Document Detail


Connective tissue metabolism in muscular dystrophy. Amino acid composition of native types I, III, IV and V collagen isolated from the gastrocnemius muscle of embryonic chickens with genetic muscular dystrophy.
MedLine Citation:
PMID:  4017536     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The amino acid composition data on types I, III, IV and V collagen isolated from embryonic dystrophic skeletal muscle strongly indicate that alterations in collagen synthesis occur in intramuscular connective tissue of developing muscles in embryonic dystrophic chickens. The changes observed in the amino acid composition of dystrophic collagen were: (a) a selective removal of polar amino acids and substitution with non-polar amino acids; (b) significant decreases in basic (lysine, hydroxylysine and arginine) and hydroxylated (4-hydroxyproline and hydroxylysine) amino acids; and (c) significant increases in the amounts of glycine, proline and alanine. The amino acid substitutions suggest a genetic alteration in the collagen synthesizing process and a change in its structure. The variations in amino acid composition of collagen from dystrophic chickens could give rise to a decrease in both inter- and intramolecular cross-linking, thus decreasing the stability and functionality of newly formed collagen fibrils. The differences associated with the dystrophic collagen reported in this study are probably due to the differences in primary structure in terms of amino acid sequence rather than post-translational modifications. The structural differences noted would also lead to an alteration of the role collagen plays in regulating the differentiation of developing muscles. The changes in amino acid structure strongly suggest that the 'collagen' formed by dystrophic chickens should be considered a collagen-like protein or 'collagenoid'.
Authors:
S J DeMichele; R G Brown; B W Krasin; P R Sweeny
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  Comparative biochemistry and physiology. B, Comparative biochemistry     Volume:  81     ISSN:  0305-0491     ISO Abbreviation:  Comp. Biochem. Physiol., B     Publication Date:  1985  
Date Detail:
Created Date:  1985-09-04     Completed Date:  1985-09-04     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2984730R     Medline TA:  Comp Biochem Physiol B     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  149-57     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / analysis
Animals
Chick Embryo
Collagen / isolation & purification*
Connective Tissue / metabolism*
Macromolecular Substances
Muscles / metabolism*
Muscular Dystrophy, Animal / genetics,  metabolism*
Reference Values
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Macromolecular Substances; 9007-34-5/Collagen

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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