scholarly journals Muscle-Type Specific Autophosphorylation of CaMKII Isoforms after Paced Contractions

2014 ◽  
Vol 2014 ◽  
pp. 1-20 ◽  
Author(s):  
Wouter Eilers ◽  
Wouter Gevers ◽  
Daniëlle van Overbeek ◽  
Arnold de Haan ◽  
Richard T. Jaspers ◽  
...  
Keyword(s):  
Buffer Capacity ◽  
Muscle Type ◽  
Gastrocnemius Medialis ◽  
Calcium Buffer ◽  
Calcium Sensing ◽  
Slow Type ◽  
Muscle Types ◽  
Specific Increase ◽  
Isoform Specificity ◽  
Specific Regulation

We explored to what extent isoforms of the regulator of excitation-contraction and excitation-transcription coupling, calcium/calmodulin protein kinase II (CaMKII) contribute to the specificity of myocellular calcium sensing between muscle types and whether concentration transients in its autophosphorylation can be simulated. CaMKII autophosphorylation at Thr287 was assessed in three muscle compartments of the rat after slow or fast motor unit-type stimulation and was compared against a computational model (CaMuZclE) coupling myocellular calcium dynamics with CaMKII Thr287 phosphorylation. Qualitative differences existed between fast- (gastrocnemius medialis) and slow-type muscle(soleus)for the expression pattern of CaMKII isoforms. Phospho-Thr287 content ofδA CaMKII, associated with nuclear functions, demonstrated a transient and compartment-specific increase after excitation, which contrasted to the delayed autophosphorylation of the sarcoplasmic reticulum-associatedβM CaMKII. In soleus muscle, excitation-inducedδA CaMKII autophosphorylation demonstrated frequency dependence (P= 0.02). In the glycolytic compartment ofgastrocnemius medialis, CaMKII autophosphorylation after excitation was blunted.In silicoassessment emphasized the importance of mitochondrial calcium buffer capacity for excitation-induced CaMKII autophosphorylation but did not predict its isoform specificity. The findings expose that CaMKII autophosphorylation with paced contractions is regulated in an isoform and muscle type-specific fashion and highlight properties emerging for phenotype-specific regulation of CaMKII.

scholarly journals The Drosophila indirect flight muscle myosin heavy chain isoform is insufficient to transform the jump muscle into a highly stretch-activated muscle type

2017 ◽  
Vol 312 (2) ◽  
pp. C111-C118 ◽  
Author(s):  
Cuiping Zhao ◽  
Douglas M. Swank
Keyword(s):  
Power Generation ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Flight Muscle ◽  
Fold Increase ◽  
Isometric Tension ◽  
Indirect Flight Muscle ◽  
Muscle Type ◽  
Myosin Heavy Chain Isoform ◽  
Muscle Types

Stretch activation (SA) is a delayed increase in force that enables high power and efficiency from a cyclically contracting muscle. SA exists in various degrees in almost all muscle types. In Drosophila, the indirect flight muscle (IFM) displays exceptionally high SA force production ( FSA), whereas the jump muscle produces only minimal FSA. We previously found that expressing an embryonic (EMB) myosin heavy chain (MHC) isoform in the jump muscle transforms it into a moderately SA muscle type and enables positive cyclical power generation. To investigate whether variation in MHC isoforms is sufficient to produce even higher FSA, we substituted the IFM MHC isoform (IFI) into the jump muscle. Surprisingly, we found that IFI only caused a 1.7-fold increase in FSA, less than half the increase previously observed with EMB, and only at a high Pi concentration, 16 mM. This IFI-induced FSA is much less than what occurs in IFM, relative to isometric tension, and did not enable positive cyclical power generation by the jump muscle. Both isometric tension and FSA of control fibers decreased with increasing Pi concentration. However, for IFI-expressing fibers, only isometric tension decreased. The rate of FSA generation was ~1.5-fold faster for IFI fibers than control fibers, and both rates were Pi dependent. We conclude that MHC isoforms can alter FSA and hence cyclical power generation but that isoforms can only endow a muscle type with moderate FSA. Highly SA muscle types, such as IFM, likely use a different or additional mechanism.

Mechanical properties of isolated human esophageal smooth muscle

1990 ◽  
Vol 258 (3) ◽  
pp. G338-G343 ◽  
Author(s):  
A. Tottrup ◽  
A. Forman ◽  
N. Uldbjerg ◽  
P. Funch-Jensen ◽  
K. E. Andersson
Keyword(s):  
Smooth Muscle ◽  
Esophagogastric Junction ◽  
Active Tension ◽  
Muscle Type ◽  
Optimum Length ◽  
Tension Development ◽  
Resting Tension ◽  
Muscle Types ◽  
Human Esophagus

Isolated smooth muscle strips from the human esophagus representing both the longitudinal and circular layers of the esophagogastric junction and the esophageal body were prepared. The strips were mounted in organ baths, and resting length was defined. By repeatedly increasing the length of the strips with 20% of resting length and recording values of resting and active tensions, length-tension relations for each muscle type were constructed. Only circular strips from the esophagogastric junction developed active, resting tension, disclosed by replacing the normal Ca2(+)-containing Krebs solution with Ca2(+)-free medium. Carbachol (10(-6) M) was used for submaximal activation of the contractile apparatus. At lengths between 180 and 260% of resting length, all strips reached optimum length (LO) where further elongation gave no further increase in active tension development. Repeated stimulations with carbachol was possible at a length of 200% of LO without affecting reproducibility. Determination of different collagen components revealed no differences between muscle types.

Effect of prior eccentric contractions on lactate/H+ transport in rat skeletal muscle

1998 ◽  
Vol 274 (3) ◽  
pp. E554-E559 ◽  
Author(s):  
Henriette Pilegaard ◽  
Sven Asp
Keyword(s):  
Skeletal Muscle ◽  
Buffer Capacity ◽  
Ph Regulation ◽  
Eccentric Contractions ◽  
Lactate Transport ◽  
Giant Vesicles ◽  
Muscle Lactate ◽  
Muscle Ph ◽  
Supramaximal Stimulation ◽  
Muscle Types

The effect of prior eccentric contractions on skeletal muscle lactate/H+transport was investigated in rats. Lactate transport was measured in sarcolemmal giant vesicles obtained from soleus and red (RG) and white gastrocnemii (WG) muscles 2 days after intense eccentric contractions (ECC) and from the corresponding contralateral control (CON) muscles. The physiochemical buffer capacity was determined in the three muscle types from both ECC and CON legs. Furthermore, the effect of prior eccentric contractions on release and muscle content of lactate and H+ during and after supramaximal stimulation was examined using the perfused rat hindlimb preparation. The lactate transport rate was lower ( P < 0.05) in vesicles obtained from ECC-WG (29%) and ECC-RG (13%) than in vesicles from the CON muscles. The physiochemical buffer capacity was reduced ( P < 0.05) in ECC-WG (13%) and ECC-RG (9%) compared with the corresponding CON muscles. There were only marginal effects on the soleus muscle. Muscle lactate concentrations and release of lactate during recovery from intense isometric contractions were lower ( P< 0.05) in ECC than in CON hindlimbs, indicating decreased anaerobic glycogenolysis. In conclusion, the sarcolemmal lactate/H+ transport capacity and the physiochemical buffer capacity were reduced in prior eccentrically stimulated WG and RG in rats, suggesting that muscle pH regulation may be impaired after unaccustomed eccentric exercise. In addition, the data indicate that the glycogenolytic potential is decreased in muscles exposed to prior eccentric contractions.

scholarly journals Insulin-modulated Akt subcellular localization determines Akt isoform-specific signaling

2009 ◽  
Vol 106 (17) ◽  
pp. 7004-7009 ◽  
Author(s):  
Eva Gonzalez ◽  
Timothy E. McGraw
Keyword(s):  
Glucose Transporter ◽  
Membrane Association ◽  
Ph Domain ◽  
Functional Specificity ◽  
Signaling Specificity ◽  
Akt Isoforms ◽  
Regulation Of Metabolism ◽  
Isoform Specificity ◽  
Subcellular Compartmentalization ◽  
Specific Regulation

The 3 Akt protein kinase isoforms have critical and distinct functions in the regulation of metabolism, cell growth, and apoptosis, yet the mechanisms by which their signaling specificity is achieved remain largely unclear. Here, we investigated potential mechanisms underlying Akt isoform functional specificity by using Akt2-specific regulation of glucose transport in insulin-stimulated adipocytes as a model system. We found that insulin activates both Akt1 and Akt2 in adipocytes, but differentially regulates the subcellular distribution of these Akt isoforms. The greater accumulation of Akt2 at the plasma membrane (PM) of insulin-stimulated adipocytes correlates with Akt2-specific regulation of the trafficking of the GLUT4 glucose transporter. Consistent with this pattern, Akt constructs that do not accumulate at the PM to the same degree as Akt2 fail to regulate GLUT4 translocation to the PM, whereas enhancement of Akt1 PM association through mutation in Akt1 PH domain is sufficient to overcome Akt-isoform specificity in GLUT4 regulation. Indeed, we found that this distinct insulin-induced PM accumulation of Akt kinases is translated into a differential regulation by the Akt isoforms of AS160, a RabGAP that regulates GLUT4 trafficking. Our data show that Akt2 specifically regulates AS160 phosphorylation and membrane association providing molecular basis for Akt2 specificity in the modulation of GLUT4 trafficking. Together, our findings reveal the stimulus-induced subcellular compartmentalization of Akt kinases as a mechanism contributing to specify Akt isoform functions.

Cell-specific regulation of cytosolic aspartate aminotransferase by glucocorticoids in the rat kidney

1993 ◽  
Vol 265 (5) ◽  
pp. C1298-C1305 ◽  
Author(s):  
S. Feilleux-Duche ◽  
M. Garlatti ◽  
M. Aggerbeck ◽  
M. Poyard ◽  
J. Bouguet ◽  
...  
Keyword(s):  
Aspartate Aminotransferase ◽  
Hormonal Regulation ◽  
Renal Cortex ◽  
Rat Kidney ◽  
Thick Ascending Limb ◽  
Outer Medulla ◽  
Maximal Increase ◽  
Basal Expression ◽  
Specific Increase ◽  
Specific Regulation

The basal expression and hormonal regulation of cytosolic aspartate aminotransferase (cAspAT) were investigated in the rat kidney. In adrenalectomized animals, the basal activity was highest in the renal cortex and in the inner stripe of the outer medulla (0.1-0.15 U/mg protein). The glucocorticoid analogue dexamethasone increased cAspAT activity about twofold in the cortex and in the inner stripe of the outer medulla but not in the papilla. A half-maximal increase in the activity was achieved at doses of approximately 5 micrograms/100 g body wt. The mineralocorticoid aldosterone did not modify the cAspAT activity. The cell specificity of the hormonal regulation was analyzed by in situ hybridization. In untreated adrenalectomized rats, a cAspAT cRNA probe labeled mainly the inner stripe of the outer medulla. After dexamethasone or hydrocortisone treatment, labeling was uniformly increased in this part of the medulla and was heterogeneously increased in the renal cortex. The specific increase in labeling within the cortex was shown to be confined to the distal convoluted tubule and the thick ascending limb. We conclude that, in addition to widespread basal expression, cAspAT is regulated by glucocorticoids in a highly cell-specific manner in the renal cortex. The enzyme may thus participate in the increased energy metabolism elicited by these hormones in these cells.

scholarly journals Rats genetically selected for low and high aerobic capacity exhibit altered soleus muscle myofilament functions

2020 ◽  
Vol 318 (2) ◽  
pp. C422-C429
Author(s):  
B. J. Biesiadecki ◽  
M. A. Brotto ◽  
L. S. Brotto ◽  
L. G. Koch ◽  
S. L. Britton ◽  
...  
Keyword(s):  
Muscle Force ◽  
Protein Composition ◽  
Contractile Properties ◽  
Muscle Type ◽  
Slow Fiber ◽  
Fast Fiber ◽  
Aerobic Exercise Capacity ◽  
Slow Type ◽  
Intact Muscle ◽  
Health And Disease

Aerobic exercise capacity is critical to bodily health. As a model to investigate the mechanisms that determine health and disease, we employed low (LCR) and high (HCR) capacity running rat models selectively bred to concentrate the genes responsible for divergent aerobic running capacity. To investigate the skeletal muscle contribution to this innate difference in running capacity we employed an approach combining examination of the myofilament protein composition and contractile properties of the fast fiber extensor digitorum longus (EDL) and slow fiber soleus (SOL) muscles from LCR and HCR rats. Intact muscle force experiments demonstrate that SOL, but not EDL, muscles from LCR rats exhibit a three times greater decrease in fatigued force. To investigate the mechanism of this increased fatigability in the LCR SOL muscle, we determined the myofilament protein composition and functional properties. Force-Ca2+ measurements demonstrate decreased Ca2+ sensitivity of single skinned SOL muscle fibers from LCR compared with that of HCR rats. Segregating SOL fibers into fast and slow types demonstrates that the decreased Ca2+ sensitivity in LCR SOL results from a specific decrease in slow-type SOL fiber Ca2+ sensitivity such that it was similar to that of fast-type fibers. These results identify that the altered myofilament contractile properties of LCR SOL slow-type fibers result in a fast muscle type Ca2+ sensitivity and the LCR muscle phenotype. Overall our findings demonstrate alterations of the myofilament proteins could contribute to fatigability of the SOL muscle and the decreased innate aerobic running performance of LCR compared with HCR rats.

scholarly journals Downstream of Identity Genes: Muscle-Type-Specific Regulation of the Fusion Process

2010 ◽  
Vol 19 (2) ◽  
pp. 317-328 ◽  
Author(s):  
Laetitia Bataillé ◽  
Isabelle Delon ◽  
Jean Philippe Da Ponte ◽  
Nicholas H. Brown ◽  
Krzysztof Jagla
Keyword(s):  
Fusion Process ◽  
Muscle Type ◽  
Specific Regulation

Effect of cold acclimation on troponin I isoform expression in striated muscle of rainbow trout

2012 ◽  
Vol 303 (2) ◽  
pp. R168-R176 ◽  
Author(s):  
Sarah L. Alderman ◽  
Jordan M. Klaiman ◽  
Courtney A. Deck ◽  
Todd E. Gillis
Keyword(s):  
Rainbow Trout ◽  
Cold Acclimation ◽  
Troponin I ◽  
Striated Muscle ◽  
Protein Isoforms ◽  
Specific Gene ◽  
Muscle Type ◽  
Gene Transcripts ◽  
Muscle Types ◽  
Isoform Expression

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.

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