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Hum. Reprod. Advance Access originally published online on November 22, 2007
Human Reproduction 2008 23(2):379-386; doi:10.1093/humrep/dem367
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© The Author 2007. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Protein repertoire of human uterine fluid duringthe mid-secretory phase of the menstrual cycle

T. Parmar1, G. Sachdeva1,5, L. Savardekar2, R.R. Katkam1, S. Nimbkar-Joshi1, S. Gadkar-Sable1, V. Salvi3, D.D. Manjramkar4, P. Meherji2 and C.P. Puri1

1 Primate Biology Division, National Institute for Research in Reproductive Health, Indian Council of Medical Research, Jehangir Merwanji Street, Parel, Mumbai 400012, Maharashtra, India 2 Division of Clinical Research, National Institute for Research in Reproductive Health, Indian Council of Medical Research, Jehangir Merwanji Street, Parel, Mumbai 400012, Maharashtra, India 3 Department of Obstetrics and Gynecology, Seth G.S. Medical College and King Edward Medical Hospital, Parel, Mumbai 400012, Maharashtra, India 4 Experimental Animal Facility, National Institute for Research in Reproductive Health, Indian Council of Medical Research, Jehangir Merwanji Street, Parel, Mumbai 400012, Maharashtra, India

5 Correspondence address. Tel: +91-22-24192111; Fax: +91-22-24139412; E-mail: ritugeet{at}vsnl.net, geetanjali_sachdeva{at}yahoo.com

BACKGROUND: This study is an attempt to construct a repository of polypeptide species in human uterine fluid during the mid-secretory phase of menstrual cycle. This information is essential to generate alternative and less invasive tools for the assessment of uterine functions.

METHODS: Two-dimensional polyacrylamide gel electrophoresis (2D PAGE) and mass spectrometric analysis were used to resolve and identify the major components of human uterine fluid.

RESULTS: Uterine fluid collected during the mid-secretory phase (n = 6) demonstrated ca. 590 polypeptide spots in the linear range of pH 4–7 after 2D PAGE. Mass spectrometric analysis revealed the presence of heavy and light chains of immunoglobulins, alpha-1 anti-trypsin precursor, anti-chymotrypsin precursor, haptoglobin, apolipoprotein A4, apolipoprotein A1 fragment, beta-actin fragment, heat shock protein 27, hemopexin precursor and transferrin precursor. 2D protein profile of fluid collected during the proliferative phase (n = 5) revealed ca. 433 polypeptide spots, of which 279 could be paired with mid-secretory phase protein spots on the basis of their coordinates (isoelectric point and molecular weight) in 2D gels. Apolipoprotein A4, apolipoprotein A1 fragment and alpha-1 anti-trypsin precursor were 2–3-fold more abundant in uterine fluid collected during the mid-secretory phase as compared with that in the proliferative phase. Further, 86 uterine fluid polypeptides were conserved across species, being detected in human, rat and bonnet monkeys.

CONCLUSIONS: The molecular repertoire of the mid-secretory phase human uterine fluid, when compared with that of the proliferative phase uterine fluid, is broadened due to differential expression of proteins. Further, some of the mid-secretory phase proteins were conserved across species.

Key words: endometrium/two-dimensional gel electrophoresis/receptivity/uterine fluid/protein maps

Submitted on May 18, 2007; resubmitted on October 2, 2007; accepted on October 22, 2007.


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