Academic literature on the topic 'Alpha-skeletal actin'
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Journal articles on the topic "Alpha-skeletal actin"
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Muscat, G. E., T. A. Gustafson, and L. Kedes. "A common factor regulates skeletal and cardiac alpha-actin gene transcription in muscle." Molecular and Cellular Biology 8, no. 10 (October 1988): 4120–33. http://dx.doi.org/10.1128/mcb.8.10.4120-4133.1988.
Full textAbstract:
The skeletal and cardiac alpha-actin genes are coexpressed in muscle development but exhibit distinctive tissue-specific patterns of expression. We used an in vivo competition assay and an in vitro electrophoretic mobility shift assay to demonstrate that both genes interact with a common trans-acting factor(s). However, there was at least one gene-specific cis-acting sequence in the skeletal alpha-actin gene that interacted with a trans-acting factor which was not rate limiting in the expression of the cardiac alpha-actin gene. The common factor(s) interacted with several cis-acting regions that corresponded to sequences that are required for the transcriptional modulation of these sarcomeric alpha-actin genes in muscle cells. These regulatory regions contained the sequence motif CC(A + T-rich)6GG, which is known as a CArG box. Results of in vivo competition assays demonstrated that the factor(s) bound by the skeletal alpha-actin gene is also essential for the maximal activity of the cardiac alpha-actin, simian virus 40 (SV40), alpha 2(I)-collagen, and the beta-actin promoters in muscle cells. In contrast, fibroblastic cells contained functionally distinct transcription factor(s) that were used by the SV40 enhancer but that did not interact with the sarcomeric alpha-actin cis-acting sequences. The existence of functionally different factors in these cell types may explain the myogenic specificity of these sarcomeric alpha-actin genes. Results of in vitro studies suggested that both the sarcomeric alpha-actin genes interact with the CArG box-binding factor CBF and that the skeletal alpha-actin promoter contains multiple CBF-binding sites. In contrast, CBF did not interact in vitro with a classical CAAT box, the SV40 enhancer, or a linker scanner mutation of an alpha-actin CArG box. Furthermore, methylation interference and DNase I footprinting assays demonstrated the precise sites of interaction of CBF with three CArG motifs at positions -98, -179, and -225 in the human skeletal alpha-actin gene.
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Muscat, G. E., T. A. Gustafson, and L. Kedes. "A common factor regulates skeletal and cardiac alpha-actin gene transcription in muscle." Molecular and Cellular Biology 8, no. 10 (October 1988): 4120–33. http://dx.doi.org/10.1128/mcb.8.10.4120.
Full textAbstract:
The skeletal and cardiac alpha-actin genes are coexpressed in muscle development but exhibit distinctive tissue-specific patterns of expression. We used an in vivo competition assay and an in vitro electrophoretic mobility shift assay to demonstrate that both genes interact with a common trans-acting factor(s). However, there was at least one gene-specific cis-acting sequence in the skeletal alpha-actin gene that interacted with a trans-acting factor which was not rate limiting in the expression of the cardiac alpha-actin gene. The common factor(s) interacted with several cis-acting regions that corresponded to sequences that are required for the transcriptional modulation of these sarcomeric alpha-actin genes in muscle cells. These regulatory regions contained the sequence motif CC(A + T-rich)6GG, which is known as a CArG box. Results of in vivo competition assays demonstrated that the factor(s) bound by the skeletal alpha-actin gene is also essential for the maximal activity of the cardiac alpha-actin, simian virus 40 (SV40), alpha 2(I)-collagen, and the beta-actin promoters in muscle cells. In contrast, fibroblastic cells contained functionally distinct transcription factor(s) that were used by the SV40 enhancer but that did not interact with the sarcomeric alpha-actin cis-acting sequences. The existence of functionally different factors in these cell types may explain the myogenic specificity of these sarcomeric alpha-actin genes. Results of in vitro studies suggested that both the sarcomeric alpha-actin genes interact with the CArG box-binding factor CBF and that the skeletal alpha-actin promoter contains multiple CBF-binding sites. In contrast, CBF did not interact in vitro with a classical CAAT box, the SV40 enhancer, or a linker scanner mutation of an alpha-actin CArG box. Furthermore, methylation interference and DNase I footprinting assays demonstrated the precise sites of interaction of CBF with three CArG motifs at positions -98, -179, and -225 in the human skeletal alpha-actin gene.
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Lyons, G. E., M. E. Buckingham, and H. G. Mannherz. "alpha-Actin proteins and gene transcripts are colocalized in embryonic mouse muscle." Development 111, no. 2 (February 1, 1991): 451–54. http://dx.doi.org/10.1242/dev.111.2.451.
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The alpha-actins are among the earliest muscle-specific mRNAs to appear in developing cardiac and skeletal muscle. To determine if there is coexpression of the alpha-actin proteins at early stages of myogenesis, we have used an alpha-actin-specific polyclonal antibody and in situ hybridization with specific cRNA probes to cardiac and skeletal alpha-actin transcripts on serial slides of mouse embryo sections. As soon as we can detect alpha-actin mRNAs in embryonic striated muscle, we also detect the protein suggesting that alpha-actin transcripts are translated very rapidly after transcription during myogenesis. In skeletal muscle, this colocalization of alpha-actin mRNA and protein was observed both in the myotomes of somites and in developing muscles in the limbs. In cardiac muscle, alpha-actin transcripts and proteins are abundantly expressed as soon as a cardiac tube forms.
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Gunning, P. W., V. Ferguson, K. J. Brennan, and E. C. Hardeman. "Alpha-skeletal actin induces a subset of muscle genes independently of muscle differentiation and withdrawal from the cell cycle." Journal of Cell Science 114, no. 3 (February 1, 2001): 513–24. http://dx.doi.org/10.1242/jcs.114.3.513.
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Muscle differentiation is characterized by the induction of genes encoding contractile structural proteins and the repression of nonmuscle isoforms from these gene families. We have examined the importance of this regulated order of gene expression by expressing the two sarcomeric muscle actins characteristic of the differentiated state, i.e. alpha-skeletal and alpha-cardiac actin, in C2 mouse myoblasts. Precocious accumulation of transcripts and proteins for a group of differentiation-specific genes was elicited by alpha-skeletal actin only: four muscle tropomyosins, two muscle actins, desmin and MyoD. The nonmuscle isoforms of tropomyosin and actin characteristic of the undifferentiated state continued to be expressed, and no myosin heavy or light chain or troponin transcripts characteristic of muscle differentiation were induced. Stable transfectants displayed a substantial reduction in cell surface area and in the levels of nonmuscle tropomyosins and beta-actin, consistent with a relationship between the composition of the actin cytoskeleton and cell surface area. The transfectants displayed normal cell cycle progression. We propose that alpha-skeletal actin can activate a regulatory pathway linking a subset of muscle genes that operates independently of normal differentiation and withdrawal from the cell cycle.
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Ruzicka, D. L., and R. J. Schwartz. "Sequential activation of alpha-actin genes during avian cardiogenesis: vascular smooth muscle alpha-actin gene transcripts mark the onset of cardiomyocyte differentiation." Journal of Cell Biology 107, no. 6 (December 1, 1988): 2575–86. http://dx.doi.org/10.1083/jcb.107.6.2575.
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The expression of cytoplasmic beta-actin and cardiac, skeletal, and smooth muscle alpha-actins during early avian cardiogenesis was analyzed by in situ hybridization with mRNA-specific single-stranded DNA probes. The cytoplasmic beta-actin gene was ubiquitously expressed in the early chicken embryo. In contrast, the alpha-actin genes were sequentially activated in avian cardiac tissue during the early stages of heart tube formation. The accumulation of large quantities of smooth muscle alpha-actin transcripts in epimyocardial cells preceded the expression of the sarcomeric alpha-actin genes. The accumulation of skeletal alpha-actin mRNAs in the developing heart lagged behind that of cardiac alpha-actin by several embryonic stages. At Hamburger-Hamilton stage 12, the smooth muscle alpha-actin gene was selectively down-regulated in the heart such that only the conus, which subsequently participates in the formation of the vascular trunks, continued to express this gene. This modulation in smooth muscle alpha-actin gene expression correlated with the beginning of coexpression of sarcomeric alpha-actin transcripts in the epimyocardium and the onset of circulation in the embryo. The specific expression of the vascular smooth muscle alpha-actin gene marks the onset of differentiation of cardiac cells and represents the first demonstration of coexpression of both smooth muscle and striated alpha-actin genes within myogenic cells.
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Hayward, L. J., and R. J. Schwartz. "Sequential expression of chicken actin genes during myogenesis." Journal of Cell Biology 102, no. 4 (April 1, 1986): 1485–93. http://dx.doi.org/10.1083/jcb.102.4.1485.
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Embryonic muscle development permits the study of contractile protein gene regulation during cellular differentiation. To distinguish the appearance of particular actin mRNAs during chicken myogenesis, we have constructed DNA probes from the transcribed 3' noncoding region of the single-copy alpha-skeletal, alpha-cardiac, and beta-cytoplasmic actin genes. Hybridization experiments showed that at day 10 in ovo (stage 36), embryonic hindlimbs contain low levels of actin mRNA, predominantly consisting of the alpha-cardiac and beta-actin isotypes. However, by day 17 in ovo (stage 43), the amount of alpha-skeletal actin mRNA/microgram total RNA increased more than 30-fold and represented approximately 90% of the assayed actin mRNA. Concomitantly, alpha-cardiac and beta-actin mRNAs decreased by 30% and 70%, respectively, from the levels observed at day 10. In primary myoblast cultures, beta-actin mRNA increased sharply during the proliferative phase before fusion and steadily declined thereafter. alpha-Cardiac actin mRNA increased to levels 15-fold greater than alpha-skeletal actin mRNA in prefusion myoblasts (36 h), and remained at elevated levels. In contrast, the alpha-skeletal actin mRNA remained low until fusion had begun (48 h), increased 25-fold over the prefusion level by the completion of fusion, and then decreased at later times in culture. Thus, the sequential accumulation of sarcomeric alpha-actin mRNAs in culture mimics some of the events observed in embryonic limb development. However, maintenance of high levels of alpha-cardiac actin mRNA as well as the transient accumulation of appreciable alpha-skeletal actin mRNA suggests that myoblast cultures lack one or more essential components for phenotypic maturation.
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Hayward, L. J., Y. Y. Zhu, and R. J. Schwartz. "Cellular localization of muscle and nonmuscle actin mRNAs in chicken primary myogenic cultures: the induction of alpha-skeletal actin mRNA is regulated independently of alpha-cardiac actin gene expression." Journal of Cell Biology 106, no. 6 (June 1, 1988): 2077–86. http://dx.doi.org/10.1083/jcb.106.6.2077.
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Specific DNA fragments complementary to the 3' untranslated regions of the beta-, alpha-cardiac, and alpha-skeletal actin mRNAs were used as in situ hybridization probes to examine differential expression and distribution of these mRNAs in primary myogenic cultures. We demonstrated that prefusion bipolar-shaped cells derived from day 3 dissociated embryonic somites were equivalent to myoblasts derived from embryonic day 11-12 pectoral tissue with respect to the expression of the alpha-cardiac actin gene. Fibroblasts present in primary muscle cultures were not labeled by the alpha-cardiac actin gene probe. Since virtually all of the bipolar cells express alpha-cardiac actin mRNA before fusion, we suggest that the bipolar phenotype may distinguish a committed myogenic cell type. In contrast, alpha-skeletal actin mRNA accumulates only in multinucleated myotubes and appears to be regulated independently from the alpha-cardiac actin gene. Accumulation of alpha-skeletal but not alpha-cardiac actin mRNA can be blocked by growth in Ca2+-deficient medium which arrests myoblast fusion. Thus, the sequential appearance of alpha-cardiac and then alpha-skeletal actin mRNA may result from factors that arise during terminal differentiation. Finally, the beta-actin mRNA was located in both fibroblasts and myoblasts but diminished in content during myoblast fusion and was absent from differentiated myotubes. It appears that in primary myogenic cultures, an asynchronous stage-dependent induction of two different alpha-striated actin mRNA species occurs concomitant with the deinduction of the nonmuscle beta-actin gene.
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Sassoon, D. A., I. Garner, and M. Buckingham. "Transcripts of alpha-cardiac and alpha-skeletal actins are early markers for myogenesis in the mouse embryo." Development 104, no. 1 (September 1, 1988): 155–64. http://dx.doi.org/10.1242/dev.104.1.155.
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Among the first tissues to differentiate in the mammalian embryo are cardiac and subsequently skeletal striated muscle. We have developed specific cRNA probes corresponding to the 5′ noncoding regions of alpha-cardiac and alpha-skeletal actin mRNAs in order to investigate myogenesis in the mouse embryo. Transcripts coding for cardiac actin which is the major isoform of the adult heart can first be detected between 7.5 and 7.8 days p.c. in the developing heart and are observed in all somites as they are formed. In addition, alpha-skeletal actin transcripts are accumulated at much lower levels in cardiac tissue and newly formed somites; both heart and skeletal muscle show co-expression of this actin gene pair at all stages of development examined. The fact that cardiac actin transcripts can be observed in the myotomal portion of the somite prior to muscle fibre differentiation indicates that cardiac actin transcripts (and to a lesser extent skeletal actin transcripts) are markers not only of striated muscle tissue, but also of earlier stages of the myogenic programme in vivo.
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Hu, M. C., S. B. Sharp, and N. Davidson. "The complete sequence of the mouse skeletal alpha-actin gene reveals several conserved and inverted repeat sequences outside of the protein-coding region." Molecular and Cellular Biology 6, no. 1 (January 1986): 15–25. http://dx.doi.org/10.1128/mcb.6.1.15-25.1986.
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The complete nucleotide sequence of a genomic clone encoding the mouse skeletal alpha-actin gene has been determined. This single-copy gene codes for a protein identical in primary sequence to the rabbit skeletal alpha-actin. It has a large intron in the 5'-untranslated region 12 nucleotides upstream from the initiator ATG and five small introns in the coding region at codons specifying amino acids 41/42, 150, 204, 267, and 327/328. These intron positions are identical to those for the corresponding genes of chickens and rats. Similar to other skeletal alpha-actin genes, the nucleotide sequence codes for two amino acids, Met-Cys, preceding the known N-terminal Asp of the mature protein. Comparison of the nucleotide sequences of rat, mouse, chicken, and human skeletal muscle alpha-actin genes reveals conserved sequences (some not previously noted) outside of the protein-coding region. Furthermore, several inverted repeat sequences, partially within these conserved regions, have been identified. These sequences are not present in the vertebrate cytoskeletal beta-actin genes. The strong conservation of the inverted repeat sequences suggests that they may have a role in the tissue-specific expression of skeletal alpha-actin genes.
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Hu, M. C., S. B. Sharp, and N. Davidson. "The complete sequence of the mouse skeletal alpha-actin gene reveals several conserved and inverted repeat sequences outside of the protein-coding region." Molecular and Cellular Biology 6, no. 1 (January 1986): 15–25. http://dx.doi.org/10.1128/mcb.6.1.15.
Full textAbstract:
The complete nucleotide sequence of a genomic clone encoding the mouse skeletal alpha-actin gene has been determined. This single-copy gene codes for a protein identical in primary sequence to the rabbit skeletal alpha-actin. It has a large intron in the 5'-untranslated region 12 nucleotides upstream from the initiator ATG and five small introns in the coding region at codons specifying amino acids 41/42, 150, 204, 267, and 327/328. These intron positions are identical to those for the corresponding genes of chickens and rats. Similar to other skeletal alpha-actin genes, the nucleotide sequence codes for two amino acids, Met-Cys, preceding the known N-terminal Asp of the mature protein. Comparison of the nucleotide sequences of rat, mouse, chicken, and human skeletal muscle alpha-actin genes reveals conserved sequences (some not previously noted) outside of the protein-coding region. Furthermore, several inverted repeat sequences, partially within these conserved regions, have been identified. These sequences are not present in the vertebrate cytoskeletal beta-actin genes. The strong conservation of the inverted repeat sequences suggests that they may have a role in the tissue-specific expression of skeletal alpha-actin genes.
Dissertations / Theses on the topic "Alpha-skeletal actin"
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Best, Heather Annette. "Gene discovery and mechanism of disease in the myopathies." Thesis, The University of Sydney, 2018. http://hdl.handle.net/2123/18940.
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Congenital myopathy and muscular dystrophy are two groups of inherited muscle diseases characterised by muscle weakness, and sub-classified by hallmark pathological features within a skeletal muscle biopsy. In order to understand the pathogenesis of inherited muscle disorders, and develop or apply therapies based on mechanistic insight, one must elucidate deep knowledge of the associated gene, genetic variant and the function of the encoded protein. This thesis focuses on three aspects of gene discovery in the inherited myopathies: (1) Identification of a novel variant and phenotype for a known disease gene; (2) understanding the functional role of a recently identified disease gene in skeletal muscle biology and disease; and (3) discovering a novel disease gene for congenital myopathy. We identified the first recessive variant within ACTA1 (encoding α-skeletal actin) as the genetic cause of congenital muscular dystrophy with rigid spine. This case uniquely describes recessive ACTA1 variants where α-skeletal actin protein is expressed. The unique clinical and histological presentation expands the spectrum of ACTA1 disease, and will help guide clinical care and future genetic diagnoses. Our team identified LMOD3 (leiomodin-3) as a novel disease gene for severe nemaline myopathy (NM). KLHL40 (encoding kelch-like family member 40) is another disease gene for severe NM. A recent study suggests mouse Klhl40 protects mouse Lmod3 protein from proteasome-mediated degradation, with the mechanistic basis of KLHL40-NM resulting from secondary loss of LMOD3. We investigated the regulation of human LMODs by human KLHL40, and unexpectedly found evidence that disputes the central paradigm that KLHL40 protects LMOD3 from proteasome-mediated degradation. We identified PYROXD1 as a new genetic cause of early-onset congenital myopathy. We provide the first characterisation of PYROXD1 as a nuclear-cytoplasmic oxidoreductase and our discovery highlights oxidative distress as a core mechanistic pathway in the myopathies. We derived a mouse model of Pyroxd1 deficiency, determining that global loss of mouse Pyroxd1 is embryonic lethal. We subsequently developed a mouse model with skeletal muscle knock-out of Pyroxd1 – as a means to elucidate the role of PYROXD1 in biology and disease.
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Ravenscroft, Gianina. "A therapeutic approach for the skeletal muscle a-actin based congenital myopathies." University of Western Australia. School of Biomedical, Biomolecular and Chemical Sciences, 2009. http://theses.library.uwa.edu.au/adt-WU2010.0049.
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[Truncated abstract] Mutations in the skeletal muscle -actin gene (ACTA1) have been shown to be one cause of a broad group of muscle disorders all termed the congenital myopathies. Over 170 different mutations have now been identified across all 6 coding exons of ACTA1 in patients presenting with muscle weakness and any one or more of the following histopathological features: nemaline rods, intranuclear rods, fibre-type disproportion, excess of thin filaments and central cores. While the identification of the causative gene has been of great comfort for affected patients and their families, with pre-natal genetic testing becoming available, the ultimate aim is to develop a therapy for these disorders. Of the therapies currently being explored for the muscular dystrophies, up-regulation of an alternative gene seemed to be one of the most promising avenues for treatment of the ACTA1 diseases. Up-regulation of utrophin, the foetal homologue of dystrophin, has been shown to be a promising therapy for the treatment of Duchenne muscular dystrophy. The main aim of my research was to determine whether up-regulation of cardiac -actin, the predominant -actin expressed in foetal skeletal muscle and in the adult heart, could be used as a therapy for the ACTA1 diseases. A proof-of-concept experiment was performed whereby skeletal muscle -actin knock-out (KO) mice (all of which die by postnatal day 9) were crossed with transgenic mice over-expressing cardiac -actin (known as Coco mice) in postnatal skeletal muscle. ... While patients that are ACTA1 nulls have been identified in a number of mainly consanguineous populations, the majority of ACTA1 mutations result in dominant disease in which the mutant protein interferes with the function of the wild-type skeletal muscle -actin. Research described in this thesis also focuses on characterizing two transgenic mouse models of dominant ACTA1 disease at the ultra-structural, cellular and functional level; this is the first step towards a proof-of-concept experiment to determine whether cardiac -actin up-regulation can dilute out the pathogenesis of dominant ACTA1 disease. It has long been noted that patients with ACTA1 disease do not have ophthalmoplegia, even in the most-severely affected individuals. Protein analysis performed on extraocular muscle (EOM) biopsies obtained from humans, sheep and pigs showed that the EOMs co-express cardiac and skeletal muscle -actin, with cardiac -actin comprising 70 % of the striated -actin pool. Thus we propose that sparing of the EOMs in ACTA1 disease is at least in part due to cardiac -actin diluting out the pathogenesis associated with expression of the mutant skeletal muscle -actin. This finding provides further support for the hypothesis that dilution of mutant skeletal muscle -actin in dominant ACTA1 disease by up-regulation of cardiac -actin may be a viable therapy for this group of devastating muscle diseases. The research contained herein has advanced the understanding of the pathobiology of skeletal muscle -actin diseases and provides strong evidence in support of cardiac -actin up-regulation as a promising therapy for these diseases.
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Hashimoto, Nara Yumi. "Efeitos do treinamento físico por natação sobre o sistema cardiovascular e marcadores moleculares de hipertrofia cardíaca em ratas wistar." Universidade de São Paulo, 2007. http://www.teses.usp.br/teses/disponiveis/39/39132/tde-12122007-135154/.
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O treinamento por natação leva a uma sobrecarga de volume no coração, que induz a hipertrofia cardíaca (HC) excêntrica, com aumento da massa e do diâmetro cardíaco. Neste trabalho foram investigadas as adaptações no sistema cardiovascular e na expressão de genes relacionados à HC patológica, na gênese da HC por treinamento de natação. 42 ratas wistar foram divididas em grupos: sedentário controle (SC) treinado protocolo 1 (P1) e treinado protocolo 2 (P2). O treinamento de P1 foi de 1x60min/dia, 5x/semana, por 10 semanas. O de P2 foi igual ao P1 até a 8ª semana. Na 9ª semana 2x/dia e na 10ª semana 3x/dia. Os grupos treinados, em relação ao SC, apresentaram bradicardia de repouso, melhora no desempenho físico do teste máximo e do consumo máximo de oxigênio e HC, sem alterar a pressão arterial média e a expressão dos genes do fator natriurético atrial e da alfa actina esquelética. O grupo P2 apresentou aumento no diâmetro cardíaco e redução da expressão do gene da beta miosina de cadeia pesada. Este último resultado é contrário à literatura para a HC patológica, que mostra o aumento não só da expressão deste gene como a dos outros genes estudados. Os resultados de HC de P2 assemelham-se aos encontrados em estudos recentes com atletas de modalidades de maior componente aeróbio, sendo este um bom modelo para investigação dos mecanismos envolvidos na HC destes atletaSwimming training leads to a cardiac volume overload that induces excentric cardiac hypertrophy (CH) with an increase in cardiac mass and diameter. Cardiovascular system adaptations and expression of genes relatated with pathological CH were investigated in swimming training CH. We studied 42 wistar females, divided in sedentary control (SC) group, protocol 1 trained group (P1) and protocol 2 trained group (P2). The P1 training program was once a day for 5 times/week for 10 weeks. P2 was the same as P1 until 8th week. In 9th week it was twice a day and in 10th week 3 times a day. Trained groups, in contrast with SC, showed rest bradycardia, improvement in physical performance, maximum oxygen uptake and CH, with no alteration in the medium arterial pressure and in the expression of atrial natriuretic factor and skeletal alpha actin genes. Moreover, P2 showed an increase in cardiac diameter and decrease in the expression of beta myosin heavy chain gene. This expression result is different of patological CH literature wich shows an increase of this gene expression and also in the others genes we had investigated. P2 CH results were similar to those recently found in endurance-type athletes, sugesting this is a good model to investigate mechanisms involved in endurance-type athletes CH
Book chapters on the topic "Alpha-skeletal actin"
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North, Kathryn N., and Nigel G. Laing. "Skeletal Muscle Alpha-Actin Diseases." In Advances in Experimental Medicine and Biology, 15–27. New York, NY: Springer New York, 2008. http://dx.doi.org/10.1007/978-0-387-84847-1_2.
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