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ARS Home » Southeast Area » Stoneville, Mississippi » Warmwater Aquaculture Research Unit » Research » Publications at this Location » Publication #375740
Research Project: Biophotonics - The Application of Novel Imaging Methodologies to Livestock Production Research

Location: Warmwater Aquaculture Research Unit

Title: Proteome changes of porcine follicular fluid during follicle development

Author
item LIAO, SHENGFA - Mississippi State University
item WILLARD, SCOTT - Mississippi State University
item RYAN, PETER - Mississippi State University
item FEUGANG, JEAN - Mississippi State University

Submitted to: Journal of Animal Science and Biotechnology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 10/18/2019
Publication Date: 12/10/2019
Citation: Liao, S., Willard, S., Ryan, P., Feugang, J. 2019. Proteome changes of porcine follicular fluid during follicle development. Journal of Animal Science and Biotechnology. 10:94.

Interpretive Summary: Folliculogenesis and oogenesis in mammals occur in parallel within the ovary. These processes ensure the production of fully developmental competent oocytes that are capable of normal fertilization, followed by healthy embryonic development and birth of viable offspring. Ovarian follicular fluid influences follicle and oocyte growth, but the fluctuation of its protein content, which can play important roles in the female fertility, during folliculogenesis has not been comprehensively analyzed. The current study provides extensive and functional analyses of the pFF proteome changes during folliculogenesis and offers the potential for novel biomarker discovery in pFF for oocyte quality assessment.

Technical Abstract: Here we used a shotgun approach and bioinformatics analyses to investigate and compare the proteomes of porcine follicular fluid (pFF) obtained from small (<'4'mm), medium (4–6'mm) and large (>'6–12'mm) follicles. Follicular fluid samples containing highest estrogen levels were selected as non-atretic from small (SNA: 26.1'±'15'ng/mL), medium (MNA: 162'±'54'ng/mL), and large (LNA: 290'±'37'ng/mL) follicles for proteomic analyses. We detected 1627, 1699, and 1756 proteins in SNA, MNA, and LNA samples, respectively. Nearly 60–63% of total proteins were specific to each sample, 11–13% were shared in pairwise comparisons, and 247 proteins were shared among all samples. Functional categorization indicated comparable gene ontology (GO) terms distribution per cellular component, molecular function, and biological process categories across samples; however, the ranking of highly significantly enriched GO terms per category revealed differences between samples. The patterns of protein-to-protein interactions varied throughout follicle development, and proteins such as serine protease inhibitor, clade E (SERPINE); plasminogen activator, urokinase (PLAU); and plasminogen activator, urokinase receptor (PLAUR) appeared stage-specific to SNA, MNA, and LNA, respectively. The “complement and coagulation cascades” was the common major pathway. Besides, properdin and fibulin-1 were abundant proteins that appeared absent in LNA samples.