Linked Life Data

2750893

Source:http://linkedlifedata.com/resource/pubmed/id/2750893

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1 Pt 1
pubmed:dateCreated
1989-8-11
pubmed:abstractText
The effect of exercise on the rate of total and myofibrillar protein degradation was determined by measuring the rate of release of tyrosine and 3-methylhistidine, respectively, from isolated rat soleus muscle strips after exercise. The rate of tyrosine release was 30-50% greater from the muscles of the exercised rats, whereas the rate of 3-methylhistidine release was unchanged. Thus the exercise-induced increase in the rate of protein degradation is due to increased breakdown of nonmyofibrillar proteins. The rate of protein degradation increases as a function of exercise duration and rapidly returns to the preexercise level during recovery. The exercise-induced increase in the rate of protein degradation is not inhibited by chloroquine. Together these observations suggest that the increase in the rate of protein degradation observed immediately after exercise is due to the breakdown of nonmyofibrillar proteins and occurs via the nonlysosomal pathway of protein degradation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0002-9513
pubmed:author
pubmed:issnType
Print
pubmed:volume
257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
E1-5
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Total and myofibrillar protein degradation in isolated soleus muscles after exercise.
pubmed:affiliation
Department of Biochemistry, School of Medicine, East Carolina University, Greenville, North Carolina 27858.
pubmed:publicationType
Journal Article