Transcriptional Regulation of Phospholamban Gene and Translational Regulation of SERCA2 Gene Produces Coordinate Expression of These Two Sarcoplasmic Reticulum Proteins during Skeletal Muscle Phenotype Switching

Hu, Ping; Yin, Chang; Zhang, Ke-Min; Wright, Leon D.; Nixon, Todd E.; Wechsler, Andrew S.; Spratt, John A.; Briggs, F. Norman

doi:10.1074/jbc.270.19.11619

Cited by 42 publications

(25 citation statements)

References 18 publications

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“…The assignment was also based on the observation by Ennion, Pereira, Sargent, Young & Goldspink (1995) that large mammals, like humans, do not express the HC-IIb isoform. mRNA detection by Northern blot The slow -and fast-twitch isoforms of sarco-/endoplasmic reticulum Ca2+-ATPase (SERCA2a and SERCA1a, respectively) and phospholamban mRNAs were detected as described by Hu et al (1995). Total RNA was extracted from frozen muscle by the guanidinium thiocyanate method (Chomczynski & Sacchi, 1987).…”

Section: Methodsmentioning

confidence: 99%

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Salbutamol changes the molecular and mechanical properties of canine skeletal muscle.

Zhang

Wang

et al. 1996

The Journal of Physiology

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1. Salbutamol, a fl2-agonist, increased the weight of the canine latissimus dorsi muscle. It also increased fusion frequency, and decreased time-to-peak tension, half-relaxation time, and total contraction time. These changes in twitch times and fusion frequency were associated with changes in the levels of proteins expressed in slow-and fast-twitch fibres. Salbutamol decreased the levels of the slow-twitch cardiac isoform of sarco-/endoplasmic reticulum Ca2P-ATPase (SERCA2a) and phospholamban proteins, and increased the level of the fast-twitch isoform of sarco-/endoplasmic reticulum Ca2+-ATPase (SERCAla).2. Changes in the levels of SERCA proteins, particularly SERCAla, could account for most of the increases in calcium uptake rate observed in homogenates of muscles from the salbutamol-treated animals and could partially account for the changes in half-relaxation rates and other twitch times.3. Changes in the levels of SERCAla, SERCA2a and phospholamban protein did not always follow changes in the levels of their corresponding mRNAs. Divergence depended upon the SERCA isoform and muscle. The muscles studied were latissimus dorsi and vastus intermedius. 4. Salbutamol did not change the level of myosin heavy chain (HC)-I isoforms in either muscle, suggesting that it did not increase the proportion of slow-twitch fibres in these muscles. It did increase the level of HC-IIx and decrease the level of HC-IIa isoforms in the latissimus dorsi. Salbutamol did not produce these effects in the vastus intermedius. It is of particular interest that salbutamol changed the relative levels of SERCA proteins in the latissimus dorsi muscle without producing significant changes in the level of HC-I isoform.

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Section: Methodsmentioning

confidence: 99%

“…After blocking with 5 % non-fat dry milk, the transblotted proteins were exposed to specific monoclonal antibodies followed by horseradish peroxidase-labelled secondary antibodies. (Hu et al 1995 …”

Section: Sds-page and Western Blotsmentioning

confidence: 99%

Salbutamol changes the molecular and mechanical properties of canine skeletal muscle.

Zhang

Wang

et al. 1996

The Journal of Physiology

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“…In the time-dependent process of fast-to-slow fiber type transition, myofibrillar and Ca 2ϩ regulatory protein isoforms are converted from fast-twitch isoforms to their slow-twitch isoform counterparts. In this process the SERCA1⅐SLN complex which is regulated through both K Ca and V max effects is replaced by a SERCA2a⅐PLN complex with powerful K Ca regulation but no V max regulation (46,47).…”

Section: Role Of Sln As a Regulator Of Serca1 Function-hek-293mentioning

confidence: 99%

Sarcolipin Regulates the Activity of SERCA1, the Fast-twitch Skeletal Muscle Sarcoplasmic Reticulum Ca2+-ATPase

Odermatt

Becker

Khanna

et al. 1998

Journal of Biological Chemistry

213

291

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The 31-amino acid proteolipid, sarcolipin (SLN), is associated with the fast-twitch skeletal muscle sarcoplasmic reticulum Ca 2؉ -ATPase (SERCA1). Constructs of human and rabbit SLN and of rabbit SLN with the FLAG epitope at its N terminus (NF-SLN) or its C terminus (SLN-FC) were coexpressed with SERCA1 in HEK-293 T-cells. Immunohistochemistry was used to demonstrate colocalization of NF-SLN and SERCA1 in the endoplasmic reticulum membrane and to demonstrate the cytosolic orientation of the N terminus of SLN. Coexpression of native rabbit SLN or NF-SLN with SERCA1 decreased the apparent affinity of SERCA1 for Ca 2؉ but stimulated maximal Ca 2؉ uptake rates (V max ). The N terminus of SLN is not well conserved among species, and the addition of an N-terminal FLAG epitope did not alter SLN function. Anti-FLAG antibody reversed both the inhibition of Ca 2؉ uptake by NF-SLN at low Ca 2؉ concentrations and the stimulatory effect of NF-SLN on V max . Addition of the FLAG epitope to the highly conserved C terminus decreased the apparent affinity of SERCA1 for Ca 2؉ relative to native SLN and decreased V max significantly. Mutations in the C-terminal domain showed that this sequence is critical for SLN function. Mutational analysis of the transmembrane helix, together with the additive regulatory effects of coexpression of both SLN and phospholamban (PLN) with SERCA1, provided evidence for different mechanisms of interaction of SLN and PLN with SERCA molecules. Ca 2؉ uptake rates in sarcoplasmic reticulum vesicles, isolated from rabbit fast-twitch muscle (tibialis anterior) subjected to chronic low frequency stimulation, were reduced by approximately 40% in 3-and 4-day stimulated muscle, with a marginal increase in apparent affinity of SERCA1 for Ca 2؉ . SERCA1 mRNA and protein levels were unaltered after stimulation. In contrast, SLN mRNA was decreased by 15%, and SLN protein was reduced by 40%. Reduced SLN expression could explain the decrease in SERCA1 activity observed in these muscles and might represent an early functional adaptation to chronic low frequency stimulation.

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“…& p . 2 : Total RNA was extracted from 1 g of frozen muscle from the same animals studied by Hu et al [2]. The levels of SERCA1, SERCA2 and phospholamban presented in that report are presented here as well to facilitate the comparison of the MyoD and myogenin mRNA levels to these transcript levels.…”

Section: Methodsmentioning

confidence: 99%

“…The MyoD and myogenin levels are presented as ratios to α-actin levels. The MyoD and myogenin measurements were made on the same muscles in which SERCA1, SERCA2 and phospholamban mRNAs were measured and previously reported by Hu et al [2]. Statistical Methods.…”

Section: Methodsmentioning

confidence: 99%

Correlations between MyoD, myogenin, SERCA1, SERCA2 and phospholamban transcripts during transformation of type-II to type-I skeletal muscle fibers

Zhang

Wright

et al. 1997

Pfl�gers Archiv European Journal of Physiology

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Canine latissimus dorsi, composed predominantly of fast-twitch muscle fibers, were subjected to chronic 1 Hz neuromuscular stimulation for periods up to 42 days to induce changes in gene expression. This produced down regulation of SERCA1 (fast-twitch isoform of sarco(endo)plasmic reticulum Ca2+-ATPase), a gene product of fast-twitch muscle, and up regulation fo SERCA2 (slow-twitch isoform of sarco(endo)plasmic reticulum Ca2+-ATPase) and phospholamban, products of genes expressed by slow-twitch muscles. To assess the involvement of MyoD and myogenin in the regulation of the expression of these genes their levels were measured during the stimulation period. The prompt, at 7 days, fall in SERCA1 mRNA preceded the fall in MyoD by about 7 days, suggesting that the decline in MyoD was not causally related to the decline in SERCA1. The prompt rise in SERCA2 mRNA at 7 days preceded the rise in myogenin by 14 days. The rise in myogenin at 21 days did correlate with the similar rise in phospholamban mRNA.

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Transcriptional Regulation of Phospholamban Gene and Translational Regulation of SERCA2 Gene Produces Coordinate Expression of These Two Sarcoplasmic Reticulum Proteins during Skeletal Muscle Phenotype Switching

Cited by 42 publications

References 18 publications

Salbutamol changes the molecular and mechanical properties of canine skeletal muscle.

Salbutamol changes the molecular and mechanical properties of canine skeletal muscle.

Sarcolipin Regulates the Activity of SERCA1, the Fast-twitch Skeletal Muscle Sarcoplasmic Reticulum Ca2+-ATPase

Correlations between MyoD, myogenin, SERCA1, SERCA2 and phospholamban transcripts during transformation of type-II to type-I skeletal muscle fibers

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