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Am J Physiol Regul Integr Comp Physiol 288: R1306-R1315, 2005. First published January 6, 2005; doi:10.1152/ajpregu.00007.2004
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INFLAMMATION AND CYTOKINES

Parotid secretory protein is an HDL-associated protein with anticandidal activity

Weerapan Khovidhunkit,1,2 Jean Pierre Hachem,3 Katalin F. Medzihradszky,4 Philippe N. Duchateau,5 Judy K. Shigenaga,1 Arthur H. Moser,1 Irina Movsesyan,5 Josefina Naya-Vigne,5 John P. Kane,2,5 Kenneth R. Feingold,1,2,3 and Carl Grunfeld1,2

1Metabolism Section, Medical Service, and 3Dermatology Service, Department of Veterans Affairs Medical Center, San Francisco; 2Department of Medicine, 4Pharmaceutical Chemistry and Mass Spectrometry Facility, and 5Cardiovascular Research Institute, University of California, San Francisco, California

Submitted 6 January 2004 ; accepted in final form 14 December 2004

High-density lipoprotein (HDL) is part of innate immunity, protecting against infection and inflammation. Using a proteomic approach, we identified an amino acid sequence in a hamster HDL protein that showed homology to rat and mouse parotid secretory protein (PSP), a salivary protein secreted from the parotid glands. We cloned the cDNA encoding a putative hamster homolog of rat and mouse PSP. Searches for conserved domains of the protein showed that the COOH terminus of hamster PSP contains a region homologous to the NH2 termini of a family of HDL-associated proteins, including LPS-binding protein, cholesteryl ester transfer protein, and phospholipid transfer protein. In mice, PSP was also associated with HDL but was not detected in very-low-density lipoprotein, low-density lipoprotein, or lipoprotein-deficient sera. In addition to salivary glands, we found that PSP mRNA was expressed in lung, testis, and ovary. The level of PSP in HDL was increased after endotoxin injection in hamsters, but not in mice. Recombinant PSP inhibits growth of Candida albicans in culture. In summary, our results showed that PSP is a novel anticandidal protein associated with HDL.

endotoxins; acute-phase reaction; two-dimensional gel electrophoresis; proteomics; Candida albicans


Address for reprint requests and other correspondence: C. Grunfeld, Metabolism Sect., Dept. of Veterans Affairs Medical Center, 4150 Clement St., Box 111 F, San Francisco, CA 94121 (E-mail: grunfld{at}itsa.ucsf.edu)






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