scholarly journals Length‐dependent activation in three striated muscle types of the rat

2002 ◽  
Vol 544 (1) ◽  
pp. 225-236 ◽  
Author(s):  
John P. Konhilas ◽  
Thomas C. Irving ◽  
Pieter P. Tombe
Author(s):  
Brian Glancy ◽  
Robert S Balaban

The design of the energy metabolism system in striated muscle remains a major area of investigation. Here, we review our current understanding and emerging hypotheses regarding the metabolic support of muscle contraction. Maintenance of ATP free energy, so called energy homeostasis, via mitochondrial oxidative phosphorylation is critical to sustained contractile activity and this major design criterion is the focus of this review. Cell volume invested in mitochondria reduces the space available for generating contractile force, and this spatial balance between mitochondria and contractile elements to meet the varying sustained power demands across muscle types is another important design criterion. This is accomplished with remarkably similar mass-specific mitochondrial protein composition across muscle types, implying that it is the organization of mitochondria within the muscle cell that is critical to supporting sustained muscle function. Beyond the production of ATP, ubiquitous distribution of ATPases throughout the muscle requires rapid distribution of potential energy across these large cells. Distribution of potential energy has long been thought to occur primarily through facilitated metabolite diffusion but recent analysis has questioned the importance of this process under normal physiological conditions. Recent structural and functional studies have supported the hypothesis that the mitochondrial reticulum provides a rapid energy distribution system via the conduction of the mitochondrial membrane potential to maintain metabolic homeostasis during contractile activity. We extensively review this aspect of the energy metabolism design contrasting it with metabolite diffusion models and how mitochondrial structure can play a role in the delivery of energy in the striated muscle.


Muscles like the smooth adductors of lamellibranch molluscs, and the anterior byssus retractor of Mytilus ( ABRM ) possess two remarkable features which have been studied intensively during recent years. They can maintain a steady level of tension (tonic contraction) for longer than any other muscle type (see Marceau 1909), and their contractile apparatus contains, in addition to the usual actomyosin, large quantities of a protein (tropomyosin A—TMA ) apparently not found in vertebrate striated muscle (Bailey 1956; Kominz, Saad & Laki 1957). As in vertebrate striated muscle, the contractile apparatus of these smooth molluscan muscles contains two kinds of filaments, thin ones and thicker ones (Hanson & Lowy 1959; Philpott, Kahlbrock & Szent-Györgyi 1960). In both muscle types the thin filaments are of similar diameter and contain actin; but the diameter of the thick filaments is about ten times greater in the molluscan muscles, and it is these filaments which contain TMA (see Lowy & Hanson 1962). When large quantities of TMA were found in these molluscan muscles, their outstanding capacity for tonic contraction was not unnaturally connected with the presence of that protein (Bailey 1957). A hypothesis was proposed according to which there exist in such muscles two independent systems acting in parallel: the usual actomyosin system which produces tension, and a unique system ( TMA filaments) which, by becoming rigid, can maintain this tension with negligible energy expenditure, after the actomyosin system has relaxed (Rüegg 1958; Johnson, Kahn & Szent-Györgyi 1959). The evidence in support of this ‘independent catch hypothesis’ is based on studies with preparations of TMA , on experiments with glycerol-extracted muscles, and on certain experiments with the living ABRM treated with thiourea. Results obtained from structural studies and from extensive investigations on living tonic molluscan muscles have suggested an alternative hypothesis, the ‘linkage hypothesis’. This holds that, as in vertebrate striated muscle, tension in tonic molluscan muscles is both generated and maintained by the same system, which is one that involves interaction between adjacent actin- and myosin-containing filaments in a sliding filament system (Lowy & Millman 1959 b , 1963).


1990 ◽  
Vol 69 (1) ◽  
pp. 321-327 ◽  
Author(s):  
D. P. Fitzsimons ◽  
R. E. Herrick ◽  
K. M. Baldwin

In this study we examined the effects of 6-8 wk of thyroid hormone manipulation on striated muscle isomyosin expression in adult female rats. Animals were randomly assigned to one of three groups: 1) euthyroid controls, 2) thyroid deficient (propylthiouracil treated), and 3) hyperthyroid (triiodothyronine treated). Thyroid deficiency resulted in a marked increase in the low-adenosinetriphosphatase V3 isoform by 20- and 49-fold in the left and right ventricle, respectively. Conversely, hyperthyroidism induced a modest (3-11%) but significant increase in the high-adenosinetriphosphatase V1 isoform in both ventricles. The thyroid-deficient rats exhibited significant increases in slow myosin in both soleus (8%) and red gastrocnemius (24%), with concomitant reductions in intermediate myosin in both muscles. Interestingly, while the slow-myosin isoform was decreased in both the soleus (-19%) and the red gastrocnemius (-43%) of the hyperthyroid group, the intermediate-myosin isoform was affected differentially in the two muscles, with a fivefold increase in the former vs. a 16% decrease in the latter. Furthermore, hyperthyroidism increased the fast myosins in the red gastrocnemius while exerting no effect on the same isoforms in the white gastrocnemius. Collectively these data suggest both different specificity and sensitivity among the myosin genes of different striated muscle types in response to thyroid hormone.


2012 ◽  
Vol 303 (2) ◽  
pp. R168-R176 ◽  
Author(s):  
Sarah L. Alderman ◽  
Jordan M. Klaiman ◽  
Courtney A. Deck ◽  
Todd E. Gillis

In vertebrates each of the three striated muscle types (fast skeletal, slow skeletal, and cardiac) contain distinct isoforms of a number of different contractile proteins including troponin I (TnI). The functional characteristics of these proteins have a significant influence on muscle function and contractility. The purpose of this study was to characterize which TnI gene and protein isoforms are expressed in the different muscle types of rainbow trout ( Oncorhynchus mykiss) and to determine whether isoform expression changes in response to cold acclimation (4°C). Semiquantitative real-time PCR was used to characterize the expression of seven different TnI genes. The sequence of these genes, cloned from Atlantic salmon ( Salmo salar) and rainbow trout, were obtained from the National Center for Biotechnology Information databases. One-dimensional gel electrophoresis and tandem mass spectrometry were used to identify the TnI protein isoforms expressed in each muscle type. Interestingly, the results indicate that each muscle type expresses the gene transcripts of up to seven TnI isoforms. There are significant differences, however, in the expression pattern of these genes between muscle types. In addition, cold acclimation was found to increase the expression of specific gene transcripts in each muscle type. The proteomics analysis demonstrates that fast skeletal and cardiac muscle contain three TnI isoforms, whereas slow skeletal muscle contains four. No other vertebrate muscle to date has been found to express as many TnI protein isoforms. Overall this study underscores the complex molecular composition of teleost striated muscle and suggests there is an adaptive value to the unique TnI profiles of each muscle type.


Author(s):  
William J. Dougherty ◽  
Samuel S. Spicer

In recent years, considerable attention has focused on the morphological nature of the excitation-contraction coupling system of striated muscle. Since the study of Porter and Palade, it has become evident that the sarcoplastic reticulum (SR) and transverse tubules constitute the major elements of this system. The problem still exists, however, of determining the mechamisms by which the signal to interdigitate is presented to the thick and thin myofilaments. This problem appears to center on the movement of Ca++ions between myofilaments and SR. Recently, Philpott and Goldstein reported acid mucosubstance associated with the SR of fish branchial muscle using the colloidal thorium dioxide technique, and suggested that this material may serve to bind or release divalent cations such as Ca++. In the present study, Hale's iron solution adapted to electron microscopy was applied to formalin-fixed myofibrils isolated from glycerol-extracted rabbit psoas muscles and to frozen sections of formalin-fixed rat psoas muscles.


Author(s):  
W. J. Larsen ◽  
R. Azarnia ◽  
W. R. Loewenstein

Although the physiological significance of the gap junction remains unspecified, these membrane specializations are now recognized as common to almost all normal cells (excluding adult striated muscle and some nerve cells) and are found in organisms ranging from the coelenterates to man. Since it appears likely that these structures mediate the cell-to-cell movement of ions and small dye molecules in some electrical tissues, we undertook this study with the objective of determining whether gap junctions in inexcitable tissues also mediate cell-to-cell coupling.To test this hypothesis, a coupling, human Lesh-Nyhan (LN) cell was fused with a non-coupling, mouse cl-1D cell, and the hybrids, revertants, and parental cells were analysed for coupling with respect both to ions and fluorescein and for membrane junctions with the freeze fracture technique.


Author(s):  
J. Borejdo ◽  
S. Burlacu

Polarization of fluorescence is a classical method to assess orientation or mobility of macromolecules. It has been a common practice to measure polarization of fluorescence through a microscope to characterize orientation or mobility of intracellular organelles, for example anisotropic bands in striated muscle. Recently, we have extended this technique to characterize single protein molecules. The scientific question concerned the current problem in muscle motility: whether myosin heads or actin filaments change orientation during contraction. The classical view is that the force-generating step in muscle is caused by change in orientation of myosin head (subfragment-1 or SI) relative to the axis of thin filament. The molecular impeller which causes this change resides at the interface between actin and SI, but it is not clear whether only the myosin head or both SI and actin change orientation during contraction. Most studies assume that observed orientational change in myosin head is a reflection of the fact that myosin is an active entity and actin serves merely as a passive "rail" on which myosin moves.


Author(s):  
Gisèle Nicolas ◽  
Jean-Marie Bassot ◽  
Marie-Thérèse Nicolas

The use of fast-freeze fixation (FFF) followed by freeze-substitution (FS) brings substantial advantages which are due to the extreme rapidity of this fixation compared to the conventional one. The initial step, FFF, physically immobilizes most molecules and therefore arrests the biological reactions in a matter of milliseconds. The second step, FS, slowly removes the water content still in solid state and, at the same time, chemically fixes the other cell components in absence of external water. This procedure results in an excellent preservation of the ultrastructure, avoids osmotic artifacts,maintains in situ most soluble substances and keeps up a number of cell activities including antigenicities. Another point of interest is that the rapidity of the initial immobilization enables the capture of unstable structures which, otherwise, would slip towards a more stable state. When combined with electrophysiology, this technique arrests the ultrastructural modifications at a well defined state, allowing a precise timing of the events.We studied the epithelium of the elytra of the scale-worm, Harmothoe lunulata which has excitable, conductible and bioluminescent properties. The intracellular sites of the light emission are paracrystals of endoplasmic reticulum (PER), named photosomes (Fig.1). They are able to flash only when they are coupled with plasma membrane infoldings by dyadic or triadic junctions (Fig.2) basically similar to those of the striated muscle fibers. We have studied them before, during and after stimulation. FFF-FS showed that these complexes are labile structures able to diffentiate and dedifferentiate within milliseconds. Moreover, a transient network of endoplasmic reticulum was captured which we have named intermediate endoplasmic reticulum (IER) surrounding the PER (Fig.1). Numerous gap junctions are found in the membranous infoldings of the junctional complexes (Fig.3). When cryofractured, they cleave unusually (Fig.4-5). It is tempting to suggest that they play an important role in the conduction of the excitation.


2019 ◽  
Vol 47 (5) ◽  
pp. 1393-1404 ◽  
Author(s):  
Thomas Brand

Abstract The Popeye domain-containing gene family encodes a novel class of cAMP effector proteins in striated muscle tissue. In this short review, we first introduce the protein family and discuss their structure and function with an emphasis on their role in cyclic AMP signalling. Another focus of this review is the recently discovered role of POPDC genes as striated muscle disease genes, which have been associated with cardiac arrhythmia and muscular dystrophy. The pathological phenotypes observed in patients will be compared with phenotypes present in null and knockin mutations in zebrafish and mouse. A number of protein–protein interaction partners have been discovered and the potential role of POPDC proteins to control the subcellular localization and function of these interacting proteins will be discussed. Finally, we outline several areas, where research is urgently needed.


Author(s):  
Tara A Shrout

Titin is the largest known protein in the human body, and forms the backbone of all striated muscle sarcomeres. The elastic nature of titin is an important component of muscle compliance and functionality. A significant amount of energy is expended to synthesize titin, thus we postulate that titin gene expression is under strict regulatory control in order to conserve cellular resources. In general, gene expression is mediated in part by post-transcriptional control elements located within the 5’ and 3’ untranslated regions (UTRs) of mature mRNA. The 3’UTR in particular contains structural features that affect binding capacity to other RNA components, such as MicroRNA, which control mRNA localization, translation, and degradation. The degree and significance of the regulatory effects mediated by two determined variants of titin’s 3’ UTR were evaluated in Neonatal Rat Ventricular Myocyte and Human Embryonic Kidney cell lines. Recombinant plasmids to transfect these cells lines were engineered by insertion of the variant titin 3’UTR 431- and 1047-base pairs sequences into luciferase reporter vectors. Expression due to an unaltered reporter vector served as the control. Quantitative changes in luciferase activity due to the recombinants proportionally represented the effect titin’s respective 3’UTR conferred on downstream post-transcriptional expression relative to the control. The effect due to titin’s shorter 3’UTR sequence was inconclusive; however, results illustrated that titin’s longer 3’UTR sequence caused a 35 percent decrease in protein expression. Secondary structural analysis of the two sequences revealed differential folding patterns that affect the stability and degree of MicroRNA-binding within titin’s variant 3’UTR sequences.


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