Molecular Cloning and Characterization of Spiggin: An androgen-regulated extraorganismal adhesive with structural similarities to von Willebrand Factor-related proteins
2001 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 276, no 21, 17857-17863 p.Article in journal (Refereed) Published
One of the most definitive examples of a vertebrate extraorganismal structural protein can be found in three-spined sticklebacks (Gasterosteus aculeatus). In the breeding male the kidney hypertrophies and synthesizes an adhesive protein called "spiggin," which is secreted into the urinary bladder from where it is employed as a structural thread for nest building. This paper describes the first molecular characterization of spiggin and demonstrates that this adhesive is a protein complex assembled from a potential of three distinct subunits (alpha, beta, and gamma). These subunits arise by alternative splicing, and 11-ketoandrogens induce their expression in stickleback kidneys. Analysis of the predicted amino acid sequence of each subunit reveals a modular organization whose structural elements display a similarity to the multimerization domains found within von Willebrand Factor-related proteins. These results implicate that spiggin utilizes a conserved multimerization mechanism for the formation of a viscous agglutinate from its constituent subunits in the urinary bladders of male sticklebacks. This novel extraorganismal structural protein is therefore ideally suited to its function as an adhesive thread.
Place, publisher, year, edition, pages
2001. Vol. 276, no 21, 17857-17863 p.
Adhesives, Agglutinins/genetics/urine, Amino Acid Sequence, Androgens/metabolism, Animals, Bladder/metabolism, Fishes, Male, Molecular Sequence Data, RNA; Messenger/biosynthesis/genetics, Research Support; Non-U.S. Gov't, Sequence Alignment, von Willebrand Factor/genetics/metabolism
Medical and Health Sciences
IdentifiersURN: urn:nbn:se:uu:diva-73562DOI: 10.1074/jbc.M101142200PubMedID: 11279178OAI: oai:DiVA.org:uu-73562DiVA: diva2:101472