Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Echinobase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Echinobase
ECB-ART-39276
Comp Biochem Physiol B Biochem Mol Biol 2004 Dec 01;1394:607-17. doi: 10.1016/j.cbpc.2004.07.008.
Show Gene links Show Anatomy links

Anti-adhesive glycoproteins in echinoderm mucus secretions.

Bavington CD , Lever R , Mulloy B , Grundy MM , Page CP , Richardson NV , McKenzie JD .


???displayArticle.abstract???
Marine invertebrates produce a large variety of mucus secretions which are rich in glycoproteins. As part of our studies of natural antifouling mechanisms, mucus secretions from the starfish Marthasterias glacialis and Porania pulvillus and the brittlestar Ophiocomina nigra have been used to characterise the structure and function of some of the glycoproteins present in these secretions. Mucus was collected from all three species and fractionated by size exclusion chromatography. A high molecular weight glycoprotein fraction was collected from each species. Monosaccharide analysis and FTIR demonstrated a composition consistent with a mucin-type glycoprotein. The mucin from M. glacialis and O. nigra inhibited in vitro bacterial adhesion in a dose-dependent manner. In contrast, the mucin from P. pulvillus promoted bacterial adhesion in a dose-dependent manner. All of the mucins inhibited the adhesion of human neutrophils to cultured human vascular endothelial cells (HUVECs) and had no anticoagulant activity. The mucins described here have adhesion-regulating functions that may have a role in the antifouling or feeding mechanisms of the organisms that produce them. These mucins may also be of therapeutic value through their ability to regulate human neutrophil adhesion or bacterial adhesion.

???displayArticle.pubmedLink??? 15581793
???displayArticle.link??? Comp Biochem Physiol B Biochem Mol Biol


Genes referenced: LOC115925415