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(Circulation Research. 2005;97:964.)
© 2005 American Heart Association, Inc.

Editorials

Cardiac Remodeling

UPS Lost in Transit

Peter Razeghi, Heinrich Taegtmeyer

From the Division of Cardiology, University of Texas–Houston Medical School.

Correspondence to Heinrich Taegtmeyer, MD, DPhil, Department of Internal Medicine, Division of Cardiology, University of Texas–Houston Medical School, 6431 Fannin, MSB 1.222, Houston, TX 77030. E-mail Heinrich.Taegtmeyer@uth.tmc.edu

See related article on pages 1018–1026

Key Words: hypertrophy • atrophy • ubiquitin • proteasome • myocardial remodeling

An extract of the first 250 words of the full text is provided, because this article has no abstract.

When challenged to write an editorial, it is difficult to resist a play of words. To state it up front: UPS is the ubiquitin–proteasome system and not the trusted parcel carrier. UPS also epitomizes our current understanding of the complex system by which the cardiomyocyte (like virtually every cell in the body) breaks down useless proteins to make room for new (and useful) proteins that make up the cell. The concept of protein turnover is not new. More then 60 years ago, Rudolf Schönheimer, a pioneer in the use of stable isotopes to assess biological processes, formulated the revolutionary idea of The Dynamic State of Body Constituents.¹ Today, we recognize that in the heart, like in every other organ of the body, protein turnover is a result of the ordered, regulated, and balanced equilibrium of protein synthesis and degradation (Figure 1). We also recognize the fact, that with both hypertrophic and atrophic remodeling, the fetal gene program is reactivated² and rates of protein turnover are increased,^3,4 although relative rates differ (Figure). Although pathways regulating protein synthesis are already quite well characterized in the heart,^3,5 our knowledge about pathways that regulate myocardial proteolysis is still limited.⁶ Protein breakdown is essential for the removal of dysfunctional proteins and for the adaptation to new physiologic states when it is of advantage for the organism to survive by breaking down its own constituents (eg, starvation induces skeletal muscle atrophy). Although each protein has its own characteristic half-life, even under . . . [Full Text of this Article]

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