Abstract
The fibulins are a group of glycoproteins that function predominantly though not exclusively in the extracellular matrix (ECM). In common with the fibrillins and hemicentins, which are also ECM protein families, their basic characteristic is an FC (fibulin-type) unit at the protein C-terminal preceded by an array of adjoining cbEGF (Ca++ binding epidermal growth factor-like) modules of varying number. They may have up to four protein domains (N, I, II, III) and can be subdivided into two main subgroups (1 and 2) (Timpl et al., Nat Rev Mol Cell Biol 4(6):479–489, 2003). Subgroup 1, which contains fibulin-1 and fibulin-2, has the largest molecules (Table 9.1). Fibulin-1 can have up to three protein domains but fibulin-2 is unique in also containing a large N domain preceding domain I at the N terminus of the protein. Subgroup 2 contains fibulin-3, fibulin-4 and fibulin-5 and these have three domains, one of which is very small. These complete molecules are much smaller than either of those in subgroup 1. The new fibulins, fibulin-6 and fibulin-7 are only being characterized presently.
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Cooney, H.C., Gallagher, W.M. (2011). Fibulins and Their Role in the ECM. In: Mueller, M., Fusenig, N. (eds) Tumor-Associated Fibroblasts and their Matrix. The Tumor Microenvironment, vol 4. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-0659-0_9
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DOI: https://doi.org/10.1007/978-94-007-0659-0_9
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