The presence of elastic fibres in the extracellular matrix (ECM) provi
des physiologically important elastic properties for many tissues. Unt
il recently, microfibrils, one component of the ECM, were thought prim
arily to serve as a scaffolding on which elastin is deposited during d
evelopment to form elaunin fibres [1]. The most prominent protein that
forms mammalian microfibrils is fibrillin. It is known that mutations
in the fibrillin gene cause a heterogenous connective tissue disease
called Marfan syndrome [2], so information on mechanical properties of
microfibrils or their role in tissue function would be useful. Microf
ibrils are also found in the ECM of some invertebrate tissues, and the
re is growing evidence that the protein forming the structure is homol
ogous to mammalian fibrillin [3, 4]. It has been shown that the microf
ibril-based arterial wall of the lobster has viscoelastic properties [
5], and we have now utilized this primitive artery to measure the modu
lus of elasticity of microfibrils. It is similar to that of the rubber
-like protein elastin.