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AIM: Cervico-vaginal fluid (CVF) may provide insight into the biochemical pathways of human reproduction and parturition. The aim of this study was to establish a 2-D electrophoretic map of human CVF in healthy, pregnant women at term. METHODS: CVF was collected, concentrated and processed by routine 2-D polyacrylamide gel electrophoresis using pH 4-7-immobilised pH gradient strips and 8-16% gradient polyacrylamide gels. Imaged gels were analysed, yielding more than 400 proteins. A total of 157 proteins were common to all gels with a subgroup of the most abundant proteins being excised and characterised either by MALDI or by electrospray ion-trap mass spectrometry. RESULTS: Twenty-one proteins were successfully identified, yielding 15 different proteins. These included blood transport proteins (albumin and transthyretin); a structural protein (beta-actin); proteins involved in fatty acid metabolism (fatty acid-binding protein and acetyl-CoA-binding protein); a calcium-binding protein (annexin III); an anti-inflammatory cytokine (interleukin-1 receptor antagonist); proteinase inhibitors (alpha-1-antitrypsin, monocyte/neutrophil elastase inhibitor, squamous cell carcinoma antigen-1 and cystatin A); and enzymes involved in oxidative stress defence (thioredoxin, peroxiredoxin 2, glutathione S-transferase P and copper,zinc superoxide dismutase). CONCLUSION: CVF is a complex body fluid consisting of both endogenous and environmental proteins. The putative role of some of these proteins in the human reproductive tract is discussed.
Quinzio et al. (Mon,) studied this question.