4.4 Article Proceedings Paper

Expression and anti-bacterial activity of human parotid secretory protein (PSP)

Journal

BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 31, Issue -, Pages 815-818

Publisher

PORTLAND PRESS LTD
DOI: 10.1042/bst0310815

Keywords

antibody; BPI (bactericidal/permeability-increasing protein); chromosome 20; Pseudomonas aeruginosa; saliva

Funding

  1. NIDCR NIH HHS [R01 DE12205] Funding Source: Medline

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Parotid secretory protein (PSP) is an abundant protein in mouse and rat parotid glands. A related sequence (C20orf70) was identified on human chromosome 20. The goal of this study was to determine if PSP is expressed in the human parotid gland. The cDNA for human PSP was amplified from a human parotid cDNA sample. A peptide antibody, raised to the C-terminal peptide of PSP, identified the protein in human parotid tissue by immunofluorescence microscopy. Immunoaffinity chromatography suggested that PSP was expressed in human saliva. PSP is related to bactericidal/permeability-increasing protein (BPI). To test if PSP exhibits anti-bacterial activity, epitope-tagged PSP was expressed in rat GH4C1 cells. The secretion medium exhibited bacteristatic or bactericidal effects on Pseudomonas aeruginosa in a colony-forming assay when compared with secretion medium from GH4C1 cells that did not express PSP. These results suggest that PSP is expressed in the human parotid gland and saliva, where it functions as a BPI-like anti-bacterial protein.

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