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Titolo:
The supramolecular organization of fibrillin-rich microfibrils
Autore:
Baldock, C; Koster, AJ; Ziese, U; Rock, MJ; Sherratt, MJ; Kadler, KE; Shuttleworth, CA; Kielty, CM;
Indirizzi:
Univ Manchester, Sch Biol Sci, Wellcome Trust Ctr Cell Matrix Res, Manchester M13 9PT, Lancs, England Univ Manchester Manchester Lancs England M13 9PT M13 9PT, Lancs, England Univ Manchester, Sch Med, Manchester M13 9PT, Lancs, England Univ Manchester Manchester Lancs England M13 9PT M13 9PT, Lancs, England Univ Utrecht, Dept Mol & Cell Biol, NL-3584 CH Utrecht, Netherlands Univ Utrecht Utrecht Netherlands NL-3584 CH 3584 CH Utrecht, Netherlands
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 5, volume: 152, anno: 2001,
pagine: 1045 - 1056
SICI:
0021-9525(20010305)152:5<1045:TSOOFM>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
CONNECTIVE-TISSUE MICROFIBRILS; SEA-CUCUMBER DERMIS; FACTOR-LIKE DOMAINS; MARFAN-SYNDROME; EXTRACELLULAR MICROFIBRILS; TERMINAL SEQUENCES; CALCIUM DETERMINES; ELASTIC TISSUES; VITREOUS-HUMOR; BINDING;
Keywords:
three-dimensional reconstruction; automated electron tomography; fibrillin microfibrils; molecular alignment; scanning transmission electron microscopy mass mapping;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Baldock, C Univ Manchester, Sch Biol Sci, Wellcome Trust Ctr Cell Matrix Res, 2-205 Stopford Bldg, Manchester M13 9PT, Lancs, England Univ Manchester2-205 Stopford Bldg Manchester Lancs England M13 9PT
Citazione:
C. Baldock et al., "The supramolecular organization of fibrillin-rich microfibrils", J CELL BIOL, 152(5), 2001, pp. 1045-1056

Abstract

We propose a new model for the alignment of fibrillin molecules within fibrillin microfibrils. Automated electron tomography was used to generate three-dimensional microfibril reconstructions to 18.6-Angstrom resolution, which revealed many new organizational details of untensioned microfibrils, including heart-shaped beads from which two arms emerge, and inter-bead diameter variation. Antibody epitope mapping of untensioned microfibrils revealed the juxtaposition of epitopes at the COOH terminus and near the proline-rich region, and of two internal epitopes that would be 42-nm apart in unfolded molecules, which infers intramolecular folding. Colloidal gold binds microfibrils in the absence of antibody. Comparison of colloidal gold and antibody binding sites in untensioned microfibrils and those extended in vitro, and immunofluorescence studies of fibrillin deposition in cell layers, indicate conformation changes and intramolecular folding. Mass mapping shows that, in solution, microfibrils with periodicities of <70 and >140 nm are stable, but periodicities of similar to 100 nm are rare. Microfibrils comprise two in-register filaments with a longitudinal symmetry axis, with eight fibrillin molecules in cross section. We present a model of fibrillin alignment that fits all the data and indicates that microfibril extensibility follows conformation-dependent maturation from an initial head-to-tail alignment to a stable approximately one-third staggered arrangement.

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Documento generato il 19/09/20 alle ore 07:37:27