Fibrillin-rich microfibrils: an X-ray diffraction study of the fundamental axial periodicity.
Microfibrils are ubiquitous matrix polymers which are thought to provide elastic properties in all extracellular matrix structures. The major component of the elastic microfibrils is the protein fibrillin; its molecular structure is unknown. In electron microscopy, microfibrils appear as beaded structures exhibiting a variable periodicity, indicating that they may be elastomeric. The X-ray diffraction of fibrillin-rich microfibrils in the form of zonular filaments from bovine eyes exhibits meridional diffraction peaks indexing on a fundamental periodicity of 55 nm in the relaxed state. The application of a 40% extension produced a lengthening of the periodicity by 3% as judged by alteration of the D spacing of the principal peaks. This effect was shown to be reversible. Changes in the periodicity of the meridional reflections indicate changes in the fundamental structure of the microfilaments, but cannot account for all long range elastomeric properties of fibrillin-containing microfibrils.
Wess
T J
TJ
Department of Biological and Molecular Sciences, University of Stirling, UK. tjw3@stir.ac.uk
Purslow
P P
PP
Kielty
C M
CM
D008841:Actin Cytoskeleton / Q000737:chemistry / Q000648:ultrastructure*; D000818:Animals; D002417:Cattle; D002924:Ciliary Body / Q000737:chemistry / Q000648:ultrastructure*; D000071837:Fibrillins; D008840:Microfilament Proteins / Q000737:chemistry*; D008854:Microscopy, Electron; D014961:X-Ray Diffraction / Q000379:methods
D000071837:Fibrillins; D008840:Microfilament Proteins