The mouse myoglobin gene

Blanchetot, Alain; Price, Melanie; Jeffreys, Alec J.

doi:10.1111/j.1432-1033.1986.tb09909.x

Cited by 41 publications

(13 citation statements)

References 23 publications

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“…Teleost Mb is comprised of 146 amino acids (23), with an apparent molecular size of approximately 16 kDa. The more slowly migrating human Mb with a molecular size of 17.8 kDa contains 153 amino acids and is typical of mammalian Mbs (24,25). Heart ventricles of the notothenioid species contained a 0.9-kb mRNA (Fig.…”

Section: Resultsmentioning

confidence: 98%

Variable expression of myoglobin among the hemoglobinless Antarctic icefishes

Sidell

Vayda

Small

et al. 1997

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

113

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The important intracellular oxygen-binding protein, myoglobin (Mb), is thought to be absent from oxidative muscle tissues of the family of hemoglobinless Antarctic icefishes, Channichthyidae. Within this family of fishes, which is endemic to the Southern Ocean surrounding Antarctica, there exist 15 known species and 11 genera. To date, we have examined eight species of icefish (representing seven genera) using immunoblot analyses. Results indicate that Mb is present in heart ventricles from five of these species of icefish. Mb is absent from heart auricle and oxidative skeletal muscle of all species. We have identified a 0.9-kb mRNA in Mbexpressing species that hybridizes with a Mb cDNA probe from the closely related red-blooded Antarctic nototheniid fish, Notothenia coriiceps. In confirmation that the 0.9-kb mRNA encodes Mb, we report the full-length Mb cDNA sequence of the ocellated icefish, Chionodraco rastrospinosus. Of the eight icefish species examined, three lack Mb polypeptide in heart ventricle, although one of these expresses the Mb mRNA. All species of icefish retain the Mb gene in their genomic DNA. Based on phylogeny of the icefishes, loss of Mb expression has occurred independently at least three times and by at least two distinct molecular mechanisms during speciation of the family.

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Section: Resultsmentioning

confidence: 98%

Variable expression of myoglobin among the hemoglobinless Antarctic icefishes

Sidell

Vayda

Small

et al. 1997

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

113

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“…The murine aldolase A pM-derived mRNAs (M-mRNA)-specific probe corresponds to the M-specific exon of the mouse aldolase A gene (18). The myoglobin probe was synthesized by reverse transcription-polymerase chain reaction and corresponds to the third exon of the gene (27). MyHC-2B transcripts were detected using a 76-bp fragment of the 3Ј-untranslated region of the rat gene (28); in this case, hybridization was performed at 55°C (in these conditions, there is no cross-hybridization with other MyHC as shown by the absence of signal in soleus (see Fig.…”

Section: Methodsmentioning

confidence: 99%

Proximal Sequences of the Aldolase A Fast Muscle-specific Promoter Direct Nerve- and Activity-dependent Expression in Transgenic Mice

Spitz¹,

Vasconcelos²,

Châtelet³

et al. 1998

Journal of Biological Chemistry

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Muscle activity is known to modulate the muscle fiber phenotype. Changes in muscle activity (normal or experimentally induced) lead to modifications of the expression status of several muscle-specific genes. However, the transcription regulatory elements involved in the adaptative response are mainly unknown. The aldolase A muscle-specific promoter, pM, is expressed in adult fast twitch muscle with a preferential expression in fast glycolytic-2B fibers. Its activity is induced during postnatal muscle maturation, suggesting a role of nerve and/or muscle activity. Indeed, denervation of gastrocnemius in newborn mice prevented the activation of the promoter in this muscle, despite the nerve-independent formation of 2B fibers. Although the nerve was necessary for pM onset during development, denervating the gastrocnemius in adults had only mild effects on pM activity. By contrast, a transgene including the pM proximal regulatory sequences that are sufficient to reproduce the 2B fiber-specific expression of the endogenous promoter was shown to be highly sensitive to both neonatal and adult denervation. Transgenes containing muscle-specific pM proximal promoter elements were used to delineate the regulatory elements involved in this response to innervation and changes in the contractile activity pattern. Nerve-and activity-dependent elements could be localized in the 130-base pair-long proximal promoter region of the human aldolase A gene.

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“…Myoglobin, cytoglobin and hemoglobin are believed to have shared a common ancestral globin more than 500 million years ago (Burmester et al, 2002). The genomic structure of the myoglobin gene has been extensively studied in a variety of species, including the Grey seal (Halichoerus grypus), human (Homo sapiens), mouse (Mus musculus) and sperm whale (Physeter catodon) (Blanchetot et al, 1986;Weller et al, 1986;Wittenberg and Wittenberg, 1989). These studies have demonstrated a considerable homology among various species in regards to the genomic structure of the myoglobin gene.…”

Section: Myoglobin Genomic Organization and Gene Structurementioning

confidence: 99%

“…O 2 , NO, free radicals, etc.) (Blanchetot et al, 1986). expressed in smooth muscle cells, certain human epithelial cancers and in non-muscle tissues of certain species of fish (Cossins and Berenbrink, 2008;Cossins et al, 2009;Flonta et al, 2009;Fraser et al, 2006;Rayner et al, 2009;Roesner et al, 2006).…”

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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The mouse myoglobin gene

Cited by 41 publications

References 23 publications

Variable expression of myoglobin among the hemoglobinless Antarctic icefishes

Variable expression of myoglobin among the hemoglobinless Antarctic icefishes

Proximal Sequences of the Aldolase A Fast Muscle-specific Promoter Direct Nerve- and Activity-dependent Expression in Transgenic Mice

Regulation of myoglobin expression

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