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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Müller, Werner E. G. Boreiko, Alexandra Schlossmacher, Ute Wang, Xiaohong Eckert, Carsten Kropf, Klaus Li, Jinhe Schröder, Heinz C. |
| Description | Country affiliation: Germany Author Affiliation: Müller WE ( Institut für Physiologische Chemie, Abteilung Angewandte Molekularbiologie, Universität, Duesbergweg 6, D-55099 Mainz, Germany. wmueller@uni-mainz.de) |
| Abstract | Silicateins, members of the cathepsin L family, are enzymes that have been shown to be involved in the biosynthesis/condensation of biosilica in spicules from Demospongiae (phylum Porifera), e.g. Tethya aurantium and Suberites domuncula. The class Hexactinellida also forms spicules from this inorganic material. This class of sponges includes species that form the largest biogenic silica structures on earth. The giant basal spicules from the hexactinellids Monorhaphis chuni and Monorhaphis intermedia can reach lengths of up to 3 m and diameters of 10 mm. The giant spicules as well as the tauactines consist of a biosilica shell that surrounds the axial canal, which harbours the axial filament, in regular concentric, lamellar layers, suggesting an appositional growth of the spicules. The lamellae contain 27 kDa proteins, which undergo post-translational modification (phosphorylation), while total spicule extracts contain additional 70 kDa proteins. The 27 kDa proteins cross-reacted with anti-silicatein antibodies. The extracts of spicules from the hexactinellid Monorhaphis displayed proteolytic activity like the silicateins from the demosponge S. domuncula. Since the proteolytic activity in spicule extracts from both classes of sponge could be sensitively inhibited by E-64 (a specific cysteine proteinase inhibitor), we used a labelled E-64 sample as a probe to identify the protein that bound to this inhibitor on a blot. The experiments revealed that the labelled E-64 selectively recognized the 27 kDa protein. Our data strongly suggest that silicatein(-related) molecules are also present in Hexactinellida. These new results are considered to also be of impact for applied biotechnological studies. |
| File Format | HTM / HTML |
| ISSN | 00220949 |
| e-ISSN | 14779145 |
| Journal | Journal of Experimental Biology |
| Issue Number | Pt 3 |
| Volume Number | 211 |
| Language | English |
| Publisher | The Company of Biologists |
| Publisher Date | 2008-02-01 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | Open |
| Subject Keyword | Discipline Biology Animal Structures Enzymology Cathepsins Metabolism Porifera Anatomy & Histology Amino Acid Sequence Drug Effects Ultrastructure Animals Binding Sites Cystatins Chemistry Cysteine Proteinase Inhibitors Pharmacology Molecular Probes Molecular Sequence Data Molecular Weight Oceans And Seas Phylogeny Protein Processing, Post-translational Research Support, Non-u.s. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Physiology Medicine Aquatic Science Molecular Biology Animal Science and Zoology Ecology, Evolution, Behavior and Systematics Insect Science |
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