Characterization of Hydra type IV collagen: Type IV collagen is essential is essential for head regeneration and its expression is up-regulated upon exposure to glucose: 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, Raymond P. Boot-Handford

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Hydra vulgaris mesoglea is a primitive basement membrane that also exhibits some features of an interstitial matrix. We have characterized cDNAs that encode the full-length hydra α1(IV) chain. The 5169-base pair transcript encodes a protein of 1723 amino acids, including an interrupted 1455-residue collagenous domain and a 228-residue C-terminal noncollagenous 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 nonreducible cross-links. Hydra collagen IV exhibits no functional evidence for the presence of a 7 S 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 h 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.
    Original languageEnglish
    Pages (from-to)39589-39599
    Number of pages10
    JournalJournal of Biological Chemistry
    Volume275
    Issue number50
    DOIs
    Publication statusPublished - 15 Dec 2000

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