ArticleArchives of biochemistry and biophysics2016
Insights into length-dependent regulation of cardiac cross-bridge cycling kinetics in human myocardium.
Article in Archives of biochemistry and biophysics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 11 citations in OpenAlex.
- Maternal Body Mass Index, Myometrium Contractility and Uterotonic Receptor Expression in Pregnancy.Reproductive sciences (Thousand Oaks, Calif.) · 2024Article
- The Case for, and Challenges of, Human Cardiac Tissue in Advancing Phosphoprotein Research.Frontiers in physiology · 2022Review
- Effect of hypothyroidism on contractile performance of isolated end-stage failing human myocardium.PloS one · 2022Article
- Contraction-relaxation coupling is unaltered by exercise training and infarction in isolated canine myocardium.The Journal of general physiology · 2021Article
- Assessment of PKA and PKC inhibitors on force and kinetics of non-failing and failing human myocardium.Life sciences · 2018Article
- Protein Kinase A as a Promising Target for Heart Failure Drug Development.Archives of medical research · 2018Review
- Human Myocardium Has a Robust α1A-Subtype Adrenergic Receptor Inotropic Response.Journal of cardiovascular pharmacology · 2018Article
- Etiology-dependent impairment of relaxation kinetics in right ventricular end-stage failing human myocardium.Journal of molecular and cellular cardiology · 2018Article
- Increased cross-bridge recruitment contributes to transient increase in force generation beyond maximal capacity in human myocardium.Journal of molecular and cellular cardiology · 2018Article
- Myofilament modulation of contraction.Archives of biochemistry and biophysics · 2016Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Cross-bridge cycling kinetics play an essential role in the heart's ability to contract and relax. The rate of tension redevelopment (ktr) slows down as a muscle length is increased in intact human myocardium. We set out to determine the effect of rapid length step changes and protein kinase A (PKA) and protein kinase C-βII (PKC-βII) inhibitors on the ktr in ultra-thin non-failing and failing human right ventricular trabeculae. After stabilizing the muscle either at L90 (90% of optimal length) or at Lopt (optimal length), we rapidly changed the length to either Lopt or L90 and measured ktr. We report that length-dependent changes in ktr occur very rapidly (in the order of seconds or faster) in both non-failing and failing muscles and that the length at which a muscle had been stabilized prior to the length change does not significantly affect ktr. In addition, at L90 and at Lopt, PKA and PKC-βII inhibitors did not significantly change ktr. Our results reveal that length-dependent regulation of cross-bridge cycling kinetics predominantly occurs rapidly and involves the intrinsic properties of the myofilament rather than post-translational modifications that are known to occur in the cardiac muscle as a result of a change in muscle/sarcomere length.
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Registered trials
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.