The supramolecular organisation of fibrillin-rich microfibrils determines the mechanical properties of bovine zonular filaments.
J Exp Biol
; 202(Pt 21): 3011-20, 1999 Nov.
Article
em En
| MEDLINE
| ID: mdl-10518482
ABSTRACT
The zonular filaments from the eyes of cows are rich in microfibrils containing fibrillin. Tensile tests, stress-relaxation tests and X-ray diffraction studies were used to study the relationship between the mechanical behaviour of zonular filaments and the molecular packing and structure of the fibrillin-rich microfibrils. Zonular filaments show a non-linear (J-shaped) stress-strain curve and appreciable stress-relaxation. It is proposed that the non-linear properties are due to local variations in waviness in the microfibrils or assemblies of microfibrils, which straighten out and become more regularly aligned with strain. Previous and current X-ray diffraction results consistently show a partial ordering of microfibrils in zonular filaments into staggered aggregates which become more ordered and laterally aligned on stretching. Although the removal and re-addition of Ca(2+) is known to change the molecular structure of fibrillin, no effect was observed on the tensile properties of the zonular filaments. It is hypothesised that strain-induced deformation in the supramolecular aggregate packing may not be Ca(2+)-sensitive but could dominate the mechanical behaviour of microfibrillar arrays in zonular filaments.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Bovinos
/
Microfibrilas
/
Olho
/
Proteínas dos Microfilamentos
Limite:
Animals
Idioma:
En
Revista:
J Exp Biol
Ano de publicação:
1999
Tipo de documento:
Article