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ARS Home » Plains Area » Clay Center, Nebraska » U.S. Meat Animal Research Center » Nutrition, Growth and Physiology » Research » Publications at this Location » Publication #339129
Title: Characterization and comparison of proteins in the sperm storage tubules of female chickens to bovine epididymal fluid

Author
item PERKINS, STEPHANIE - SOUTH DAKOTA STATE UNIVERSITY
item Cushman, Robert - Bob
item RICH, JERICA - SOUTH DAKOTA STATE UNIVERSITY
item NORTHROP, EMMALEE - SOUTH DAKOTA STATE UNIVERSITY
item PERRY, GEORGE - SOUTH DAKOTA STATE UNIVERSITY

Submitted to: Society for the Study of Reproduction Annual Meeting
Publication Type: Abstract Only
Publication Acceptance Date: 4/11/2017
Publication Date: 7/10/2017
Citation: Perkins, S.D., Cushman, R.A., Rich, J.J., Northrop, E.L., Perry, G.A. 2017. Characterization and comparison of proteins in the sperm storage tubules of female chickens to bovine epididymal fluid [abstract]. Society for the Study of Reproduction Annual Meeting. Abstract #P467 (Scientific Program p. 158-159). Available: http://www.ssr.org/sites/ssr.org/files/uploads/attachments/node/482/ssr2017abstracts.pdf

Interpretive Summary:

Technical Abstract: Female birds are able to store sperm in crypts called sperm storage tubules (SSTs) in their reproductive tracts for between two and six weeks. Comparatively, sperm in a cow’s reproductive tract remain viable for between 18 and 24 hours. The objective of this experiment was to try to identify and compare proteins in the female chicken SSTs to proteins in the bull epididymis, which is capable of storing sperm for approximately two weeks. Proteins were collected by dissecting the reproductive tracts of 6 chickens. The mucosal layer was scraped from the utero-vaginal junction and incubated in buffer to wash off the proteins. The samples from each chicken were pooled and the proteins were identified by LCMS-MS at the University of Minnesota Mass Spectrometry facility. The software package PEAKS 8 was used to characterize proteins against known databases. Epididymal fluid and sperm was collected from each of 9 bulls after slaughter. Following collection, samples were centrifuged to separate sperm from fluid. Spermatozoa were washed with a high ionic solution to remove any proteins attached to the spermatozoa, samples were pooled, and proteins were identified by LCMS-MS at the University of Minnesota Mass Spectrometry facility. The software package Scaffold was used to characterize proteins against bovine databases. There were 322 unique proteins identified in the chicken samples, and 311 unique proteins identified in the bovine epididymal fluid. Eighty-seven proteins were present in both the chicken pools and the bovine epididymal fluid. Pathway analysis of these 87 proteins in DAVID v6.7 identified enrichment for proteins involved in eukaryotic cell surface binding (P = 0.05). Specifically within this pathway, ANXA5 has been associated with asthenospermia. Since a large proportion (27%) of proteins were similar between the chicken pools and the bovine epididymal fluid, further investigation into these proteins may provide insight into the process that allows sperm to be stored for extended periods of time.