Enzyme changes in neonatal skeletal muscle: effect of thyroid deficiency

Baldwin, K. M.; Hooker, Antony M.; Campbell, Patrick; Lewis, Richard

doi:10.1152/ajpcell.1978.235.3.c97

Cited by 1,106 publications

(20 citation statements)

References 31 publications

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“…However, in less mature species such as the pig and rabbit, H 4 represents the greater part of LDH isozymes of foetal skeletal muscle at birth [13,15] [19], rabbit [11] and sheep [10] [5], guinea pigs [7] and rabbits [11].…”

Section: Discussionmentioning

confidence: 99%

Comparison of foetal metabolic differentiation in three cattle muscles

Gagnière¹,

Picard²,

Jurie³

et al. 1999

Reprod. Nutr. Dev.

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Section: Discussionmentioning

confidence: 99%

Comparison of foetal metabolic differentiation in three cattle muscles

Gagnière¹,

Picard²,

Jurie³

et al. 1999

Reprod. Nutr. Dev.

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“…cytochrome oxidase-1, -hydroxyacyl CoA dehydrogenase, lactate dehydrogenase, malate dehydrogenase and phosphofructokinase) (Baldwin et al, 1978;Garry et al, 1996;Kelly et al, 1991;Kim et al, 1995;Yan et al, 2001). The coexpression of these sets of genes defines the oxidative fiber phenotype of fast and slow myofibers, which becomes evident within the first 10 days of postnatal life (Garry et al, 1996).…”

Section: Myoglobin Genomic Organization and Gene Structurementioning

confidence: 99%

Regulation of myoglobin expression

Kanatous

Mammen

2010

Journal of Experimental Biology

105

101

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SUMMARY Myoglobin is a well-characterized, cytoplasmic hemoprotein that is expressed primarily in cardiomyocytes and oxidative skeletal muscle fibers. However, recent studies also suggest low-level myoglobin expression in various non-muscle tissues. Prior studies incorporating molecular, pharmacological, physiological and transgenic technologies have demonstrated that myoglobin is an essential oxygen-storage hemoprotein capable of facilitating oxygen transport and modulating nitric oxide homeostasis within cardiac and skeletal myocytes. Concomitant with these studies, scientific investigations into the transcriptional regulation of myoglobin expression have been undertaken. These studies have indicated that activation of key transcription factors (MEF2, NFAT and Sp1) and co-activators (PGC-1α) by locomotor activity, differential intracellular calcium fluxes and low intracellular oxygen tension collectively regulate myoglobin expression. Future studies focused on tissue-specific transcriptional regulatory pathways and post-translational modifications governing myoglobin expression will need to be undertaken. Finally, further studies investigating the modulation of myoglobin expression under various myopathic processes may identify myoglobin as a novel therapeutic target for the treatment of various cardiac and skeletal myopathies.

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“…At birth, muscle glycogen and triacylglycerol content are similar to those seen in the adult muscle (Colling-Saltin, 1978b (Colling-Saltin, 1978b (Novak et al, 1972;Baldwin et al, 1978 ;Glatz and Veerkamp, 1982) and least in cardiac muscle (Baldwin, Cooke and Cheadle, 1977 ;Glatz and Veerkamp, 1982).…”

Section: Introductionmentioning

confidence: 61%