Evidence map›Paper›PMID 25410495›Full record

ArticlePflugers Archiv : European journal of physiology2015

Echinochrome A regulates phosphorylation of phospholamban Ser16 and Thr17 suppressing cardiac SERCA2A Ca²⁺ reuptake.

Hyoung Kyu Kim, Jae Boum Youm, Seung Hun Jeong, Sung Ryul Lee, In-Sung Song, Tae Hee Ko, Julius Ryan Pronto, Kyung Soo Ko, Byoung Doo Rhee, Nari Kim and 5 more

Abstract read
PubMed Publisher
In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  12. Quantitative cardiac phosphoproteomics profiling during ischemia-reperfusion in an immature swine model.American journal of physiology. Heart and circulatory physiology · 2017
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

15 authors.

Hyoung Kyu KimCardiovascular and Metabolic Disease Center (CMDC), National Research Laboratory for Mitochondrial Signaling, Department of Physiology, College of Medicine, Inje University, Busan, South Korea.
Jae Boum YoumCardiovascular and Metabolic Disease Center (CMDC), National Research Laboratory for Mitochondrial Signaling, Department of Physiology, College of Medicine, Inje University, Busan, South Korea.
Seung Hun JeongCardiovascular and Metabolic Disease Center (CMDC), National Research Laboratory for Mitochondrial Signaling, Department of Physiology, College of Medicine, Inje University, Busan, South Korea.
Sung Ryul LeeCardiovascular and Metabolic Disease Center (CMDC), National Research Laboratory for Mitochondrial Signaling, Department of Physiology, College of Medicine, Inje University, Busan, South Korea.
In-Sung SongCardiovascular and Metabolic Disease Center (CMDC), National Research Laboratory for Mitochondrial Signaling, Department of Physiology, College of Medicine, Inje University, Busan, South Korea.
Tae Hee KoCardiovascular and Metabolic Disease Center (CMDC), National Research Laboratory for Mitochondrial Signaling, Department of Physiology, College of Medicine, Inje University, Busan, South Korea.
Julius Ryan ProntoCardiovascular and Metabolic Disease Center (CMDC), National Research Laboratory for Mitochondrial Signaling, Department of Physiology, College of Medicine, Inje University, Busan, South Korea.
Kyung Soo KoCardiovascular and Metabolic Disease Center (CMDC), National Research Laboratory for Mitochondrial Signaling, Department of Physiology, College of Medicine, Inje University, Busan, South Korea.
Byoung Doo RheeCardiovascular and Metabolic Disease Center (CMDC), National Research Laboratory for Mitochondrial Signaling, Department of Physiology, College of Medicine, Inje University, Busan, South Korea.
Nari KimCardiovascular and Metabolic Disease Center (CMDC), National Research Laboratory for Mitochondrial Signaling, Department of Physiology, College of Medicine, Inje University, Busan, South Korea.
Bernd NiliusDepartment Cell Molecular Medicine, Laboratory Ion Channel Research, Campus Gasthuisberg, KU Leuven, Leuven, Belgium.
Natalia P MischchenkoG.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Science, Prospect 100 let Vladivostoku, 159, Vladivostok, 690022, Russia.
Sergey A FedoreyevG.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Science, Prospect 100 let Vladivostoku, 159, Vladivostok, 690022, Russia.
Valentin A StonikG.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Science, Prospect 100 let Vladivostoku, 159, Vladivostok, 690022, Russia.
Jin HanCardiovascular and Metabolic Disease Center (CMDC), National Research Laboratory for Mitochondrial Signaling, Department of Physiology, College of Medicine, Inje University, Busan, South Korea. phyhanj@gmail.com.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Echinochrome A (Ech A), a marine bio-product isolated from sea urchin eggs, is known to have cardioprotective effects through its strong antioxidant and ATP-sparing capabilities. However, the effects of Ech A on cardiac excitation-contraction (E-C) are not known. In this study, we investigated the effects of Ech A on cardiac contractility and Ca(2+) handling in the rat heart. In ex vivo Langendorff hearts, Ech A (3 μM) decreased left ventricular developing pressure to 77.7 ± 6.5 % of basal level. In isolated ventricular myocytes, Ech A reduced the fractional cell shortening from 3.4 % at baseline to 2.1 %. Ech A increased both diastolic and peak systolic intracellular Ca(2+) ([Ca(2+)]i). However, the ratio of peak [Ca]i to resting [Ca]i was significantly decreased. Ech A did not affect the L-type Ca(2+) current. Inhibiting the Na(+)/Ca(2+) exchanger with either NiCl2 or SEA400 did not affect the Ech A-dependent changes in Ca(2+) handling. Our data demonstrate that treatment with Ech A results in a significant reduction in the phosphorylation of phospholamban at both serine 16 and threonine 17 leading to a significant inhibition of SR Ca(2+)-ATPase 2A (SERCA2A) and subsequent reduced Ca(2+) uptake into the intracellular Ca(2+) store. Taken together, our data show that Ech A negatively regulates cardiac contractility by inhibiting SERCA2A activity, which leads to a reduction in internal Ca(2+) stores.

Indexed as

Calcium SignalingAnimalsCalcium-Binding ProteinsCardiotonic AgentsCells, CulturedHeart VentriclesMaleMyocardial ContractionMyocytes, CardiacNaphthoquinonesPhospholambanPhosphorylationRatsRats, WistarSarcoplasmic Reticulum Calcium-Transporting ATPasesSerineCalcium-Binding ProteinsCardiotonic Agentsechinochrome ANaphthoquinonesPhospholambanSarcoplasmic Reticulum Calcium-Transporting ATPasesSerineThreonineEchinochrome ANegative inotropic effectPhospholamban phosphorylationSERCA2A inhibition

Identifiers

PMID25410495

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.