PMID: 26338867Sep 5, 2015Paper

Involvement of aquaporin channels in water extrusion from biosilica during maturation of sponge siliceous spicules

The Biological Bulletin
Xiaohong Wang, Werner E G Müller

Abstract

Aquaporins are a family of small, pore-forming, integral cell membrane proteins. This ancient protein family functions as water channels and is found in all kingdoms (including archaea, eubacteria, fungi, plants, and animals). We discovered that in sponges aquaporin plays a novel role during the maturation of spicules, their skeletal elements. Spicules are synthesized enzymatically via silicatein following a polycondensation reaction. During this process, a 1:1 stoichiometric release of water per one Si-O-Si bond formed is produced. The product of silicatein, biosilica, is a fluffy, soft material that must be hardened in order to function as a solid rod. Using the model of the demosponge species Suberites domuncula Olivi, 1792, which expresses aquaporin, cDNA was cloned and the protein was heterologously expressed. The sponge aquaporin is grouped with the type 8 aquaporins. The function of the sponge aquaporin can be blocked by Mn-sulfate (MnSO4) and mercury chloride (HgCl2). Microscopic and functional studies suggest that aquaporin is involved in removal of the reaction water at the site where siliceous spicules are formed. Another molecule that is likely to be involved in biosilica maturation is the mucin/nidogen-like polypep...Continue Reading

Citations

Nov 18, 2018·Marine Biotechnology·P R Gabbai-ArmelinR N Granito
Sep 6, 2019·Journal of Comparative Physiology. B, Biochemical, Systemic, and Environmental Physiology·Kamila FoguesattoMarta Marques Souza

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