Transcription rates of SERCA and phospholamban genes change in response to chronic stimulation of skeletal muscle

Hu, Ping; Zhang, K M; Spratt, John A.; Wechsler, Andrew S.; Briggs, F. Norman

doi:10.1016/s0167-4781(97)00135-8

Cited by 8 publications

(3 citation statements)

References 13 publications

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“…The rat SERCA1 proximal promoter contains no Sp1 sites, and although it contains three of the related GC-rich CACC sites, the difference in the GC content of rat SERCA1 promoter (62.4%) versus the rabbit SERCA2 (81.6%) and human SERCA3 (81.2%) promoters suggests that transcriptional regulation of SERCA1 is distinct. This idea is further supported by the observation that thyroid stimulation (44,45) and contractile activity (14,17,19,46) differentially target SERCA1 and SERCA2a in skeletal muscle.…”

Section: Discussionmentioning

confidence: 76%

“…Increased contractile activity leads to decreases in SERCA1 and SERCA2a expression in skeletal (13,14) and cardiac (15,16) muscle, respectively, whereas decreased contractile activity leads to increases in expression (17)(18)(19). SERCA1 expression is particularly sensitive to the reduction of contractile activity due to rat soleus muscle unloading, with significant increases by 2 days and 7-fold increases by 7 days (19).…”

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confidence: 99%

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Identification of Weight-bearing-responsive Elements in the Skeletal Muscle Sarco(endo)plasmic Reticulum Ca2+ ATPase (SERCA1) Gene

Mitchell-Felton

Hunter

Stevenson

et al. 2000

Journal of Biological Chemistry

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The skeletal muscle sarco(endo)plasmic reticulum calcium ATPase (SERCA1) gene is transactivated as early as 2 days after the removal of weight-bearing (Peters, D. G., Mitchell-Felton, H., and Kandarian, S. C. (1999) Am. J. Physiol. 276, C1218-C1225), but the transcriptional mechanisms are elusive. Here, the rat SERCA1 5 flank and promoter region (؊3636 to ؉172 base pairs) was comprehensively examined using in vivo somatic gene transfer into rat soleus muscles (n ‫؍‬ 804) to identify region(s) that are both necessary and sufficient for sensitivity to weight-bearing. In all, 40 different SERCA1 reporter plasmids were constructed and tested. Several different regions of the SERCA1 5 flank were sufficient to confer a transcriptional response to 7 days of muscle unloading when placed upstream of a heterologous promoter. Two of these regions were analyzed further because they were necessary for the unloading response of ؊3636 to ؉172, as demonstrated using internal deletion constructs. Deletion analysis of these regions (؊1373 to ؊1158 and ؊330 to ؉172) suggested that unloading responsiveness corresponded to CACC sites and E-boxes. Mutagenesis of cis-elements in the first region showed that a specific CACC box (؊1262) was involved in SERCA1 transactivation and a nearby E-box (؊1248) was also implicated. Constructs containing trimerized CACC sites and E-boxes showed that the presence of both elements is required to activate transcription. This is the first identification of specific ciselements required for the regulation of a Ca 2؉ handling gene by changes in muscle loading condition.The sarco(endo)plasmic reticulum is the major organelle that regulates the Ca 2ϩ signaling associated with a multitude of cellular processes (1, 2). The sarco(endo)plasmic reticulum Ca 2ϩ ATPase (SERCA) 1 proteins translocate Ca 2ϩ from the cytosol to the sarcoplasmic reticulum or endoplasmic reticulum lumen, thereby reducing intracellular Ca 2 and refilling the sarcoplasmic/endoplasmic reticulum Ca 2ϩ stores. The cloning, expression, and functional characterization of three SERCA genes and their splicing variants have been described (3-12).At least one of the SERCA gene products is expressed in every mammalian tissue studied, emphasizing the fundamental role of this protein in cellular function. Products of the SERCA1 gene are the predominant isoforms expressed in skeletal muscle (SERCA1a adult, SERCA1b neonatal) (4, 9), and one product of the SERCA2 gene is the predominant isoform expressed in cardiac myocytes (SERCA2a (3)). The alternative splicing product of SERCA2 (SERCA2b (3)) and the products of the SERCA3 gene (3, 11) are ubiquitously expressed in muscle and non-muscle tissue but in much lower levels. SERCA expression is much higher in striated muscle than in smooth muscle or non-muscle to accommodate the large calcium fluxes associated with excitation-contraction coupling.Contractile activity has a marked effect on SERCA expression in striated muscle. Increased contractile activity leads to decreases in SERCA1 and SERCA2a express...

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Section: Discussionmentioning

confidence: 76%

mentioning

confidence: 99%

Identification of Weight-bearing-responsive Elements in the Skeletal Muscle Sarco(endo)plasmic Reticulum Ca2+ ATPase (SERCA1) Gene

Mitchell-Felton

Hunter

Stevenson

et al. 2000

Journal of Biological Chemistry

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“…SERCA isoform switching; [49]). This idea is supported by the observation in human skeletal muscle that SERCA activity and subtype expression depend on fibre type [50] and that transcription rates of SERCA and phospholamban genes change in response to chronic stimulation [51]. On the other hand, decoding of the Ca 2+ signal might be altered by expression of CaMKII isoforms with different Ca 2+ -dependent kinetics [52].…”

Section: Physiological Implicationsmentioning

confidence: 88%

Amplitude modulation of nuclear Ca2+ signals in human skeletal myotubes: A possible role for nuclear Ca2+ buffering

Koopman¹,

Willems²,

Oosterhof³

et al. 2005

Cell Calcium

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Video-rate confocal microscopy of Indo-1-loaded human skeletal myotubes was used to assess the relationship between the changes in sarcoplasmic ( [Ca 2+ ] N then increased to a maximum that was 2.3-fold higher than that of the single transient and equalled that of [Ca 2+ ] S . In the nucleus, and to a lesser extent in the sarcoplasm, [Ca 2+ ] decreased faster at the end of the stimulus train than after the preceding single stimulus (time constants of 3.3 and 2.1 s, respectively). To gain insight into the molecular principles underlying the shaping of the nuclear Ca 2+ signal, a 3-D mathematical model was constructed. Intriguingly, quantitative modelling required the inclusion of a satiable nuclear Ca 2+ buffer. Alterations in the concentration of this putative buffer had dramatic effects on the kinetics of the nuclear Ca 2+ signal. This finding unveils a possible mechanism by which the skeletal muscle can adapt to changes in physiological demand.

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How Animals Move: Comparative Lessons on Animal Locomotion

Schaeffer

Lindstedt

2013

Comprehensive Physiology

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Comparative physiology often provides unique insights in animal structure and function. It is specifically through this lens that we discuss the fundamental properties of skeletal muscle and animal locomotion, incorporating variation in body size and evolved difference among species. For example, muscle frequencies in vivo are highly constrained by body size, which apparently tunes muscle use to maximize recovery of elastic recoil potential energy. Secondary to this constraint, there is an expected linking of skeletal muscle structural and functional properties. Muscle is relatively simple structurally, but by changing proportions of the few muscle components, a diverse range of functional outputs is possible. Thus, there is a consistent and predictable relation between muscle function and myocyte composition that illuminates animal locomotion. When animals move, the mechanical properties of muscle diverge from the static textbook force-velocity relations described by A. V. Hill, as recovery of elastic potential energy together with force and power enhancement with activation during stretch combine to modulate performance. These relations are best understood through the tool of work loops. Also, when animals move, locomotion is often conveniently categorized energetically. Burst locomotion is typified by high-power outputs and short durations while sustained, cyclic, locomotion engages a smaller fraction of the muscle tissue, yielding lower force and power. However, closer examination reveals that rather than a dichotomy, energetics of locomotion is a continuum. There is a remarkably predictable relationship between duration of activity and peak sustainable performance.

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Transcription rates of SERCA and phospholamban genes change in response to chronic stimulation of skeletal muscle

Cited by 8 publications

References 13 publications

Identification of Weight-bearing-responsive Elements in the Skeletal Muscle Sarco(endo)plasmic Reticulum Ca2+ ATPase (SERCA1) Gene

Identification of Weight-bearing-responsive Elements in the Skeletal Muscle Sarco(endo)plasmic Reticulum Ca2+ ATPase (SERCA1) Gene

Amplitude modulation of nuclear Ca2+ signals in human skeletal myotubes: A possible role for nuclear Ca2+ buffering

How Animals Move: Comparative Lessons on Animal Locomotion

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