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Originally published as JHC exPRESS on May 18, 2006.
doi:10.1369/jhc.5A6903.2006
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Journal of Histochemistry and Cytochemistry
Volume 54 (9): 1031-1040, 2006
Copyright ©The Histochemical Society, Inc.

Histochemical and Electron Microscopic Analysis of Spiculogenesis in the Demosponge Suberites domuncula

Carsten Eckert, Heinz C. Schröder, David Brandt, Sanja Perovic-Ottstadt and Werner E.G. Müller

Museum für Naturkunde, Universität, Institut für Systematische Zoologie, Berlin, Germany (CE), and Institut für Physiologische Chemie, Abteilung Angewandte Molekularbiologie, Universität, Mainz, Germany (HCS,DB,SP-O,WEGM)

Correspondence to: Prof. Dr. W.E.G. Müller, Institut für Physiologische Chemie, Abteilung Angewandte Molekularbiologie, Universität, Duesbergweg 6, 55099 Mainz; Germany. E-mail: wmueller{at}uni-mainz.de

The skeleton of demosponges is built of spicules consisting of biosilica. Using the primmorph system from Suberites domuncula, we demonstrate that silicatein, the biosilica-synthesizing enzyme, and silicase, the catabolic enzyme, are colocalized at the surface of growing spicules as well as in the axial filament located in the axial canal. It is assumed that these two enzymes are responsible for the deposition of biosilica. In search of additional potential structural molecules that might guide the mineralization process during spiculogenesis to species-specific spicules, electron microscopic studies with antibodies against galectin and silicatein were performed. These studies showed that silicatein forms a complex with galectin; the strings/bundles of this complex are intimately associated with the surface of the spicules and arranged concentrically around them. Collagen fibers are near the silactein/galectin complexes. The strings/bundles formed from silicatein/galectin display a lower degree of orientation than the collagen fibers arranged in a highly ordered pattern around the spicules. These data indicate that species-specific formation of spicules involves a network of (diffusible) regulatory factor(s) controlling enzymatic silica deposition; this mineralization process proceeds on a galectin/collagen organic matrix. (J Histochem Cytochem 54:1031–1040, 2006)

Key Words: sponges • Porifera • Suberites domuncula • spicules • biosilica • silicatein • silicase • collagen • galectin


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W. E. G. Muller, A. Boreiko, U. Schlossmacher, X. Wang, C. Eckert, K. Kropf, J. Li, and H. C. Schroder
Identification of a silicatein(-related) protease in the giant spicules of the deep-sea hexactinellid Monorhaphis chuni
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