Basic axes of human heart in correlation with heart mass and right ventricular wall thickness

A comparison of the data published in anatomy textbooks and anthropological tables does not reveal any change in basic heart dimensions during the period since the beginning of the 20th century to nowadays. However, normal values of many other parameters have changed up to 30% over the same period. These changes may be caused by the acceleration phenomenon or the extension of average lifespan. The progress of laboratory medicine methodology permitted the introduction of new biochemical tests in myocardial infarct diagnosis, such as myoglobin and troponins T and I measurement, as well as better understanding of cardiac metabolism. Parameters describing the direction and intensity of metabolic changes are substrate extraction and metabolic equilibrium. The expression describing metabolic equilibrium contains heart mass value. Therefore, as studying heart mass in vivo is not possible, it may be important to study it in vitro. The study was performed on a group of 107 formalin-fixed human hearts. The organs came from adults of both sexes: 30 women and 77 men, aged 18 to 90 years. None of the hearts carried signs of macroscopic developmental abnormalities or pathologic changes

Contractility-dependent actin dynamics in cardiomyocyte sarcomeres

In contrast to the highly dynamic actin cytoskeleton in nonmuscle cells, actin filaments in muscle sarcomeres are thought to be relatively stable and undergo dynamics only at their ends. However, many proteins that promote rapid actin dynamics are also expressed in striated muscles. We show that a subset of actin filaments in cardiomyocyte sarcomeres displays rapid turnover. Importantly, we found that turnover of these filaments depends on contractility of the cardiomyocytes. Studies using an actin-polymerization inhibitor suggest that the pool of dynamic actin filaments is composed of filaments that do not contribute to contractility. Furthermore, we provide evidence that ADF/cofilins, together with myosin-induced contractility, are required to disassemble non-productive filaments in developing cardiomyocytes. These data indicate that an excess of actin filaments is produced during sarcomere assembly, and that contractility is applied to recognize non-productive filaments that are subsequently destined for depolymerization. Consequently, contractility-induced actin dynamics plays an important role in sarcomere maturation

Notes on the morphology of the tricuspid valve in the adult human heart

Rapid progress in the field of interventional cardiology has caused research in the field of morphometry of the heart to be in constant demand [7–10, 12]. In this study, performed on a group of 75 adult human hearts, the authors have attempted to assess the form and number of the main and accessory cusps in the tricuspid valve. We have classified particular forms into 8 groups, depending on the number of cusps and we have divided the cusps into 3 main groups, depending on the support of the chordae tendineae

Investigation of Allotropic ß→α-Sn Transition in High Tin Content Solder Alloys with Different Microscopy and Spectroscopy Techniques

In the microelectronics, β-Sn (white tin) is the base material of the solder alloys and surface finishes. The so-called “tin pest” phenomenon is the spontaneous allotropic transition of ß-Sn to the semiconductor α-Sn (gray tin) below 13.2°C. In this work, different microscopy and spectroscopy techniques were applied to characterize the tin pest phenomenon in the case of different solder alloys and inoculator materials as well as to study the applicability of these techniques in tin pest research. The optical imaging technique was used to compare the surface marks of the allotropic transition in the case of different inoculator materials. The development of the transition towards the sample bodies was studied on metallurgical cross-sections. Electrical resistance measurements were applied to determine the different phases of the transition in the case of different alloys and inoculators. The grain sliding and α -Sn expansion during the transition was observed by scanning electron microscopy and focused ion beam - scanning ionic microscopy. The ratio of the transitioned tin and the duration of the transition process was determined by Mössbauer spectroscopy. Our results have shown that the transition phases can considerably differ at the different alloys and inoculators, like different nucleation, growth, and the saturation phase. The accurate characterization of the transition in the given material combinations is possible only with the combined application of the applied analytical methods

Different Localizations and Cellular Behaviors of Leiomodin and Tropomodulin in Mature Cardiomyocyte Sarcomeres

Lmod is a muscle-specific actin nucleator that displays structural similarity to the filament pointed-end–capping protein, Tmod. The mechanisms of localizations of Lmod and Tmod in muscle sarcomeres are strikingly different. Lmod contributes to the organization of mature myofibrils through a mechanism that requires interaction with tropomyosin

Sarcomeric Pattern Formation by Actin Cluster Coalescence

Contractile function of striated muscle cells depends crucially on the almost crystalline order of actin and myosin filaments in myofibrils, but the physical mechanisms that lead to myofibril assembly remains ill-defined. Passive diffusive sorting of actin filaments into sarcomeric order is kinetically impossible, suggesting a pivotal role of active processes in sarcomeric pattern formation. Using a one-dimensional computational model of an initially unstriated actin bundle, we show that actin filament treadmilling in the presence of processive plus-end crosslinking provides a simple and robust mechanism for the polarity sorting of actin filaments as well as for the correct localization of myosin filaments. We propose that the coalescence of crosslinked actin clusters could be key for sarcomeric pattern formation. In our simulations, sarcomere spacing is set by filament length prompting tight length control already at early stages of pattern formation. The proposed mechanism could be generic and apply both to premyofibrils and nascent myofibrils in developing muscle cells as well as possibly to striated stress-fibers in non-muscle cells

DAAM is required for thin filament formation and Sarcomerogenesis during muscle development in Drosophila.

During muscle development, myosin and actin containing filaments assemble into the highly organized sarcomeric structure critical for muscle function. Although sarcomerogenesis clearly involves the de novo formation of actin filaments, this process remained poorly understood. Here we show that mouse and Drosophila members of the DAAM formin family are sarcomere-associated actin assembly factors enriched at the Z-disc and M-band. Analysis of dDAAM mutants revealed a pivotal role in myofibrillogenesis of larval somatic muscles, indirect flight muscles and the heart. We found that loss of dDAAM function results in multiple defects in sarcomere development including thin and thick filament disorganization, Z-disc and M-band formation, and a near complete absence of the myofibrillar lattice. Collectively, our data suggest that dDAAM is required for the initial assembly of thin filaments, and subsequently it promotes filament elongation by assembling short actin polymers that anneal to the pointed end of the growing filaments, and by antagonizing the capping protein Tropomodulin