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Figures
- 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).
- 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 formsγ -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).
- Fig. 3.
Tapping mode atomic force microscopy (TMAFM) of isolated fibrillin-rich microfibrils on mica. (A) 1 μm×1 μm scan of beaded microfibrils isolated from fetal bovine nuchal ligament. (B,C) 180 nm×80 nm extracted region of three beaded repeats (C shows height contour map). (D) 3D height contour profile of the three beaded repeat units.
- Table 1.
Reported microfibril and elastic fibre associated molecules
Molecule Chromosome Location References Fibrillin-1 15q21.1 Microfibrils Pereira et al., 1993; Baldock et al., 2001 Fibrillin-2 5q23-q31 Microfibrils Zhang et al., 1994 Fibrillin-3 19p ? Microfibrils Nagase et al., 2001 MAGP-1 1pter — 1qter Microfibrils Brown-Augsberger et al., 1996 MAGP-2 12p13.1-p12.3 Some microfibrils Gibson et al., 1998 LTBP-1 2p12-q22 Some microfibrils Miyazono et al., 1988; Sinha et al., 1998 LTBP-2 14q22-q33 Microfibrils/elastic fibres Gibson et al., 1995; Bashir et al., 1996 LTBP-3 11q12 ? Yin et al., 1995 LTBP-4 19q13.1 ? Giltay et al., 1997 Decorin 12q13.2 Microfibrils Trask et al., 2000a Biglycan Xq28 Elastic fibre core Reinboth et al., 2001 Versican 5q12-q14 Some microfibrils Isogai et al., 2002 MFAP-1 15q15-q21 Some microfibrils Liu et al., 1997 MFAP-3 5q32-q32.2 Some microfibrils Abrams et al., 1995 MFAP-4 (MAGP-36) 17p11.2 Some microfibrils Lausen et al., 1999; Hirano et al., 2002 Tropoelastin 7q11.2 Elastic fibre core Mecham and Davis, 1994 Lysyl oxidase (LOX) 5q23.3-q31.2 Microfibrils/tropoelastin Csiszar, 2001 LOXL 8p21.3-p21.2 ? Borel et al., 2001 LOXL2 15q22 ? Csiszar, 2001 LOXL3 2p13 ? Csiszar, 2001 BigH3 (keratoepithelin) 5q31 Elastic fibre/collagen interface Gibson et al., 1997 Fibulin-1 22q13.3 Elastic fibre core Kostka et al., 2001 Fibulin-2 3p24-25 Elastin-microfibril interface Tsuda et al., 2001 Fibulin-5 14q32.1 Elastic fibre—cell interface Nakamura et al., 2002; Yanagisawa et al., 2002 Emilin-1 2p23 Elastin-microfibril interface Doliana et al., 1999 Emilin-2 18p11.3 Elastin-microfibril interface Doliana et al., 2001 Elastin-binding protein 3p21.33 Newly secreted tropoelastin Prody et al., 1998 Vitronectin 17q11 Some microfibrils Dählback et al., 1990 Amyloid Some microfibrils Dählback et al., 1990 Collagen VIII [α1(VIII)] 3q12-q13.1 Some elastic fibres Sadawa and Konomi, 1991 Collagen XVI [α1(XVI)] 1p34 Dermal microfibrils Grässel et al., 1999 Endostatin [α1(XVIII)] 21q22.3 Vascular elastic fibres Miosge et al., 1999 Collagen VI Some microfibrils Finnis and Gibson, 1997 [α1(VI) α2(VI)] 21q22.3 [α3(VI)] 2q37 - 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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