ABSTRACT
AIMS: The mechanisms by which the left ventricular wall escapes anoxia during the systolic phase of low blood perfusion are investigated, especially the role of myoglobin (Mb), which can (i) store oxygen and (ii) facilitate intracellular oxygen transport. The quantitative role of these two Mb functions is studied in the maximally working human heart. METHODS AND RESULTS: Because discrimination between Mb functions has not been achieved experimentally, we use a Krogh cylinder model here. At a heart rate of 200 beats/min and a 1:1 ratio of diastole/systole, the systole lasts for 150 ms. The basic model assumption is that, with mobile Mb, the oxygen stored in the end-diastolic left ventricle wall exactly meets the demand during the 150 ms of systolic cessation of blood flow. The coronary blood flow necessary to achieve this agrees with literature data. By considering Mb immobile or setting its concentration to zero, respectively, we find that, depending on Mb concentration, Mb-facilitated O(2) transport maintains O(2) supply to the left ventricle wall during 22-34 of the 150 ms, while Mb storage function accounts for a further 12-17 ms. When Mb is completely absent, anoxia begins to develop after 116-99 ms. CONCLUSION: While Mb plays no significant role during diastole, it supplies O(2) to the left ventricular wall for < or = 50 ms of the 150 ms systole, whereas capillary haemoglobin is responsible for approximately 80 ms. Slight increases in haemoglobin concentration, blood flow, or capillary density can compensate the absence of Mb, a finding which agrees well with the observations using Mb knockout mice.
Subject(s)
Coronary Circulation , Heart Ventricles/metabolism , Microcirculation , Models, Cardiovascular , Myocardium/metabolism , Myoglobin/blood , Oxygen Consumption , Oxygen/blood , Adaptation, Physiological , Animals , Diffusion , Heart Rate , Hemoglobins/metabolism , Humans , Mice , Mice, Knockout , Myocardial Contraction , Myoglobin/deficiency , Myoglobin/genetics , Reproducibility of Results , Sarcoplasmic Reticulum/metabolism , Time Factors , Ventricular Function, LeftABSTRACT
Pulmonary surfactant, a complex mixture of lipids and proteins, lowers the surface tension in terminal air spaces and is crucial for lung function. Within an animal species, surfactant composition can be influenced by development, disease, respiratory rate, and/or body temperature. Here, we analyzed the composition of surfactant in three heterothermic mammals (dunnart, bat, squirrel), displaying different torpor patterns, to determine: 1) whether increases in surfactant cholesterol (Chol) and phospholipid (PL) saturation occur during long-term torpor in squirrels, as in bats and dunnarts; 2) whether surfactant proteins change during torpor; and 3) whether PL molecular species (molsp) composition is altered. In addition, we analyzed the molsp composition of a further nine mammals (including placental/marsupial and hetero-/homeothermic contrasts) to determine whether phylogeny or thermal behavior determines molsp composition in mammals. We discovered that like bats and dunnarts, surfactant Chol increases during torpor in squirrels. However, changes in PL saturation during torpor may not be universal. Torpor was accompanied by a decrease in surfactant protein A in dunnarts and squirrels, but not in bats, whereas surfactant protein B did not change in any species. Phosphatidylcholine (PC)16:0/16:0 is highly variable between mammals and is not the major PL in the wombat, dunnart, shrew, or Tasmanian devil. An inverse relationship exists between PC16:0/16:0 and two of the major fluidizing components, PC16:0/16:1 and PC16:0/14:0. The PL molsp profile of an animal species is not determined by phylogeny or thermal behavior. We conclude that there is no single PL molsp composition that functions optimally in all mammals; rather, surfactant from each animal is unique and tailored to the biology of that animal.
Subject(s)
1,2-Dipalmitoylphosphatidylcholine/physiology , Chiroptera/physiology , Marsupialia/physiology , Pulmonary Surfactants/chemistry , Pulmonary Surfactants/metabolism , Sciuridae/physiology , Animals , Body Temperature , Cholesterol/analysis , Cholesterol/physiology , Cold Temperature , Humans , Macropodidae , Male , Phascolarctidae , Phospholipids/analysis , Phospholipids/physiology , Phylogeny , Rabbits , Rats , Rats, Sprague-Dawley , Shrews , Species Specificity , SwineABSTRACT
The skeletal muscles of the smallest mammal, the Etruscan shrew Suncus etruscus, are functionally and structurally adapted to the requirements of an enormously high energy turnover. Isometric twitch contractions of the extensor digitorum longus (EDL) and soleus muscles are shorter than in any other mammal, allowing these muscles to contract at outstandingly high frequencies. The skeletal muscles of S. etruscus contract at up to 900 min(-1) for respiration, up to 780 min(-1) for running and up to 3500 min(-1) for shivering. All skeletal muscles investigated lack slow-twitch type I fibres and consist only of fast-twitch type IID fibres. These fibres are optimally equipped with properties enabling a high rate of almost purely oxidative metabolism: they have a small diameter, their citrate synthase activity is higher and their lactate dehydrogenase activity is lower than in the muscles of any other mammal and they have a rapid shortening velocity. Differences in isometric twitch contraction times between different muscles are, at least in part, probably due to differences in cytosolic creatine kinase activities.
Subject(s)
Body Constitution/physiology , Muscle, Skeletal/physiology , Shrews/physiology , Animals , Energy Metabolism , Isometric ContractionABSTRACT
Besides acting as an oxygen store during times of reduced blood oxygen supply, myoglobin can also facilitate intracellular oxygen transport by diffusion of oxymyoglobin along a PO(2) gradient. We reassess the importance of myoglobin-facilitated oxygen diffusion by applying new findings on the intracellular diffusivity of myoglobin in a model calculation.