| Title | Proteomic Analysis of Human Cervico-Vaginal Fluid. | | Author(s) | Shaw JL, Smith CR, Diamandis EP | | Institution | Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, Toronto, Ontario, Canada M5G 1X5, and Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario, Canada M5G 1L5. | | Source | J Proteome Res 2007 Jun 14. | | Abstract | Human cervico-vaginal fluid (CVF) is a mixture of fluids originating from the vagina, cervix, endometrium, and oviduct. CVF has been shown to play an important role in protecting the vagina from infection. We used "bottom-up" proteomic approaches to characterize the protein repertoire of human CVF. We applied two different sample prefractionation methods, one-dimensional-SDS-PAGE (1D-SDS-PAGE) and strong cation-exchange chromatography, followed by LC-MS/MS and bioinformatic analysis. We identified a total of 685 proteins. Strong cation-exchange chromatography prefractionation resulted in a larger number of proteins identified when compared with 1D-SDS-PAGE. Extracellular or membrane proteins made up 30% of the proteins identified, according to Genome Ontology (GO) classifications. We confirmed the presence of defense-related proteins, such as haptoglobin, defensins, and lactoferrin; and identified new ones such as azurocidin and dermcidin. We also identified many serine and cysteine proteases, including 6 members of the kallikrein family (KLKs 6, 7, 10, 11, 12, and 13). The same KLKs were also confirmed quantitatively by ELISA assays. Knowledge of the CVF proteome will aid in the discovery of potential biomarkers for gynecological malignancies and infections and provide additional clues for its physiological functions. Keywords: cervico-vaginal fluid * mass spectrometry * proteomes * intravaginal infections * host defense * proteases * protease inhibitors * kallikreins. | | Language | ENG | | Pub Type(s) | JOURNAL ARTICLE
| | PubMed ID | 17567164 |
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