Evidence map›Paper›PMID 32122157›Full record

ArticleCirculation2020

Integrin β1D Deficiency-Mediated RyR2 Dysfunction Contributes to Catecholamine-Sensitive Ventricular Tachycardia in Arrhythmogenic Right Ventricular Cardiomyopathy.

Yihui Wang, Chunyan Li, Ling Shi, Xiuyu Chen, Chen Cui, Jinhua Huang, Biyi Chen, Duane D Hall, Zhenwei Pan, Minjie Lu and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Circulation, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
8.1field-weighted citation impact, top 2% of its field
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

39 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
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  6. Decreased RYR2 Cluster Size and Abnormal SR CaAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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  15. Caveolae-associated cAMP/CaJournal of molecular and cellular cardiology · 2023
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 5 institutions in 3 countries.

Yihui WangState Key Laboratory of Cardiovascular Disease, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing (Y.W., C.L., X.C., C.C., M.L., S.Z.).
Chunyan LiState Key Laboratory of Cardiovascular Disease, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing (Y.W., C.L., X.C., C.C., M.L., S.Z.).
Ling ShiDepartment of Pharmacology, College of Pharmacy, and State-Province Key Laboratories of Biomedicine-Pharmaceutics of China, Key Laboratory of Cardiovascular Research, Ministry of Education, Harbin Medical University, Heilongjiang, China (L.S., Z.P.).
Xiuyu ChenState Key Laboratory of Cardiovascular Disease, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing (Y.W., C.L., X.C., C.C., M.L., S.Z.).
Chen CuiState Key Laboratory of Cardiovascular Disease, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing (Y.W., C.L., X.C., C.C., M.L., S.Z.).
Jinhua Huang
Biyi ChenDivision of Cardiovascular Medicine, Department of Internal Medicine, Abboud Cardiovascular Research Center, Carver College of Medicine, University of Iowa, Iowa City (B.C., D.D.H., L.-S.S.).
Duane D HallDivision of Cardiovascular Medicine, Department of Internal Medicine, Abboud Cardiovascular Research Center, Carver College of Medicine, University of Iowa, Iowa City (B.C., D.D.H., L.-S.S.).
Zhenwei PanDepartment of Pharmacology, College of Pharmacy, and State-Province Key Laboratories of Biomedicine-Pharmaceutics of China, Key Laboratory of Cardiovascular Research, Ministry of Education, Harbin Medical University, Heilongjiang, China (L.S., Z.P.).
Minjie LuState Key Laboratory of Cardiovascular Disease, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing (Y.W., C.L., X.C., C.C., M.L., S.Z.).
Jiang HongDepartment of Cardiology, Fujian Institute of Coronary Heart Disease, Fujian Medical University Union Hospital, China (J.H.).
Long-Sheng SongDivision of Cardiovascular Medicine, Department of Internal Medicine, Abboud Cardiovascular Research Center, Carver College of Medicine, University of Iowa, Iowa City (B.C., D.D.H., L.-S.S.).
Shihua ZhaoState Key Laboratory of Cardiovascular Disease, National Center for Cardiovascular Diseases, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing (Y.W., C.L., X.C., C.C., M.L., S.Z.).
Chinese Academy of Medical Sciences & Peking Union Medical College · CNUniversity of Iowa · USHarbin Medical University · CNFujian Medical University · CNJinhua Academy of Agricultural Sciences · CN

Funding

Novel Functions of the E-C Coupling Structural Protein Junctophilin-2 in the HeartR01HL130346 · NHLBI · UNIVERSITY OF IOWA · PI SONG, LONG-SHENG · 2016 to 2023
$4.4M
T-tubule remodeling and Ca2+-dependent arrhythmogenesis in cardiomyopathies.R01HL090905 · NHLBI · UNIVERSITY OF IOWA · PI SONG, LONG-SHENG · 2008 to 2017
$4.0M
Understanding the multifaceted functions of MG53 in heart failure pathogenesisI01BX002334 · VA · IOWA CITY VA MEDICAL CENTER · PI SONG, LONG-SHENG · 2016 to 2021
–
BLRD VA I01 BX002334NHLBI NIH HHS R01 HL090905NHLBI NIH HHS R01 HL130346
6 · The paper itself

Abstract

backgroundArrhythmogenic right ventricular cardiomyopathy (ARVC) is a hereditary heart disease characterized by fatty infiltration, life-threatening arrhythmias, and increased risk of sudden cardiac death. The guideline for management of ARVC in patients is to improve quality of life by reducing arrhythmic symptoms and to prevent sudden cardiac death. However, the mechanism underlying ARVC-associated cardiac arrhythmias remains poorly understood.

methodsUsing protein mass spectrometry analyses, we identified that integrin β1 is downregulated in ARVC hearts without changes to Ca

resultsIntegrin β1D deficiency and RyR2 Ser-2030 hyperphosphorylation were detected by Western blotting in left ventricular tissues from patients with ARVC but not in patients with ischemic or hypertrophic cardiomyopathy. Using lipid bilayer patch clamp single channel recordings, we found that purified integrin β1D protein could stabilize RyR2 function by decreasing RyR2 open probability, mean open time, and increasing mean close time. Also, β1D knockout mice exhibited normal cardiac function and morphology but presented with catecholamine-sensitive polymorphic ventricular tachycardia, consistent with increased RyR2 Ser-2030 phosphorylation and aberrant Ca

conclusionsOur data suggest that integrin β1D deficiency represents a novel mechanism underlying the increased risk of ventricular arrhythmias in patients with ARVC.

Indexed as

Calcium SignalingAdultAgedAnimalsArrhythmogenic Right Ventricular DysplasiaDesmoplakinsDisease Models, AnimalDown-RegulationExtracellular Signal-Regulated MAP KinasesFemaleFibronectinsHumansIntegrin beta1Ion Channel GatingMaleMice, Inbred C57BLDesmoplakinsDsp protein, mouseExtracellular Signal-Regulated MAP KinasesFibronectinsIntegrin beta1Itgb1 protein, humanItgb1 protein, mouseProtein Isoformsryanodine receptor 2. mouseRyanodine Receptor Calcium Release ChannelRyR2 protein, humanarrhythmogenic right ventricular cardiomyopathymechanicsphosphorylationRyR2ventricular tachycardiaβ integrins

Identifiers

PMID32122157
PMCPMC7200284
OpenAlexW3009875259

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.