Lymperopoulos A, Wertz SL, Pollard CM, Desimine VL, Maning J, McCrink KA. Not all arrestins are created equal: Therapeutic implications of the functional diversity of the β-arrestins in the heart. World J Cardiol 2019; 11(2): 47-56 [PMID: 30820275 DOI: 10.4330/wjc.v11.i2.47]
Corresponding Author of This Article
Anastasios Lymperopoulos, BPharm, MSc, PhD, FAHA, FESC, Associate Professor, Laboratory for the Study of Neurohormonal Control of the Circulation, Department of Pharmaceutical Sciences (Pharmacology), College of Pharmacy, Nova Southeastern University, 3200 S. University Dr., HPD (Terry) Bldg/Room 1338, Fort Lauderdale, FL33328, United States. al806@nova.edu
Research Domain of This Article
Cardiac & Cardiovascular Systems
Article-Type of This Article
Editorial
Open-Access Policy of This Article
This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
World J Cardiol. Feb 26, 2019; 11(2): 47-56 Published online Feb 26, 2019. doi: 10.4330/wjc.v11.i2.47
Not all arrestins are created equal: Therapeutic implications of the functional diversity of the β-arrestins in the heart
Anastasios Lymperopoulos, Shelby L Wertz, Celina M Pollard, Victoria L Desimine, Jennifer Maning, Katie A McCrink
Anastasios Lymperopoulos, Shelby L Wertz, Celina M Pollard, Victoria L Desimine, Jennifer Maning, Katie A McCrink, Laboratory for the Study of Neurohormonal Control of the Circulation, Department of Pharmaceutical Sciences (Pharmacology), College of Pharmacy, Nova Southeastern University, Fort Lauderdale, FL 33328, United States
Jennifer Maning, Jackson Memorial Hospital, Miami, FL 33136, United States
Katie A McCrink, Massachusetts General Hospital, Boston, MA 02114, United States
Author contributions: All authors performed literature research and contributed to the writing of the manuscript; Lymperopoulos A supervised the project and wrote the paper.
Supported bya NSU’s President’s Faculty Research and Development Grant (PFRDG).
Conflict-of-interest statement: The authors declare no conflict of interest related to this publication.
Open-Access: This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
Corresponding author: Anastasios Lymperopoulos, BPharm, MSc, PhD, FAHA, FESC, Associate Professor, Laboratory for the Study of Neurohormonal Control of the Circulation, Department of Pharmaceutical Sciences (Pharmacology), College of Pharmacy, Nova Southeastern University, 3200 S. University Dr., HPD (Terry) Bldg/Room 1338, Fort Lauderdale, FL33328, United States. al806@nova.edu
Telephone: +1-954-262-1338 Fax: +1-954-262-2278
Received: October 16, 2018 Peer-review started: October 16, 2018 First decision: November 15, 2018 Revised: November 28, 2018 Accepted: January 10, 2019 Article in press: January 10, 2019 Published online: February 26, 2019 Processing time: 132 Days and 7.8 Hours
Core Tip
Core tip: Presumed functionally similar for a long time, we now know that the two β-arrestins display significant functional diversity in several organs and tissues, including in the cardiovascular system. Their functional distinction also in the mammalian heart has been clearly documented over the past few years. β-arrestin-1, which is far more abundant than β-arrestin-2 in almost every tissue including the myocardium, opposes the cyclic adenosine monophosphate (cAMP)-dependent pro-contractile signaling of the β1 adrenergic receptor (β1AR), and promotes cardiac apoptosis, inflammation, and other adverse remodeling-associated processes post-myocardial infarction. Conversely, β-arrestin-2 promotes catecholamine-dependent cardiac contractility directly, via SERCA2a potentiation, and indirectly, by leaving β1AR’s cAMP-dependent pro-contractile signaling unaffected.
