A 5′ duplication of the alpha-cardiac actin gene in BALB/c mice is associated with abnormal levels of alpha-cardiac and alpha-skeletal actin mRNAs in adult cardiac tissue.

Garner, Ian; Minty, Adrian; Alonso, Serge; Barton, Paul J.R.; Buckingham, M

doi:10.1002/j.1460-2075.1986.tb04535.x

Cited by 72 publications

(42 citation statements)

References 67 publications

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“…Thus, even if ␥-SMA can substitute ␣-CAA, it cannot completely rescue the heart function. However, perfused hearts isolated from BALB/c mice, which naturally express high levels of ␣-SKA (Garner et al, 1986), show increased levels of contractility compared with other strains of mice (Hewett et al, 1994). Altogether, these observations support the assumption that very few amino acid differences between muscle actin isoforms can have major functional consequences.…”

Section: Introductionsupporting

confidence: 60%

Expression and function of α-smooth muscle actin during embryonic-stem-cell-derived cardiomyocyte differentiation

Clément

Stouffs

Bettiol

et al. 2007

Journal of Cell Science

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Three α-muscle actin isoforms are sequentially expressed during in vivo cardiac development. α-Smooth muscle actin is first and transiently expressed, followed by α-skeletal and finally α-cardiac actin. The significance of these transitions in actin gene expression during myogenesis remains to be determined. To understand whether actin isoforms have specific functions during cardiac development and cardiomyocyte contractility, we have hampered α-smooth muscle and α-skeletal actin expression and organization during embryonic stem cell differentiation towards cardiomyocyte. We show that the sequence of actin isoform expression displays similar pattern in the in vitro model and in mouse heart embryogenesis. Treatment with an interfering fusion peptide containing the N-terminal sequence of α-smooth muscle actin during a time window preceding spontaneous beating, prevents proper cardiac sarcomyogenesis, whereas α-skeletal actin-fusion peptide has no effect. Knockdown of α-smooth muscle actin in embryonic stem cells using RNA interference also affects cardiac differentiation. The application of both fusion peptides on beating embryoid bodies impairs frequency. These results suggest specific functional activities for actin isoforms in cardiogenesis and cardiomyocyte contractility.

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Section: Introductionsupporting

confidence: 60%

Expression and function of α-smooth muscle actin during embryonic-stem-cell-derived cardiomyocyte differentiation

Clément

Stouffs

Bettiol

et al. 2007

Journal of Cell Science

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“…In addition, the daughterless gene product, which appears to be a homolog of the mammalian El2 protein (Caudy et al 1988a, b), may be playing a role in cooperation with MyoD1 in these cells. The existence of both functional and positional relationships among the Spl, MyoD1, and SRF-related factor binding sites is supported strongly by the structural and sequence conservation within this region when the human (Minty and Kedes 1986) and mouse sequences (Garner et al 1986) are compared (Fig. 2B).…”

Section: Discussionmentioning

confidence: 88%

“…Both sense and antisense DNA strands were investigated and, as shown in Figure 4, A and B, the methylation of two guanine residues at positions -5 6 and -4 9 on the antisense strand and of a guanine at po- (Minty and Kedes 1986) and mouse HCA sequences (Garner et al 1986). Capitalized, shaded base pairs represent the location in the human sequence and the putative locations in the mouse sequence of the transcription regulatory factors SRF, Spl, and MyoD1.…”

Section: The Myod1 Protein Activates Transcription From the Hca Promomentioning

confidence: 99%

Muscle-specific expression of the cardiac alpha-actin gene requires MyoD1, CArG-box binding factor, and Sp1.

1990

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Expression of the human cardiac ~-actin gene (HCA) depends on the interactions of multiple transcriptional regulators with promoter elements. We report here that the tissue-specific expression of this promoter is determined by the simultaneous interaction of at least three specific protein-DNA complexes. The myogenic determinant gene MyoD1 activated the transcription of transfected HCA-CAT promoter constructs in nonmuscle cells, including CV-1 and HeLa cells. Gel mobility-shift and footprinting assays revealed that MyoD1 specifically interacted with a single consensus core sequence, CANNTG, at -50. Previously characterized sites interact with a protein identical with or related to the serum response factor (SRF) at -100 and Spl at -70. All three elements must be intact to support transcription in muscle cells: site-specific mutation within any one of these three elements eliminated transcriptional expression by the promoter. Furthermore, expression of the promoter in embryonic Drosophila melanogaster cells that lack MyoD1 andSpl is strictly dependent on all three sites remaining intact and on the presence of exogenously supplied Spl and MyoD1. These experiments suggest that the presence of three sequence-specific binding proteins, including MyoD1, and their intact target DNA sequences are minimal requirements for muscle-specific expression of the HCA gene.

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“…However, the adult human heart has more skeletal than cardiac ␣-actin mRNA (9). Though the preponderance of cardiac ␣-actin in the adult rodent heart is the norm, BALB͞c mice, which show a perturbation of the cardiac ␣-actin locus (10), contain almost equivalent amounts of skeletal and cardiac ␣-actins in their hearts (2).…”

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confidence: 99%

Rescue of cardiac α-actin-deficient mice by enteric smooth muscle γ-actin

Kumar

Crawford

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

176

166

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The muscle actins in higher vertebrates display highly conserved amino acid sequences, yet they show distinct expression patterns. Thus, cardiac ␣-actin, skeletal ␣-actin, vascular smooth muscle ␣-actin, and enteric smooth muscle ␥-actin comprise the major actins in their respective tissues. To assess the functional and developmental significance of cardiac ␣-actin, the murine (129͞SvJ) cardiac ␣-actin gene was disrupted by homologous recombination. The majority (Ϸ56%) of the mice lacking cardiac ␣-actin do not survive to term, and the remainder generally die within 2 weeks of birth. Increased expression of vascular smooth muscle and skeletal ␣-actins is observed in the hearts of newborn homozygous mutants and also heterozygotes but apparently is insufficient to maintain myofibrillar integrity in the homozygous mutants. Mice lacking cardiac ␣-actin can be rescued to adulthood by the ectopic expression of enteric smooth muscle ␥-actin using the cardiac ␣-myosin heavy chain promoter. However, the hearts of such rescued cardiac ␣-actin-deficient mice are extremely hypodynamic, considerably enlarged, and hypertrophied. Furthermore, the transgenically expressed enteric smooth muscle ␥-actin reduces cardiac contractility in wild-type and heterozygous mice. These results demonstrate that alterations in actin composition in the fetal and adult heart are associated with severe structural and functional perturbations.

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A 5′ duplication of the alpha-cardiac actin gene in BALB/c mice is associated with abnormal levels of alpha-cardiac and alpha-skeletal actin mRNAs in adult cardiac tissue.

Cited by 72 publications

References 67 publications

Expression and function of α-smooth muscle actin during embryonic-stem-cell-derived cardiomyocyte differentiation

Expression and function of α-smooth muscle actin during embryonic-stem-cell-derived cardiomyocyte differentiation

Muscle-specific expression of the cardiac alpha-actin gene requires MyoD1, CArG-box binding factor, and Sp1.

Rescue of cardiac α-actin-deficient mice by enteric smooth muscle γ-actin

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