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Elastic fibres

Cay M. Kielty1,*, Michael J. Sherratt2 and C. Adrian Shuttleworth2

1 School of Medicine, University of Manchester, Manchester M13 9PT, UK
2 School of Biological Sciences, University of Manchester, Manchester M13 9PT, UK



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  		Fig. 1. Transmission electron microscopy of fibrillin-rich microfibrils and elastic fibres. (A) Human ciliary zonular microfibrils in loose, roughly parallel arrays. (B) Lobster aorta microfibrils, showing periodic striations. (C) Deposition of microfibrils and elastin by cultured bovine nuchal ligament fibroblasts. (D) Close-up of elastic fibres forming in bovine nuchal ligament fibroblast cultures. (E) Internal elastic lamina (IEL) of murine aorta, with associated endothelial cell (EC) and smooth muscle cell (SMC).

 


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  		Fig. 2. Microfibril and elastic fibre formation. Fibrillin is assembled pericellularly into microfibrillar arrays that appear to undergo time-dependent maturation into beaded transglutaminase-crosslinked microfibrils. Mature microfibrils form parallel bundles that may be stabilised at inter-microfibrillar crosslinked regions. In elastic tissues, tropoelastin is deposited on microfibril bundles, and lysyl oxidase-derived crosslinks then stabilise the elastin core. Crosslinks catalysed by the actions of transglutaminase and lysyl oxidase are shown. Transglutaminase forms {gamma}-glutamyl-e-lysine isopeptide bonds within or between peptide chains. Lysyl oxidase catalyses the oxidative deamination of certain lysine residues in elastin and subsequent, probably spontaneous, reactions lead to the formation of bifunctional crosslinks (dehydrolysinonorleucine and allysine aldol), a trifunctional crosslink (dehydromerodesmosine), and two tetrafunctional crosslinks (desmosine and isodesmosine, shown here).

 


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  		Fig. 3. Tapping mode atomic force microscopy (TMAFM) of isolated fibrillin-rich microfibrils on mica. (A) 1 µmx1 µm scan of beaded microfibrils isolated from fetal bovine nuchal ligament. (B,C) 180 nmx80 nm extracted region of three beaded repeats (C shows height contour map). (D) 3D height contour profile of the three beaded repeat units.

 


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  		Fig. 4. Domain structures of fibrillin-1 and elastin, showing molecular interaction sites identified in vitro (see Molecular Interactions). (A) Fibrillin-1 has 47 cbEGF-like domains, interspersed with TB modules. A proline-rich region is towards the N-terminus. N-glycosylation sites are indicated. (B) Elastin contains alternating hydrophobic and crosslinking domains. The C-terminus has two cysteines and a negatively charged pocket.

 

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© The Company of Biologists Ltd 2002