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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1998-11-24
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pubmed:abstractText |
Collagen and elastin fibres are of major importance in providing the aorta with tensile strength and elasticity. The presence of cross-links in collagen and elastin is essential for the mechanical stability of collagen and elastin fibres. beta-aminopropionitrile (BAPN) reduces the formation of cross-links by inhibiting the enzyme lysyloxidase. Young rats were injected with BAPN to inhibit the formation of cross-links, and the changes in the biomechanical and biochemical properties of the thoracic aorta were studied. The biomechanical analyses of aortic samples from BAPN-treated rats showed a significantly increased diameter (1.64 +/-0.02 mm), a significantly reduced maximum load (1.08+/-0.08 N), and a significantly reduced maximum stiffness (3.34+/-0.10 N) compared with controls (1.57+/-0.02 mm, 1.55+/-0.04 N and 4.49 +/-0.14 N, respectively). No changes in the concentrations of collagen and elastin were found. The content of pyridinoline, a mature collagen cross-link, was significantly decreased by 49% in the BAPN-treated group compared with controls. No changes in the concentration of desmosine + isodesmosine, the major cross-links of elastin. were found. The present study shows that cross-links are essential in providing mechanical stability of the aorta. Even a partial inhibition of the cross-linking processes results in a destabilisation of the aortic wall with increased diameter and reduced strength and stiffness.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/Desmosine,
http://linkedlifedata.com/resource/pubmed/chemical/Elastin,
http://linkedlifedata.com/resource/pubmed/chemical/pyridinoline
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9150
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
140
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
135-45
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9733224-Aging,
pubmed-meshheading:9733224-Amino Acids,
pubmed-meshheading:9733224-Animals,
pubmed-meshheading:9733224-Aorta,
pubmed-meshheading:9733224-Collagen,
pubmed-meshheading:9733224-Desmosine,
pubmed-meshheading:9733224-Elasticity,
pubmed-meshheading:9733224-Elastin,
pubmed-meshheading:9733224-Female,
pubmed-meshheading:9733224-Rats,
pubmed-meshheading:9733224-Rats, Wistar,
pubmed-meshheading:9733224-Structure-Activity Relationship
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pubmed:year |
1998
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pubmed:articleTitle |
Inhibition of cross-links in collagen is associated with reduced stiffness of the aorta in young rats.
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pubmed:affiliation |
Department of Connective Tissue Biology, Institute of Anatomy, University of Aarhus, Denmark. mb@ana.au.dk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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