About: Sarcoplasm is a research topic. Over the lifetime, 869 publications have been published within this topic receiving 35071 citations. The topic is also known as: GO:0016528.
TL;DR: Several types of striated muscle have been examined by the technics of electron microscopy and the findings in myotome fibers of Amblystoma larvae, the sartorius, and cardiac muscle of the rat are reported on in some detail.
Abstract: Several types of striated muscle have been examined by the technics of electron microscopy and the findings in myotome fibers of Amblystoma larvae, the sartorius, and cardiac muscle of the rat are reported on in some detail. Particular attention has been given to structural components of the interfibrillar sarcoplasm and most especially to a finely divided, vacuolar system known as the sarcoplasmic reticulum. This consists of membrane-limited vesicles, tubules, and cisternae associated in a continuous reticular structure which forms lace-like sleeves around the myofibrils. It shows a definable organization which repeats with each sarcomere of the fiber so that the entire system is segmented in phase with the striations of the associated myofibrils. Details of these repetitive patterns are presented diagrammatically in Text-figs. 1, 2, and 3 on pages 279, 283, and 288 respectively. The system is continuous across the fiber at the H band level and largely discontinuous longitudinally because of interruptions in the structure at the I and Z band levels. The structure of the system relates it to the endoplasmic reticulum of other cell types. The precise morphological relation of the reticulum to the myofibrils, with specializations opposite the different bands, prompts the supposition that the system is functionally important in muscle contraction. In this regard it is proposed that the membrane limiting the system is polarized like the sarcolemma and that the corresponding potential difference is utilized in the intracellular distribution of the excitatory impulse.
TL;DR: It is suggested that the Differences in the low-molecular-weight components of myosin from different types of muscle are a consequence of differences in the isoenzyme composition of the myosins.
Abstract: 1. The low-molecular-weight components of myosin freshly prepared by the standard procedure from adult rabbit skeletal muscle migrated as four main bands Ml1, Ml2, Ml3 and Ml4 on polyacrylamide-gel electrophoresis in 8m-urea. 2. The number of bands increased on storage. This change was accelerated by increasing the temperature and pH. 3. None of the bands had electrophoretic mobilities identical with those of the well-characterized proteins of the myofibril or with the sarcoplasmic proteins. 4. By varying the ionic conditions and concentration of muscle mince used for the initial extraction it was possible to change the relative proportions of the two electrophoretic bands of intermediate mobility, Ml2 and Ml3. 5. The four-band picture similar to that obtained with rabbit was observed with myosin isolated from skeletal muscle of the rat, mouse, hamster, pigeon and chicken. 6. Rabbit cardiac myosin gave only two bands on electrophoresis. Myosin from rabbit red muscle gave a pattern intermediate between cardiac and white-skeletal-muscle myosin, i.e. the two fastest bands were present in decreased relative amounts. 7. It is suggested that the differences in the low-molecular-weight components of myosin from different types of muscle are a consequence of differences in the isoenzyme composition of the myosins.
TL;DR: A decline in the synthesis rate of myosin heavy chain implies a decreased ability to remodel this important muscle contractile protein and likely contributes to the declining muscle mass and contractile function in the elderly.
Abstract: A decline in muscle mass and contractile function are prominent features of the sarcopenia of old age. Because myosin heavy chain is an important contractile protein, it was hypothesized that synth...
TL;DR: The heart and those striated muscles that contract for long periods, having available almost limitless oxygen, operate in sustained steady states of low sarcoplasmic oxygen pressure that resist change in response to changing muscle work or oxygen supply.
Abstract: The heart and those striated muscles that contract for long periods, having available almost limitless oxygen, operate in sustained steady states of low sarcoplasmic oxygen pressure that resist change in response to changing muscle work or oxygen supply. Most of the oxygen pressure drop from the erythrocyte to the mitochondrion occurs across the capillary wall. Within the sarcoplasm, myoglobin, a mobile carrier of oxygen, is developed in response to mitochondrial demand and augments the flow of oxygen to the mitochondria. Myoglobin-facilitated oxygen diffusion, perhaps by virtue of reduction of dimensionality of diffusion from three dimensions towards two dimensions in the narrow spaces available between mitochondria, is rapid relative to other parameters of cell respiration. Consequently, intracellular gradients of oxygen pressure are shallow, and sarcoplasmic oxygen pressure is nearly the same everywhere. Sarcoplasmic oxygen pressure, buffered near 0.33 kPa (2.5 torr; equivalent to approximately 4 micro mol l(-1) oxygen) by equilibrium with myoglobin, falls close to the operational K(m) of cytochrome oxidase for oxygen, and any small increment in sarcoplasmic oxygen pressure will be countered by increased oxygen utilization. The concentration of nitric oxide within the myocyte results from a balance of endogenous synthesis and removal by oxymyoglobin-catalyzed dioxygenation to the innocuous nitrate. Oxymyoglobin, by controlling sarcoplasmic nitric oxide concentration, helps assure the steady state in which inflow of oxygen into the myocyte equals the rate of oxygen consumption.