Abstract
Hemoproteins are widely distributed among prokaryotes, unicellular eurokaryotes, 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.
Original language | English (US) |
---|---|
Pages (from-to) | 896-898 |
Number of pages | 3 |
Journal | Cellular and Molecular Life Sciences |
Volume | 57 |
Issue number | 6 |
DOIs | |
State | Published - Jan 1 2000 |
Keywords
- Heart
- Myoglobin
- Oxygen transport
- Skeletal muscle
- Transgenic mice