Influence of Isoproterenol on Contractile Protein Function, Excitation-Contraction Coupling, and Energy Turnover of Isolated Nonfailing Human Myocardium

1994 ◽  
Vol 26 (11) ◽  
pp. 1461-1469 ◽  
Author(s):  
Gerd Hasenfuss ◽  
Louis A. Mulieri ◽  
Bruce J. Leavitt ◽  
Norman R. Alpert
Author(s):  
G. Hasenfuss ◽  
L. A. Mulieri ◽  
B. J. Leavitt ◽  
P. D. Allen ◽  
C. Holubarsch ◽  
...  

Author(s):  
Walter C. Thompson ◽  
Paul H. Goldspink

Abstract 14–3-3 proteins (14–3-3 s) are a family of highly conserved proteins that regulate many cellular processes in eukaryotes by interacting with a diverse array of client proteins. The 14–3-3 proteins have been implicated in several disease states and previous reviews have condensed the literature with respect to their structure, function, and the regulation of different cellular processes. This review focuses on the growing body of literature exploring the important role 14–3-3 proteins appear to play in regulating the biochemical and biophysical events associated with excitation–contraction coupling (ECC) in muscle. It presents both a timely and unique analysis that seeks to unite studies emphasizing the identification and diversity of 14–3-3 protein function and client protein interactions, as modulators of muscle contraction. It also highlights ideas within these two well-established but intersecting fields that support further investigation with respect to the mechanistic actions of 14–3-3 proteins in the modulation of force generation in muscle.


Circulation ◽  
1996 ◽  
Vol 94 (12) ◽  
pp. 3155-3160 ◽  
Author(s):  
Gerd Hasenfuss ◽  
Louis A. Mulieri ◽  
Paul D. Allen ◽  
H. Just ◽  
N.R. Alpert

2021 ◽  
Vol 7 (1) ◽  
Author(s):  
Yankun Lyu ◽  
Vipin K. Verma ◽  
Younjee Lee ◽  
Iosif Taleb ◽  
Rachit Badolia ◽  
...  

AbstractIt is well established that the aging heart progressively remodels towards a senescent phenotype, but alterations of cellular microstructure and their differences to chronic heart failure (HF) associated remodeling remain ill-defined. Here, we show that the transverse tubular system (t-system) and proteins underlying excitation-contraction coupling in cardiomyocytes are characteristically remodeled with age. We shed light on mechanisms of this remodeling and identified similarities and differences to chronic HF. Using left ventricular myocardium from donors and HF patients with ages between 19 and 75 years, we established a library of 3D reconstructions of the t-system as well as ryanodine receptor (RyR) and junctophilin 2 (JPH2) clusters. Aging was characterized by t-system alterations and sarcolemmal dissociation of RyR clusters. This remodeling was less pronounced than in HF and accompanied by major alterations of JPH2 arrangement. Our study indicates that targeting sarcolemmal association of JPH2 might ameliorate age-associated deficiencies of heart function.


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