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Originally published In Press as doi:10.1074/jbc.M101142200 on March 1, 2001

J. Biol. Chem., Vol. 276, Issue 21, 17857-17863, May 25, 2001
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Molecular Cloning and Characterization of Spiggin
AN ANDROGEN-REGULATED EXTRAORGANISMAL ADHESIVE WITH STRUCTURAL SIMILARITIES TO Von Willebrand FACTOR-RELATED PROTEINS*

Iwan JonesDagger , Christina LindbergDagger , Staffan Jakobsson§, Anna Hellqvist§, Ulf Hellman, Bertil Borg§, and Per-Erik OlssonDagger ||

From the Dagger  Department of Cell and Molecular Biology, Unit of Physiology, Umeå University, SE-901 87 Umeå, Sweden, the § Department of Zoology, Stockholm University, SE-106 91 Stockholm, Sweden and the  Ludwig Institute for Cancer Research, Uppsala Biomedical Center, SE-751 24 Uppsala, Sweden

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.


* This work was supported by the Swedish Forestry and Agriculture Research Council (to P.-E. O.), the Swedish Environmental Protection Agency (to P.-E. O.), and the Swedish Natural Science Research Council (to B. B.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF323732 (spiggin subunit-alpha ), AF323733 (spiggin subunit-beta ), and AF323734 (spiggin subunit-gamma ).

|| To whom correspondence should be addressed: Dept. of Cell and Molecular Biology, Unit of Physiology, Umeå University, SE-901 87 Umeå, Sweden. Tel.: 46-90-7869545; Fax: 46-90-7866691; E-mail: Per-Erik.Olsson@biology.umu.se.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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