatory subunit (MYPT1) of smooth muscle myosin phosphatase involved in the regulation of contraction was determined under physiological conditions. Methods and Results - Using HIV Tat protein-mediated protein transduction, the N-terminal fragments of MYPT1 were introduced to the intact porcine coronary arterial strips. Pre-incubation with 3 μmol/L TAT-MYPT1 1-374 , a construct containing the Tat peptide and the residues 1 to 374 of MYPT1, for 15 minutes augmented (2.4-fold) the subsequent contraction induced by adding 1.25 mmol/L of extracellular Ca 2+ under 118 mmol/L K + depolarization, with no augmentation of the [Ca 2+ ] i elevation. The deletion of the Tat peptide, MYPT1 1-374 , abolished the augmenting effect. TAT-MYPT1 1-296 demonstrated a weaker but significant augmentation (1.7-fold). However, TAT-MYPT1 1-171 , TAT-MYPT1 39-374 , TAT-MYPT1 39-296 , and TAT-MYPT1 297-374 had no augmenting activity. The myosin light chain phosphorylation level as a function of extracellular Ca 2+ concentrations was shifted to the left in the strips pretreated with TAT-MYPT1 1-374 compared with the control. Conclusions - Region 1 to 296 was the minimal region involved in the enhancement of contraction, and region 297 to 374 played a supplemental role. These results suggested that the interaction mainly between catalytic subunit and MYPT1 play a critical role in the regulation of the endogenous myosin phosphatase in intact smooth muscle.

元の言語英語
ページ(範囲)464-469
ページ数6
ジャーナルArteriosclerosis, thrombosis, and vascular biology
24
発行部数3
DOI
出版物ステータス出版済み - 3 1 2004

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Myosin-Light-Chain Phosphatase
Myofibrils
Coronary Vessels
Human Immunodeficiency Virus tat Gene Products
Smooth Muscle Myosins
Myosin Light Chains
Peptides
Smooth Muscle
Catalytic Domain
Swine
Phosphorylation
Proteins

All Science Journal Classification (ASJC) codes

  • Cardiology and Cardiovascular Medicine

これを引用

Transduction of the N-Terminal Fragments of MYPT1 Enhances Myofilament Ca 2+ Sensitivity in an Intact Coronary Artery . / Hirano, Katsuya; Derkach, Dmitry N.; Hirano, Mayumi; Nishimura, Junji; Takahashi, Shosuke; Kanaide, Hideo.

:: Arteriosclerosis, thrombosis, and vascular biology, 巻 24, 番号 3, 01.03.2004, p. 464-469.

研究成果: ジャーナルへの寄稿記事

Hirano, Katsuya ; Derkach, Dmitry N. ; Hirano, Mayumi ; Nishimura, Junji ; Takahashi, Shosuke ; Kanaide, Hideo. / Transduction of the N-Terminal Fragments of MYPT1 Enhances Myofilament Ca 2+ Sensitivity in an Intact Coronary Artery :: Arteriosclerosis, thrombosis, and vascular biology. 2004 ; 巻 24, 番号 3. pp. 464-469.
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abstract = "Objective - The region of the 110 kDa regulatory subunit (MYPT1) of smooth muscle myosin phosphatase involved in the regulation of contraction was determined under physiological conditions. Methods and Results - Using HIV Tat protein-mediated protein transduction, the N-terminal fragments of MYPT1 were introduced to the intact porcine coronary arterial strips. Pre-incubation with 3 μmol/L TAT-MYPT1 1-374 , a construct containing the Tat peptide and the residues 1 to 374 of MYPT1, for 15 minutes augmented (2.4-fold) the subsequent contraction induced by adding 1.25 mmol/L of extracellular Ca 2+ under 118 mmol/L K + depolarization, with no augmentation of the [Ca 2+ ] i elevation. The deletion of the Tat peptide, MYPT1 1-374 , abolished the augmenting effect. TAT-MYPT1 1-296 demonstrated a weaker but significant augmentation (1.7-fold). However, TAT-MYPT1 1-171 , TAT-MYPT1 39-374 , TAT-MYPT1 39-296 , and TAT-MYPT1 297-374 had no augmenting activity. The myosin light chain phosphorylation level as a function of extracellular Ca 2+ concentrations was shifted to the left in the strips pretreated with TAT-MYPT1 1-374 compared with the control. Conclusions - Region 1 to 296 was the minimal region involved in the enhancement of contraction, and region 297 to 374 played a supplemental role. These results suggested that the interaction mainly between catalytic subunit and MYPT1 play a critical role in the regulation of the endogenous myosin phosphatase in intact smooth muscle.",
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AU - Hirano, Mayumi

AU - Nishimura, Junji

AU - Takahashi, Shosuke

AU - Kanaide, Hideo

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AB - Objective - The region of the 110 kDa regulatory subunit (MYPT1) of smooth muscle myosin phosphatase involved in the regulation of contraction was determined under physiological conditions. Methods and Results - Using HIV Tat protein-mediated protein transduction, the N-terminal fragments of MYPT1 were introduced to the intact porcine coronary arterial strips. Pre-incubation with 3 μmol/L TAT-MYPT1 1-374 , a construct containing the Tat peptide and the residues 1 to 374 of MYPT1, for 15 minutes augmented (2.4-fold) the subsequent contraction induced by adding 1.25 mmol/L of extracellular Ca 2+ under 118 mmol/L K + depolarization, with no augmentation of the [Ca 2+ ] i elevation. The deletion of the Tat peptide, MYPT1 1-374 , abolished the augmenting effect. TAT-MYPT1 1-296 demonstrated a weaker but significant augmentation (1.7-fold). However, TAT-MYPT1 1-171 , TAT-MYPT1 39-374 , TAT-MYPT1 39-296 , and TAT-MYPT1 297-374 had no augmenting activity. The myosin light chain phosphorylation level as a function of extracellular Ca 2+ concentrations was shifted to the left in the strips pretreated with TAT-MYPT1 1-374 compared with the control. Conclusions - Region 1 to 296 was the minimal region involved in the enhancement of contraction, and region 297 to 374 played a supplemental role. These results suggested that the interaction mainly between catalytic subunit and MYPT1 play a critical role in the regulation of the endogenous myosin phosphatase in intact smooth muscle.

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