Characterisation of hydra type IV collagen: Type IV collagen is essential for head regeneration and its expression is up-regulated upon exposure to glucose

doi:10.1074/jbc.M005871200

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Characterisation of hydra type IV collagen: Type IV collagen is essential for head regeneration and its expression is up-regulated upon exposure to glucose

Susan J. Fowler, Sheba Jose, Xiaoming Zhang, Rainer Deutzmann, Michael P. Sarras Jr, and Raymond P. Boot-Handford

School of Biological Sciences, University of Manchester, M13 9PT, Manchester

Corresponding Author: ray.boot-handford{at}man.ac.uk

Hydra vulgaris mesoglea is a primitive basement membrane that also exhibits some features of an interstitial matrix. We have characterised cDNAs that encode the full length hydra a1(IV) chain. The 5,169 bp transcript encodes a protein of 1,723 amino acids, including an interrupted 1,455 residue collagenous domain and a 228 residue carboxyl-terminal non-collagenous domain. N-terminal sequence analyses of collagen IV peptides suggest the molecule is homotrimeric. Denatured hydra type IV collagen protein occurs as dimers and higher order aggregates held together by non-reducible cross-links. Hydra collagen IV exhibits no functional evidence for the presence of a ?7S domain?. Type IV collagen is expressed by the ectoderm along the entire longitudinal axis of the animal, but is most intense at the base of the tentacles at the site of battery cell transdifferentiation. Antisense studies show that inhibition of collagen IV translation causes a blockage in head regeneration, indicating its importance in normal hydra development. Exposure of adult hydra to 15 mM glucose resulted in up-regulation of type IV collagen mRNA levels within 48 hours and significant thickening of the mesoglea within 14 days suggesting that basement membrane thickening seen in diabetes may be, in evolutionary terms, an ancient glucose-mediated response.

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