Quantitative proteomic profiling of bovine follicular fluid during follicle development
Bovine follicular fluid (FF) constitutes the microenvironment of follicles and includes various biologically active proteins. We performed a study involving 18 healthy nonlactating Holstein cows to determine the protein expression profile of FF at key stages of follicular development. Follicles were...
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| Veröffentlicht in: | Biology of reproduction 2017-12, Vol.97 (6), p.835-849 |
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| creator | Ferrazza, Rodrigo de Andrade Garcia, Henry David Mogollón Schmidt, Elizabeth Moreira dos Santos Carmichael, Monika Mihm Souza, Fabiana Ferreira de Burchmore, Richard Sartori, Roberto Eckersall, Peter David Ferreira, João Carlos Pinheiro |
| description | Bovine follicular fluid (FF) constitutes the microenvironment of follicles and includes various biologically active proteins. We performed a study involving 18 healthy nonlactating Holstein cows to determine the protein expression profile of FF at key stages of follicular development. Follicles were individually aspirated in vivo at predeviation (F1 ∼ 7.0 mm), deviation (F1 ∼ 8.5 mm), postdeviation (F1 ∼ 12.0 mm), and preovulatory stages of follicle development, which were confirmed by measurement of follicular estradiol and progesterone concentrations. The FFs from nine cows were selected for proteomic analysis. After albumin depletion, triplicates of pooled FF were reduced, alkylated, and digested with trypsin. The resulting peptides were labeled with TMTsixplex and quantified using liquid chromatography-mass spectrometry/mass spectrometry. A total of 143 proteins were identified and assigned to a variety of biological processes, including response to stimulus and metabolic processes. Twenty-two differentially (P < 0.05) expressed proteins were found between stages indicating intrafollicular changes over development, with expected deviation time critical to modulate the protein expression. For instance, high concentrations of follistatin, inhibin, serglycin, spondin-1, fibrinogen, and anti-testosterone antibody were found during early stages of follicular development. In contrast, apolipoprotein H, alpha-2-macroglobulin, plasminogen, antithrombin-III, and immunoglobulins were increased after deviation. Among the differentially abundant proteins, 19 were found to be associated with steroidogenesis. Pathway analysis identified proteins that were mainly associated with the acute phase response signaling, coagulation system, complement system, liver/retinoid X receptor activation, and biosynthesis of nitric oxide and reactive oxygen. The differentially expressed proteins provide insights into the size-dependent protein changes in the ovarian follicle microenvironment that could influence follicular function. Summary Sentence The protein dynamic changes in ovarian follicle microenvironment during the follicle development are critical for follicular maturation and influence follicular function in cows. |
| doi_str_mv | 10.1093/biolre/iox148 |
| format | Article |
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We performed a study involving 18 healthy nonlactating Holstein cows to determine the protein expression profile of FF at key stages of follicular development. Follicles were individually aspirated in vivo at predeviation (F1 ∼ 7.0 mm), deviation (F1 ∼ 8.5 mm), postdeviation (F1 ∼ 12.0 mm), and preovulatory stages of follicle development, which were confirmed by measurement of follicular estradiol and progesterone concentrations. The FFs from nine cows were selected for proteomic analysis. After albumin depletion, triplicates of pooled FF were reduced, alkylated, and digested with trypsin. The resulting peptides were labeled with TMTsixplex and quantified using liquid chromatography-mass spectrometry/mass spectrometry. A total of 143 proteins were identified and assigned to a variety of biological processes, including response to stimulus and metabolic processes. Twenty-two differentially (P < 0.05) expressed proteins were found between stages indicating intrafollicular changes over development, with expected deviation time critical to modulate the protein expression. For instance, high concentrations of follistatin, inhibin, serglycin, spondin-1, fibrinogen, and anti-testosterone antibody were found during early stages of follicular development. In contrast, apolipoprotein H, alpha-2-macroglobulin, plasminogen, antithrombin-III, and immunoglobulins were increased after deviation. Among the differentially abundant proteins, 19 were found to be associated with steroidogenesis. Pathway analysis identified proteins that were mainly associated with the acute phase response signaling, coagulation system, complement system, liver/retinoid X receptor activation, and biosynthesis of nitric oxide and reactive oxygen. The differentially expressed proteins provide insights into the size-dependent protein changes in the ovarian follicle microenvironment that could influence follicular function. Summary Sentence The protein dynamic changes in ovarian follicle microenvironment during the follicle development are critical for follicular maturation and influence follicular function in cows.</description><identifier>ISSN: 0006-3363</identifier><identifier>EISSN: 1529-7268</identifier><identifier>DOI: 10.1093/biolre/iox148</identifier><identifier>PMID: 29149247</identifier><language>eng</language><publisher>United States: Society for the Study of Reproduction</publisher><subject>17β-Estradiol ; Animals ; Antithrombin ; Apolipoproteins ; Biological activity ; Cattle ; Complement activation ; Developmental stages ; Female ; FEMALE REPRODUCTIVE TRACT ; Fibrinogen ; Follicles ; Follicular fluid ; Follicular Fluid - metabolism ; Follicular Phase ; folliculogenesis ; Follistatin ; Holstein cow ; Immunoglobulins ; Inhibin ; Liquid chromatography ; Liver X receptors ; Mass spectrometry ; Mass spectroscopy ; Microenvironments ; Nitric oxide ; Ovarian Follicle - physiology ; Progesterone ; Protein expression ; Proteins ; Proteome - metabolism ; proteomic ; Proteomics ; Receptor mechanisms ; Scientific imaging ; steroid hormone ; Steroidogenesis ; Testosterone ; Trypsin ; α2-Macroglobulin</subject><ispartof>Biology of reproduction, 2017-12, Vol.97 (6), p.835-849</ispartof><rights>The Author(s) 2017. Published by Oxford University Press on behalf of Society for the Study of Reproduction. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com journals.permissions@oup.com</rights><rights>The Author(s) 2017. Published by Oxford University Press on behalf of Society for the Study of Reproduction. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com 2017</rights><rights>The Author(s) 2017. Published by Oxford University Press on behalf of Society for the Study of Reproduction. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.</rights><rights>The Author(s) 2017. Published by Oxford University Press on behalf of Society for the Study of Reproduction. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-b429t-20cbca61248249871a78bec2a1a8cf0ce69bd64091933b0673eddeda095ad82d3</citedby><cites>FETCH-LOGICAL-b429t-20cbca61248249871a78bec2a1a8cf0ce69bd64091933b0673eddeda095ad82d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,1585,27929,27930</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29149247$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ferrazza, Rodrigo de Andrade</creatorcontrib><creatorcontrib>Garcia, Henry David Mogollón</creatorcontrib><creatorcontrib>Schmidt, Elizabeth Moreira dos Santos</creatorcontrib><creatorcontrib>Carmichael, Monika Mihm</creatorcontrib><creatorcontrib>Souza, Fabiana Ferreira de</creatorcontrib><creatorcontrib>Burchmore, Richard</creatorcontrib><creatorcontrib>Sartori, Roberto</creatorcontrib><creatorcontrib>Eckersall, Peter David</creatorcontrib><creatorcontrib>Ferreira, João Carlos Pinheiro</creatorcontrib><title>Quantitative proteomic profiling of bovine follicular fluid during follicle development</title><title>Biology of reproduction</title><addtitle>Biol Reprod</addtitle><description>Bovine follicular fluid (FF) constitutes the microenvironment of follicles and includes various biologically active proteins. We performed a study involving 18 healthy nonlactating Holstein cows to determine the protein expression profile of FF at key stages of follicular development. Follicles were individually aspirated in vivo at predeviation (F1 ∼ 7.0 mm), deviation (F1 ∼ 8.5 mm), postdeviation (F1 ∼ 12.0 mm), and preovulatory stages of follicle development, which were confirmed by measurement of follicular estradiol and progesterone concentrations. The FFs from nine cows were selected for proteomic analysis. After albumin depletion, triplicates of pooled FF were reduced, alkylated, and digested with trypsin. The resulting peptides were labeled with TMTsixplex and quantified using liquid chromatography-mass spectrometry/mass spectrometry. A total of 143 proteins were identified and assigned to a variety of biological processes, including response to stimulus and metabolic processes. Twenty-two differentially (P < 0.05) expressed proteins were found between stages indicating intrafollicular changes over development, with expected deviation time critical to modulate the protein expression. For instance, high concentrations of follistatin, inhibin, serglycin, spondin-1, fibrinogen, and anti-testosterone antibody were found during early stages of follicular development. In contrast, apolipoprotein H, alpha-2-macroglobulin, plasminogen, antithrombin-III, and immunoglobulins were increased after deviation. Among the differentially abundant proteins, 19 were found to be associated with steroidogenesis. Pathway analysis identified proteins that were mainly associated with the acute phase response signaling, coagulation system, complement system, liver/retinoid X receptor activation, and biosynthesis of nitric oxide and reactive oxygen. The differentially expressed proteins provide insights into the size-dependent protein changes in the ovarian follicle microenvironment that could influence follicular function. Summary Sentence The protein dynamic changes in ovarian follicle microenvironment during the follicle development are critical for follicular maturation and influence follicular function in cows.</description><subject>17β-Estradiol</subject><subject>Animals</subject><subject>Antithrombin</subject><subject>Apolipoproteins</subject><subject>Biological activity</subject><subject>Cattle</subject><subject>Complement activation</subject><subject>Developmental stages</subject><subject>Female</subject><subject>FEMALE REPRODUCTIVE TRACT</subject><subject>Fibrinogen</subject><subject>Follicles</subject><subject>Follicular fluid</subject><subject>Follicular Fluid - metabolism</subject><subject>Follicular Phase</subject><subject>folliculogenesis</subject><subject>Follistatin</subject><subject>Holstein cow</subject><subject>Immunoglobulins</subject><subject>Inhibin</subject><subject>Liquid chromatography</subject><subject>Liver X receptors</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>Microenvironments</subject><subject>Nitric oxide</subject><subject>Ovarian Follicle - physiology</subject><subject>Progesterone</subject><subject>Protein expression</subject><subject>Proteins</subject><subject>Proteome - metabolism</subject><subject>proteomic</subject><subject>Proteomics</subject><subject>Receptor mechanisms</subject><subject>Scientific imaging</subject><subject>steroid hormone</subject><subject>Steroidogenesis</subject><subject>Testosterone</subject><subject>Trypsin</subject><subject>α2-Macroglobulin</subject><issn>0006-3363</issn><issn>1529-7268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqF0EtLxDAUBeAgijM-lm6l4EaQal6TJksRXzAgguKypMmtZEibmjaD_ns71Ae4cZVw-TgcDkJHBJ8TrNhF5YKPcOHCO-FyC83Jgqq8oEJuoznGWOSMCTZDe32_wphwRtkumlFFuKK8mKOXx6TbwQ16cGvIuhgGCI0zm1_tvGtfs1BnVVi7FrI6eO9M8jpmtU_OZjbFjZjuHjILa_Cha6AdDtBOrX0Ph1_vPnq-uX66usuXD7f3V5fLvOJUDTnFpjJaEMol5UoWRBeyAkM10dLU2IBQlRUcK6IYq7AoGFgLVmO10FZSy_bR6ZQ7Fn5L0A9l43oD3usWQupLooSgDC8KOdKTP3QVUmzHdiWVlEmmuFKjyidlYuj7CHXZRdfo-FESXG4WL6fFy2nx0R9_paaqAfujvyf-bRhS92_W2UTHc2jhH_0Jn1qcgQ</recordid><startdate>20171201</startdate><enddate>20171201</enddate><creator>Ferrazza, Rodrigo de Andrade</creator><creator>Garcia, Henry David Mogollón</creator><creator>Schmidt, Elizabeth Moreira dos Santos</creator><creator>Carmichael, Monika Mihm</creator><creator>Souza, Fabiana Ferreira de</creator><creator>Burchmore, Richard</creator><creator>Sartori, Roberto</creator><creator>Eckersall, Peter David</creator><creator>Ferreira, João Carlos Pinheiro</creator><general>Society for the Study of Reproduction</general><general>Oxford University Press</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20171201</creationdate><title>Quantitative proteomic profiling of bovine follicular fluid during follicle development</title><author>Ferrazza, Rodrigo de Andrade ; Garcia, Henry David Mogollón ; Schmidt, Elizabeth Moreira dos Santos ; Carmichael, Monika Mihm ; Souza, Fabiana Ferreira de ; Burchmore, Richard ; Sartori, Roberto ; Eckersall, Peter David ; Ferreira, João Carlos Pinheiro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-b429t-20cbca61248249871a78bec2a1a8cf0ce69bd64091933b0673eddeda095ad82d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>17β-Estradiol</topic><topic>Animals</topic><topic>Antithrombin</topic><topic>Apolipoproteins</topic><topic>Biological activity</topic><topic>Cattle</topic><topic>Complement activation</topic><topic>Developmental stages</topic><topic>Female</topic><topic>FEMALE REPRODUCTIVE TRACT</topic><topic>Fibrinogen</topic><topic>Follicles</topic><topic>Follicular fluid</topic><topic>Follicular Fluid - metabolism</topic><topic>Follicular Phase</topic><topic>folliculogenesis</topic><topic>Follistatin</topic><topic>Holstein cow</topic><topic>Immunoglobulins</topic><topic>Inhibin</topic><topic>Liquid chromatography</topic><topic>Liver X receptors</topic><topic>Mass spectrometry</topic><topic>Mass spectroscopy</topic><topic>Microenvironments</topic><topic>Nitric oxide</topic><topic>Ovarian Follicle - physiology</topic><topic>Progesterone</topic><topic>Protein expression</topic><topic>Proteins</topic><topic>Proteome - metabolism</topic><topic>proteomic</topic><topic>Proteomics</topic><topic>Receptor mechanisms</topic><topic>Scientific imaging</topic><topic>steroid hormone</topic><topic>Steroidogenesis</topic><topic>Testosterone</topic><topic>Trypsin</topic><topic>α2-Macroglobulin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ferrazza, Rodrigo de Andrade</creatorcontrib><creatorcontrib>Garcia, Henry David Mogollón</creatorcontrib><creatorcontrib>Schmidt, Elizabeth Moreira dos Santos</creatorcontrib><creatorcontrib>Carmichael, Monika Mihm</creatorcontrib><creatorcontrib>Souza, Fabiana Ferreira de</creatorcontrib><creatorcontrib>Burchmore, Richard</creatorcontrib><creatorcontrib>Sartori, Roberto</creatorcontrib><creatorcontrib>Eckersall, Peter David</creatorcontrib><creatorcontrib>Ferreira, João Carlos Pinheiro</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection (ProQuest)</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biology of reproduction</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ferrazza, Rodrigo de Andrade</au><au>Garcia, Henry David Mogollón</au><au>Schmidt, Elizabeth Moreira dos Santos</au><au>Carmichael, Monika Mihm</au><au>Souza, Fabiana Ferreira de</au><au>Burchmore, Richard</au><au>Sartori, Roberto</au><au>Eckersall, Peter David</au><au>Ferreira, João Carlos Pinheiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Quantitative proteomic profiling of bovine follicular fluid during follicle development</atitle><jtitle>Biology of reproduction</jtitle><addtitle>Biol Reprod</addtitle><date>2017-12-01</date><risdate>2017</risdate><volume>97</volume><issue>6</issue><spage>835</spage><epage>849</epage><pages>835-849</pages><issn>0006-3363</issn><eissn>1529-7268</eissn><abstract>Bovine follicular fluid (FF) constitutes the microenvironment of follicles and includes various biologically active proteins. We performed a study involving 18 healthy nonlactating Holstein cows to determine the protein expression profile of FF at key stages of follicular development. Follicles were individually aspirated in vivo at predeviation (F1 ∼ 7.0 mm), deviation (F1 ∼ 8.5 mm), postdeviation (F1 ∼ 12.0 mm), and preovulatory stages of follicle development, which were confirmed by measurement of follicular estradiol and progesterone concentrations. The FFs from nine cows were selected for proteomic analysis. After albumin depletion, triplicates of pooled FF were reduced, alkylated, and digested with trypsin. The resulting peptides were labeled with TMTsixplex and quantified using liquid chromatography-mass spectrometry/mass spectrometry. A total of 143 proteins were identified and assigned to a variety of biological processes, including response to stimulus and metabolic processes. Twenty-two differentially (P < 0.05) expressed proteins were found between stages indicating intrafollicular changes over development, with expected deviation time critical to modulate the protein expression. For instance, high concentrations of follistatin, inhibin, serglycin, spondin-1, fibrinogen, and anti-testosterone antibody were found during early stages of follicular development. In contrast, apolipoprotein H, alpha-2-macroglobulin, plasminogen, antithrombin-III, and immunoglobulins were increased after deviation. Among the differentially abundant proteins, 19 were found to be associated with steroidogenesis. Pathway analysis identified proteins that were mainly associated with the acute phase response signaling, coagulation system, complement system, liver/retinoid X receptor activation, and biosynthesis of nitric oxide and reactive oxygen. The differentially expressed proteins provide insights into the size-dependent protein changes in the ovarian follicle microenvironment that could influence follicular function. Summary Sentence The protein dynamic changes in ovarian follicle microenvironment during the follicle development are critical for follicular maturation and influence follicular function in cows.</abstract><cop>United States</cop><pub>Society for the Study of Reproduction</pub><pmid>29149247</pmid><doi>10.1093/biolre/iox148</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | 17β-Estradiol Animals Antithrombin Apolipoproteins Biological activity Cattle Complement activation Developmental stages Female FEMALE REPRODUCTIVE TRACT Fibrinogen Follicles Follicular fluid Follicular Fluid - metabolism Follicular Phase folliculogenesis Follistatin Holstein cow Immunoglobulins Inhibin Liquid chromatography Liver X receptors Mass spectrometry Mass spectroscopy Microenvironments Nitric oxide Ovarian Follicle - physiology Progesterone Protein expression Proteins Proteome - metabolism proteomic Proteomics Receptor mechanisms Scientific imaging steroid hormone Steroidogenesis Testosterone Trypsin α2-Macroglobulin |
| title | Quantitative proteomic profiling of bovine follicular fluid during follicle development |
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