Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/9397
Citations
Scopus Web of ScienceĀ® Altmetric
?
?
Type: Journal article
Title: Isolation and partial characterization of a pentraxin-like protein with complement-fixing activity from snapper (Pagrus auratus, Sparidae) serum
Author: Cook, M.
Hayball, P.
Birdseye, L.
Bagley, C.
Nowak, B.
Hayball, J.
Citation: Developmental and Comparative Immunology, 2003; 27(6-7):579-588
Publisher: Pergamon-Elsevier Science Ltd
Issue Date: 2003
ISSN: 0145-305X
1879-0089
Statement of
Responsibility: 
Cook, Mathew T; Hayball, Peter J; Birdseye, Laurie; Bagley, Christopher; Nowak, Barbara F; Hayball, John D
Abstract: Pentraxin-like molecules have been isolated from a number of fish species. However, little is known about the function of these proteins in the teleosts. In this study we report the isolation and characterization of a pentraxin-like molecule from the serum of snapper (Pagrus auratus) that has the ability to activate complement. This pentraxin-like protein was isolated from serum by calcium-dependent binding to agarose. SDS-PAGE analysis demonstrated an oligomeric protein of approximately 200k Da consisting of non-covalently bound subunits of 26 and 23 kDa. Protein sequencing revealed significant (50%) sequence identity with pentraxins from both Atlantic salmon (S. salar) and rainbow trout (O. mykiss). However, polyclonal antibodies raised against snapper pentraxin did not recognise salmon or trout pentraxin in Western blot analysis. Following LPS injection, snapper pentraxin levels increased 2-fold before gradually returning to basal levels. Most significantly, the isolated pentraxin initiated complement-mediated lysis of ligand-coated sheep erythrocytes in a dose-dependent fashion. In view of the similarity between the known fish pentraxins, and their similarity to mammalian serum amyloid P-components we conclude that the isolated protein may be a snapper pentraxin homologue.
Keywords: Animals; Fishes; C-Reactive Protein; Serum Amyloid P-Component; Up-Regulation; Amino Acid Sequence; Multigene Family; Molecular Sequence Data; Complement System Proteins
RMID: 0020031233
DOI: 10.1016/S0145-305X(03)00034-X
Appears in Collections:Medicine publications

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.