Evolution of Extracellular Matrix by Josephine C. Adams (auth.), Fred W. Keeley, Robert P. Mecham

By Josephine C. Adams (auth.), Fred W. Keeley, Robert P. Mecham (eds.)

The evolution of unmarried cells into multicellular organisms was once mediated, largely, through the extracellular matrix. The proteins and glycoconjugates that make up the extracellular matrix supply structural aid to mobile complexes, facilitate phone adhesion and migration, and impart mechanical homes which are very important for tissue functionality. each one classification of ECM macromolecule has advanced to include detailed houses which are outlined by means of conserved modules which are combined jointly to accomplish applicable functionality. This quantity offers a finished research of ways the key ECM elements developed over the years with the intention to fill their particular roles present in sleek organisms. the foremost concentration is at the structural matrix proteins, matricellular proteins, and extra advanced ECM constructions akin to basement membranes. Adhesive proteins and their receptors also are discussed.

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2010). This scenario introduced other aspects of the evolution of the Xlink domain. The Xlink domain functions with the aggrecan molecule as the interface with hyaluronan (HA) (Fig. 1b). The complex consisting of HA, link protein/ HAPLN1, and aggrecan provides tensile strength for cartilage to absorb shock and resist compression in the joint. Mutations in aggrecan or the link protein/ HAPLN1 cause severe defects in cartilage and result in dwarfism (Watanabe et al. 1994; Watanabe and Yamada 1999).

Cell Mol Life Sci 64:542–554 Bader BL, Smyth N, Nedbal S, Miosge N, Baranowsky A, Mokkapati S, Murshed M, Nischt R (2005) Compound genetic ablation of nidogen 1 and 2 causes basement membrane defects and perinatal lethality in mice. Mol Cell Biol 25:6846–6856 Beck K, Brodsky B (1998) Supercoiled protein motifs: the collagen triple-helix and the alphahelical coiled coil. J Struct Biol 122:17–29 Behrens DT, Villone D, Koch M, Brunner G, Sorokin L, Robenek H, Bruckner-Tuderman L, Bruckner P, Hansen U (2012) The epidermal basement membrane is a composite of separate laminin- or collagen IV-containing networks connected by aggregated perlecan, but not by nidogens.

Using this method, we identified 47 vertebrate genes created by domain shuffling. These genes possessed domain pairs conserved in all vertebrate species but were not found in any invertebrate genomes. We found that most of the domain shuffling events were likely due to exon shuffling, because most of the new domain pairs were split by intron(s) (Kawashima et al. 2009), and nice correlation was observed between exon and domain boundaries (Liu and Grigoriev 2004). Among the exons involved in domain shuffling, a number were split by phase 1 introns at both the 50 and 30 termini (exons of intron phase type 1-1), while 0-0 phase exons were abundant in all exons (Patthy 1999; Kawashima et al.

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