Life without myoglobin
Hemoproteins are widely distributed among prokaryotes, unicellular eukaryotes, plants and animals . Myoglobin, a cytoplasmic hemoprotein that is restricted to cardiomyocytes and oxidative skeletal myofibers in vertebrates, has been proposed to facilitate oxygen transport to the mitochondria . This c...
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| Published in | Cellular and molecular life sciences : CMLS Vol. 57; no. 6; pp. 896 - 898 |
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| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
Switzerland
Birkhäuser Verlag
01.06.2000
Springer Nature B.V |
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| Online Access | Get full text |
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| Abstract | Hemoproteins are widely distributed among prokaryotes, unicellular eukaryotes, plants and animals . Myoglobin, a cytoplasmic hemoprotein that is restricted to cardiomyocytes and oxidative skeletal myofibers in vertebrates, has been proposed to facilitate oxygen transport to the mitochondria . This cytoplasmic hemoprotein was the first protein to be subjected to definitive structural analysis and has been a subject of long-standing and ongoing interest to biologists . Recently, we utilized gene disruption technology to generate mice that are viable and fertile despite a complete absence of myoglobin . This unexpected result led us to reexamine existing paradigms regarding the function of myoglobin in striated muscle. |
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| AbstractList | Hemoproteins are widely distributed among prokaryotes, unicellular eukaryotes, plants and animals . Myoglobin, a cytoplasmic hemoprotein that is restricted to cardiomyocytes and oxidative skeletal myofibers in vertebrates, has been proposed to facilitate oxygen transport to the mitochondria . This cytoplasmic hemoprotein was the first protein to be subjected to definitive structural analysis and has been a subject of long-standing and ongoing interest to biologists . Recently, we utilized gene disruption technology to generate mice that are viable and fertile despite a complete absence of myoglobin . This unexpected result led us to reexamine existing paradigms regarding the function of myoglobin in striated muscle. Hemoproteins are widely distributed among prokaryotes, unicellular eukaryotes, plants and animals [1]. Myoglobin, a cytoplasmic hemoprotein that is restricted to cardiomyocytes and oxidative skeletal myofibers in vertebrates, has been proposed to facilitate oxygen transport to the mitochondria [1-3]. This cytoplasmic hemoprotein was the first protein to be subjected to definitive structural analysis and has been a subject of long-standing and ongoing interest to biologists [1-3]. Recently, we utilized gene disruption technology to generate mice that are viable and fertile despite a complete absence of myoglobin [4]. This unexpected result led us to reexamine existing paradigms regarding the function of myoglobin in striated muscle.Hemoproteins are widely distributed among prokaryotes, unicellular eukaryotes, plants and animals [1]. Myoglobin, a cytoplasmic hemoprotein that is restricted to cardiomyocytes and oxidative skeletal myofibers in vertebrates, has been proposed to facilitate oxygen transport to the mitochondria [1-3]. This cytoplasmic hemoprotein was the first protein to be subjected to definitive structural analysis and has been a subject of long-standing and ongoing interest to biologists [1-3]. Recently, we utilized gene disruption technology to generate mice that are viable and fertile despite a complete absence of myoglobin [4]. This unexpected result led us to reexamine existing paradigms regarding the function of myoglobin in striated muscle. Hemoproteins are widely distributed among prokaryotes, unicellular eukaryotes, plants and animals [1]. Myoglobin, a cytoplasmic hemoprotein that is restricted to cardiomyocytes and oxidative skeletal myofibers in vertebrates, has been proposed to facilitate oxygen transport to the mitochondria [1-3]. This cytoplasmic hemoprotein was the first protein to be subjected to definitive structural analysis and has been a subject of long-standing and ongoing interest to biologists [1-3]. Recently, we utilized gene disruption technology to generate mice that are viable and fertile despite a complete absence of myoglobin [4]. This unexpected result led us to reexamine existing paradigms regarding the function of myoglobin in striated muscle. |
| Author | Yan, Z Williams, R. S Meeson, A Garry, D. J |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/10950305$$D View this record in MEDLINE/PubMed |
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| Snippet | Hemoproteins are widely distributed among prokaryotes, unicellular eukaryotes, plants and animals . Myoglobin, a cytoplasmic hemoprotein that is restricted to... Hemoproteins are widely distributed among prokaryotes, unicellular eukaryotes, plants and animals [1]. Myoglobin, a cytoplasmic hemoprotein that is restricted... |
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| SubjectTerms | Animals Biological Transport Cardiomyocytes Eukaryotes eukaryotic cells Gene disruption Gene Expression Regulation gene targeting Mice Mice, Knockout mitochondria Molecular biology Muscle, Skeletal - metabolism Myocardium - metabolism myoglobin Myoglobin - deficiency Myoglobin - genetics Myoglobin - metabolism Myoglobins oxygen Oxygen - metabolism plants (botany) Prokaryotes prokaryotic cells Proteins Skeletal muscle striated muscle Structural analysis Vertebrates |
| Title | Life without myoglobin |
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