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Journal Molluscan Studies Advance Access originally published online on November 2, 2007
Journal of Molluscan Studies 2008 74(1):11-17; doi:10.1093/mollus/eym037
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© The Author 2007. Published by Oxford University Press on behalf of The Malacological Society of London, all rights reserved

Origin of a metal-binding protein in serum of Mytilus edulis

Lothar Renwrantz and Irena Werner

Biozentrum Grindel und Zoologisches Museum, Martin-Luther-King-Platz 3, 20146 Hamburg, Germany

Correspondence: L. Renwrantz; e-mail: l.renwrantz{at}gmx.de


  Abstract

The most abundant humoral protein of the haemolymph of Mytilus edulis is known to bind a variety of heavy metals (Renwrantz et al., 1998 Comp. Biochem. Physiol. A, 121: 175–180). This serum protein band 1 (SPB1) was isolated from Mytilus serum by a two-step purification procedure. For the purified protein a molecular weight of 34 kDa was estimated under denaturing conditions and of 37 kDa in its reduced form. After blotting of Mytilus serum onto a nitrocellulose membrane, Cu-binding by SPB1 was visualized. Furthermore, indications were obtained of Ca-binding properties of SPB1 and of some bands postulated to be SPB1-oligomers. Formation of dimers was confirmed by their reaction with SPB1-specific antibodies. On immunoblots, anti-SPB1 detected the metal-binding protein in postnuclear haemocyte extracts. After further fractionation of the cell homogenate by sucrose gradient centrifugation, the indicator antibodies recognized SPB1 in the cytosol, as a component of the plasma membrane and in the fraction of granules which was assumed to include secretory vesicles. Investigation of the supernatant from a 24 h haemocyte culture indicated release of the metal-binding protein by blood-cells. Incubations of different haemocyte monolayers on slides with anti-SPB1 indicated expression of SPB1 in amounts of 55% to almost 100% of the cells, whereby the intensity of antibody-staining varied between individual haemocytes. Intensity was independent of cell type as density gradient separation of haemocytes into basophilic and eosinophilic granulocytes resulted in similar staining patterns in both groups. Thus, all granulocytes seemed to be able to produce SPB1 with a varying degree of activity indicating a hitherto unknown regulation system.

(Received 4 June 2007; accepted 6 September 2007)


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