X-RAY DIFFRACTION STUDIES OF FIBRILLIN-RICH ICROFIBRILS

T.J.Wess,1 P.P. Purslow2 and C.M. Kielty3

1Department of Biological and Molecular Sciences, University of Stirling, Stirling FK9 4LA.
2The Royal Veterinary and Agricultural University, Rolighedsvej 30, 1958 Fredriksberg C Denmark.
3
School of Biological Sciences, 2.205 Stopford Building, University of Manchester, Manchester M13 9PT.

Keywords fibrillin-rich microfibrils, X-ray small angle scattering, diffraction

Microfibrils are ubiquitous fibrillin-rich polymers which are thought to provide long-range elasticity to extracellular matrices, including the zonular filaments of mammalian eyes. The microfibrils appear in electron microscopy as beaded structures several hundred nm in length with a fundamental bead periodicity of around 56nm. The possible basis for elasticity of the tissue is based on the reversible changes in the beaded periodicity. X-ray diffraction of hydrated bovine zonular filaments (at the Daresbury Synchrotron) demonstrated meridional diffraction peaks indexing on a fundamental periodicity of ~56nm[1]. The effect of stretching the tissue up to 50% of the rest length had little effect on the position of meridional Bragg reflections, indicating a static population of bead lengths. The effect of extension up to 100% causes a deterioration of the diffraction signal and a weak fundamental peak can be observed at 84nm[2]. A Ca2+ induced reversible change in the intensities of the meridional Bragg peaks indicated that supramolecular rearrangements occurred in response to altered concentrations of free Ca2+. In the presence of Ca2+, the dominant diffracting subspecies were microfibrils aligned in an axial 0.33 D stagger. The removal of Ca2+ caused an overall enhanced regularity in molecular spacing, and the contribution from microfibrils not involved in staggered arrays became more dominant[3]. Simulated diffraction profiles and analyses of the staggered arrays of isolated microfibrils formed in vitro in the presence of Ca2+ were used to interpret the effects of Ca2+. These observations indicate how Ca2+ could modulate the organisation of individual microfibrils and three-dimensional arrays in vivo. This data allows a mechanism for elasticity at the molecular level to be related to the macroscopic tissue elasticity. Under the usual conditions of extension in the eye, bead periodicity changes in a discrete population along fibrils facilitate elasticity. Molecular junctions of specifically staggered microfibrils maintain the integrity of the tissue and serve as anchors connecting the stretched microfibrils and allows the force to be transmitted through the tissue. the removal of Ca2+ is to enhance the regularity of the bead regions where stretching occurs and also allows the diffraction from this population to be observed.

  1. Wess T.J. Purslow P.P and Kielty C.M. (1997) Fibrillin rich microfibrils: an X-ray diffraction study of the fundamental axial periodicity. FEBS Lett. 413 424-428.
  2. Wess T.J. Kielty C.M. Purslow P.P. (1998) Calcium determines the supramolecular organisation of fibrillin rich microfibrils. J.Cell .Biol. 141 829-837.
  3. Wess T.J. Purslow P.P. and Kielty C.M. (1998) Fibrillin elasticity an X-ray diffraction study. In press J. Struct.Biol. May 1998