Abstract
The second most abundant protein in human cerebrospinal fluid after albumin, named β-trace, has been recently identified to be lipocalin-type prostaglandin (PG) D synthase ((5Z,13E)-(15S)-9α, 11α-epidioxy-15-hydroxyprosta-5,13-dienoate-D-isomerase, EC 5.3.99.2)2. This enzyme catalyzes the conversion of PGH2 to PGD2 and is localized to the central nervous system3,4 and male genital organs of mammals5.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
J. Clausen, Proteins in normal cerebrospinal fluid not found in serum, Proc. Soc. Exp. Biol. Med. 107:170 (1961).
A. Hoffmann, H.S. Conradt, G. Gross, M. Nimtz, F. Lottspeich, and U. Wurster, Purification and chemical characterization of β-trace protein from human cerebrospinal fluid: its identification as prostaglandin D synthase, J. Neurochem. 61:451 (1993).
Y. Urade, N. Fujimoto, and O. Hayaishi, Purification and characterization of rat brain prostaglandin D synthetase, J. Biol. Chem. 260:12410 (1985).
C.T. Beuckmann, W.C. Gordon, Y. Kanaoka, N. Eguchi, V.L. Marcheselli, D.Y. Gerashchenko, Y. Urade, O. Hayaishi, and N.G. Bazan, Lipocalin-type prostaglandin D synthase (β-trace) is located in pigment epithelial cells of rat retina and accumulates within interphotoreceptor matrix, J. Neurosci. 16:6119 (1996).
Y. Tokugawa, I. Kunishige, Y. Kubota, K. Shimoya, T. Nobunaga, T. Kimura, F. Saji, Y. Murata, N. Eguchi, H. Oda, Y. Urade, and O. Hayaishi, Lipocalin-type prostaglandin D synthase in human male reproductive organs and seminal plasma, Biol Reprod. 58:600 (1998).
D. R. Flower, The lipocalin protein family: structure and function, Biochem. J. 318:1 (1996).
T. Tanaka, Y. Urade, H. Kimura, N. Eguchi, A. Nishikawa, and O. Hayaishi, Lipocalin-type prostaglandin D synthase (β-trace) is a newly recognized type of retinoid transporter, J. Biol Chem. 272:15789 (1997).
Y. Urade, T. Tanaka, N. Eguchi, M. Kikuchi, H. Kimura, H. Toh, and O. Hayaishi, Structural and functional significance of cysteine residues of glutathione-independent prostaglandin D synthase. Identification of Cys65 as an essential thiol, J. Biol Chem. 270:1422 (1995).
M.E Newcomer, R.S. Pappas, and D.E. Ong, X-ray chrystallographic identification of a protein-binding site for both all-trans and 9-cis-retinoic acid, Proc. Natl. Acad. Sci. USA 90:9223 (1993).
Y. Cho, C.A. Batt, and L. Sawyer, Probing the retinol-binding site of bovine beta-lactoglobulin, J. Biol Chem. 269:11102 (1994).
G. Zanotti, G. Malpeli, and R. Berni, The interaction of N-ethyl retinamide with plasma retinol-binding protein (RBP) and the crystal structure of the retinoid-RBP complex at 1.9-Å resolution, J. Biol. Chem. 268:24873 (1993).
H. Toh, H. Kubodera, N. Nakajima, T. Sekiya, N. Eguchi, T. Tanaka, Y. Urade,, and O. Hayaishi, Glutahthione-independent prostaglandin D synthase as a lead molecule for designing new functional proteins, Protein Engineering 9:1067 (1996).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1999 Springer Science+Business Media New York
About this chapter
Cite this chapter
Beuckmann, C.T., Urade, Y., Hayaishi, O. (1999). Lipocalin-type Prostaglandin D Synthase (β-Trace) Binds Non- Substrate Lipophilic Ligands. In: Honn, K.V., Marnett, L.J., Nigam, S., Dennis, E.A. (eds) Eicosanoids and Other Bioactive Lipids in Cancer, Inflammation, and Radiation Injury, 4. Advances in Experimental Medicine and Biology, vol 469. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4793-8_9
Download citation
DOI: https://doi.org/10.1007/978-1-4615-4793-8_9
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-7171-7
Online ISBN: 978-1-4615-4793-8
eBook Packages: Springer Book Archive