title: Aquaporin in Chondrosia reniformis Nardo, 1847 and Its Possible Role in the Interaction Between Cells and Engulfed Siliceous Particles.
abstract: The sponge Chondrosia reniformis selectively engulfs siliceous particles that, when in crystalline form, become quickly dissolved in its ectosome. The molecular mechanism, identity, and physiological significance of the cells involved in this process are not completely understood. In the present study, we applied light and electronic microscopic techniques to show how the quartz particles in C. reniformis are enveloped through collagen fibers and host cells near the surface of these organisms. As various aquaporins from bacteria, animals, and plants bidirectionally conduct metalloids-including silicon ions--through the cell membrane, the presence and potential involvement of aquaporins in quartz dissolution in C. reniformis have been investigated. An aquaporin-like transcript (CrAQP) was isolated according to the transcriptome sequencing results in C. reniformis The full-length CrAQP cDNA is 907 nucleotides long, with a 795-base pair (bp), open reading frame encoding a protein of 265 amino acids, a 29-bp, 5'-non-coding region, and a 83-bp, 3'-untranslated region. The Bayesian phylogenetic inference suggests that CrAqp is closely related to the Aqp8L grade, which is also implicated in H2O2 transport. Quantification of CrAQP mRNA through qPCR indicated that the transcript level was higher in the ectosome than in the choanosome. Immunofluorescence of a mammalian AQP8 in C. reniformis showed positivity in some cells near the quartz particles, a finding that may support the initial hypothesis of the potential involvement of CrAQP in quartz erosion. However, the features of the primary structure of this protein offer a new viewpoint about the functional role of these molecules in this process: that CrAQP may be involved in the permeation of H2O2 released during silica erosion.
authors.affiliation: Department of Earth, Environmental and Life Science (DISTAV), University of Genoa, Corso Europa 26, 16132, Genoa, Italy; marina.pozzolini@unige.it.
authors.forename: Marina
authors.initials: M
authors.lastname: Pozzolini
authors.affiliation: Department of Earth, Environmental and Life Science (DISTAV), University of Genoa, Corso Europa 26, 16132, Genoa, Italy;
authors.forename: Sara
authors.initials: S
authors.lastname: Ferrando
authors.affiliation: Department of Earth, Environmental and Life Science (DISTAV), University of Genoa, Corso Europa 26, 16132, Genoa, Italy;
authors.forename: Lorenzo
authors.initials: L
authors.lastname: Gallus
authors.affiliation: Institute of Marine Sciences (ISMAR) - CNR, Via De Marini 6, I-16149, Genoa, Italy; and.
authors.forename: Chiara
authors.initials: C
authors.lastname: Gambardella
authors.affiliation: Institute for Sustainable Plant Protection (IPSP, Turin Unit) - CNR, V. le P. A. Mattioli 25, I-10125, Turin, Italy.
authors.forename: Stefano
authors.initials: S
authors.lastname: Ghignone
authors.affiliation: Department of Earth, Environmental and Life Science (DISTAV), University of Genoa, Corso Europa 26, 16132, Genoa, Italy;
authors.forename: Marco
authors.initials: M
authors.lastname: Giovine
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D020346:Aquaporins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D001483:Base Sequence; D001499:Bayes Theorem; D018076:DNA, Complementary; D006861:Hydrogen Peroxide / Q000378:metabolism; D010802:Phylogeny; D011161:Porifera / Q000145:classification / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure*
chemical_list: D020346:Aquaporins; D018076:DNA, Complementary; D006861:Hydrogen Peroxide