Binding specificity of serum amyloid P component for the pyruvate acetal of galactose

doi:10.1084/jem.159.4.1058

This Article

	Full Text (PDF, 892K)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JEM
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Hind, C. R.
	Articles by Pepys, M. B.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Hind, C. R.
	Articles by Pepys, M. B.


Social Bookmarking

	What's this?

ARTICLES

Binding specificity of serum amyloid P component for the pyruvate acetal of galactose

CR Hind, PM Collins, D Renn, RB Cook, D Caspi, ML Baltz and MB Pepys

Serum amyloid P component (SAP) is a normal plasma protein that is of interest because of its presence in amyloid deposits, its presence in normal human glomerular basement membrane, and its stable evolutionary conservation. It has calcium-dependent ligand-binding specificity for amyloid fibrils, fibronectin (Fn), C4-binding protein (C4bp), and agarose. Although the binding to agarose, a linear galactan hydrocolloid derived from some marine algae, is unlikely per se to be related to the physiological function of SAP, it does provide a model system in which to explore the precise ligand requirements of SAP. We report here that the amount of SAP from human, mouse, and plaice (Pleuronectes platessa L.) serum able to bind to agarose from different sources reflect precisely their pyruvate content. Methylation with diazomethane of the carboxyl groups in the pyruvate moiety of agarose completely abolishes SAP binding to agarose. The pyruvate in agarose exists as the 4,6-pyruvate acetal of beta-D-galactopyranose. We have therefore synthesized this galactoside, using a novel procedure, established its structure by analysis of its nuclear magnetic resonance spectra, and shown that it completely inhibits all known calcium- dependent binding reactions of SAP. The R isomer of the cyclic acetal, methyl 4,6-O-(1-carboxyethylidene)-beta-D-galactopyranoside (MO beta DG) was effective at millimolar concentration and was more potent than its noncyclic analogue, while pyruvate, D-galactose, and methyl beta-D- galactopyranoside were without effect. The autologous protein ligands of SAP presumably, therefore express a structural determinant(s) that stereochemically resembles MO beta DG. Availability of this specific, well-characterized, low molecular weight ligand for SAP should facilitate further investigation of the function of SAP and its role in physiological and pathophysiological processes.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Balci-Peynircioglu, B., Waite, A. L., Schaner, P., Taskiran, Z. E., Richards, N., Orhan, D., Gucer, S., Ozen, S., Gumucio, D., Yilmaz, E. (2008). Expression of ASC in Renal Tissues of Familial Mediterranean Fever Patients with Amyloidosis: Postulating a Role for ASC in AA Type Amyloid Deposition. Exp. Biol. Med. 233: 1324-1333 [Abstract] [Full Text]
Mineo, C., Gormley, A. K., Yuhanna, I. S., Osborne-Lawrence, S., Gibson, L. L., Hahner, L., Shohet, R. V., Black, S., Salmon, J. E., Samols, D., Karp, D. R., Thomas, G. D., Shaul, P. W. (2005). Fc{gamma}RIIB Mediates C-Reactive Protein Inhibition of Endothelial NO Synthase. Circ. Res. 97: 1124-1131 [Abstract] [Full Text]
Andreishcheva, E. N., Kunkel, J. P., Gemmill, T. R., Trimble, R. B. (2004). Five Genes Involved in Biosynthesis of the Pyruvylated Gal{beta}1,3-Epitope in Schizosaccharomyces pombe N-Linked Glycans. J. Biol. Chem. 279: 35644-35655 [Abstract] [Full Text]
Palaniyar, N., Nadesalingam, J., Clark, H., Shih, M. J., Dodds, A. W., Reid, K. B. M. (2004). Nucleic Acid Is a Novel Ligand for Innate, Immune Pattern Recognition Collectins Surfactant Proteins A and D and Mannose-binding Lectin. J. Biol. Chem. 279: 32728-32736 [Abstract] [Full Text]
Bharadwaj, D., Mold, C., Markham, E., Du Clos, T. W. (2001). Serum Amyloid P Component Binds to Fc{{gamma}} Receptors and Opsonizes Particles for Phagocytosis. J. Immunol. 166: 6735-6741 [Abstract] [Full Text]
Mold, C., Gresham, H. D., Du Clos, T. W. (2001). Serum Amyloid P Component and C-Reactive Protein Mediate Phagocytosis Through Murine Fc{{gamma}}Rs. J. Immunol. 166: 1200-1205 [Abstract] [Full Text]
Noursadeghi, M., Bickerstaff, M. C. M., Gallimore, J. R., Herbert, J., Cohen, J., Pepys, M. B. (2000). Role of serum amyloid P component in bacterial infection: Protection of the host or protection of the pathogen. Proc. Natl. Acad. Sci. USA 97: 14584-14589 [Abstract] [Full Text]
Szalai, A. J., VanCott, J. L., McGhee, J. R., Volanakis, J. E., Benjamin, W. H. Jr. (2000). Human C-Reactive Protein Is Protective against Fatal Salmonella enterica Serovar Typhimurium Infection in Transgenic Mice. Infect. Immun. 68: 5652-5656 [Abstract] [Full Text]
Bottazzi, B., Vouret-Craviari, V., Bastone, A., De Gioia, L., Matteucci, C., Peri, G., Spreafico, F., Pausa, M., D'Ettorre, C., Gianazza, E., Tagliabue, A., Salmona, M., Tedesco, F., Introna, M., Mantovani, A. (1997). Multimer Formation and Ligand Recognition by the Long Pentraxin PTX3. SIMILARITIES AND DIFFERENCES WITH THE SHORT PENTRAXINS C-REACTIVE PROTEIN AND SERUM AMYLOID P COMPONENT. J. Biol. Chem. 272: 32817-32823 [Abstract] [Full Text]
Gemmill, T. R., Trimble, R. B. (1996). Schizosaccharomyces pombe Produces Novel Pyruvate-containing N-Linked Oligosaccharides. J. Biol. Chem. 271: 25945-25949 [Abstract] [Full Text]
Li, X. A., Hatanaka, K., Ishibashi-Ueda, H., Yutani, C., Yamamoto, A. (1995). Characterization of Serum Amyloid P Component From Human Aortic Atherosclerotic Lesions. Arterioscler. Thromb. Vasc. Bio. 15: 252-257 [Abstract] [Full Text]