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Updated: Jul 17, 2026
Collection, Isolation, and Flow Cytometric Analysis of Human Endocervical Samples
Published on: July 6, 2014
Proteomic analysis and characterisation of human cervico-vaginal fluid proteins
Megan K W Di Quinzio1, Karen Oliva, Sarah J Holdsworth
1Department of Obstetrics and Gynaecology, The University of Melbourne, Parkville, Victoria, Australia. algmeg@smartchat.net.au
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.
