Linked Life Data

10759599

Source:http://linkedlifedata.com/resource/pubmed/id/10759599

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2000-5-10
pubmed:abstractText
Myoglobin (Mb) is a large protein that reversibly binds oxygen in the muscle cell and is thought to be critical for O2 supply to the mitochondria during exercise. The role of Mb in aerobic function is evaluated based on the physical properties of Mb as an O2 carrier and experimental evidence of Mb function in vivo. This role depends on the reversible binding of O2 by Mb depending on PO2, which results in: (1) storage of O2; (2) buffering of PO2 in the cell to prevent mitochondrial anoxia; and (3) parallel diffusion of O2 (so-called, 'facilitated diffusion'). The storage role is well established in diving mammals and buffering of cell PO2 above anoxic levels is shown here by in vivo magnetic resonance spectroscopy (MRS). However, the quantitative role of Mb in 'facilitated' or parallel diffusion of O2 is controversial. Evidence in support of this role is from MRS analyses, which reveal rapid Mb desaturation with exercise, and from the proportionality of Mb content of a muscle to the O2 diffusion limitation. Recent experiments with myoglobin knockout mice demonstrating high levels of aerobic function in normal and myoglobin-free mice argue against a link between Mb and oxidative phosphorylation. Thus, the current evidence supports the role of Mb in the physical diffusion of O2; however, the unimpaired aerobic function of Mb knockout mice indicates that this role may not be critical to O2 supply in active muscle.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0001-6772
pubmed:author
pubmed:issnType
Print
pubmed:volume
168
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
623-34
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Deciphering the mysteries of myoglobin in striated muscle.
pubmed:affiliation
Department of Radiology, University of Washington Medical Center, Seattle, WA 98195-7115, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Review, Research Support, Non-U.S. Gov't