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4. From Peptide Masses to Pregnancy Maintenance: A Comprehensive Proteomic Analysis of The Early Equine Embryo Secretome, Blastocoel Fluid, and Capsule

Author

Swegen, Aleona, Grupen, Christopher Gerald, Gibb, Zamira, Baker, Mark, de Ruijter - Villani, Marta, Smith, Nathan Druery, Stout, Tom, Aitken, R John, dES/dFAH FR, and LS Voortplanting Inwendige Ziekten

Subjects
0301 basic medicine, Proteomics, medicine.medical_specialty, animal structures, media_common.quotation_subject, Early Pregnancy Loss, Biology, Endometrium, Biochemistry, Pregnancy Maintenance, Andrology, 03 medical and health sciences, Pregnancy, Internal medicine, medicine, Animals, Blastocyst, Horses, Molecular Biology, Ovulation, media_common, Blastocoel, Embryo, medicine.disease, Embryo, Mammalian, Peptide Fragments, 030104 developmental biology, medicine.anatomical_structure, Endocrinology, embryonic structures, Female
Abstract

Early pregnancy in the mare is a poorly understood, high risk period during which the embryo communicates its presence to the maternal endometrium. Remarkably, the maternal recognition of pregnancy signal is unknown in the horse. This study aimed to profile the proteins secreted by equine blastocysts into their immediate environment, along with proteins contained in the blastocoel and within the acellular embryo capsule. Embryos were recovered on day 8 after ovulation and cultured for 48 hours. Secretomes of day 9 and day 10 embryos were analyzed by LC-MS/MS and supported by analysis of blastocoel fluid and embryo capsule. Analyses revealed 72 (24 h) and 97 (48 h) unique protein IDs in the embryo secretome, 732 protein IDs in blastocoel fluid, and 11 proteins IDs in the embryo capsule. Novel findings of interest include secretion of a pregnancy specific proteinase (PAG) by the equine embryo at day 10, along with detection of a prostaglandin receptor inhibiting protein (PTGFRN) and a progesterone potentiating factor (FKBP4) in blastocoel fluid. This is the first comprehensive proteomic analysis of the equine embryo secretome, and provides new insights into the unique physiology of early pregnancy in this species. This article is protected by copyright. All rights reserved

Published
2016

7. The HUPO initiative on Model Organism Proteomes, iMOP

Author

Jones, Alexandra M. E., primary, Aebersold, Ruedi, additional, Ahrens, Christian H., additional, Apweiler, Rolf, additional, Baerenfaller, Katja, additional, Baker, Mark, additional, Bendixen, Emøke, additional, Briggs, Steve, additional, Brownridge, Philip, additional, Brunner, Erich, additional, Daube, Michael, additional, Deutsch, Eric W., additional, Grossniklaus, Ueli, additional, Heazlewood, Joshua, additional, Hengartner, Michael O., additional, Hermjakob, Henning, additional, Jovanovic, Marko, additional, Lawless, Craig, additional, Lochnit, Günter, additional, Martens, Lennart, additional, Ravnsborg, Christian, additional, Schrimpf, Sabine P., additional, Shim, Yhong‐Hee, additional, Subasic, Deni, additional, Tholey, Andreas, additional, van Wijk, Klaas, additional, von Mering, Christian, additional, Weiss, Manuel, additional, and Zheng, Xue, additional

Published
2012
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8. Recommendations for mass spectrometry data quality metrics for open access data (corollary to the Amsterdam principles)

Author

Kinsinger, Christopher R., primary, Apffel, James, additional, Baker, Mark, additional, Bian, Xiaopeng, additional, Borchers, Christoph H., additional, Bradshaw, Ralph, additional, Brusniak, Mi-Youn, additional, Chan, Daniel W., additional, Deutsch, Eric W., additional, Domon, Bruno, additional, Gorman, Jeff, additional, Grimm, Rudolf, additional, Hancock, William, additional, Hermjakob, Henning, additional, Horn, David, additional, Hunter, Christie, additional, Kolar, Patrik, additional, Kraus, Hans-Joachim, additional, Langen, Hanno, additional, Linding, Rune, additional, Moritz, Robert L., additional, Omenn, Gilbert S., additional, Orlando, Ron, additional, Pandey, Akhilesh, additional, Ping, Peipei, additional, Rahbar, Amir, additional, Rivers, Robert, additional, Seymour, Sean L., additional, Simpson, Richard J., additional, Slotta, Douglas, additional, Smith, Richard D., additional, Stein, Stephen E., additional, Tabb, David L., additional, Tagle, Danilo, additional, Yates, John R., additional, and Rodriguez, Henry, additional

Published
2011
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10. The Asia Oceania Human Proteome Organisation Membrane Proteomics Initiative. Preparation and characterisation of the carbonate-washed membrane standard

Author

Peng, Lifeng, primary, Kapp, Eugene A., additional, Fenyö, David, additional, Kwon, Min-Seok, additional, Jiang, Pu, additional, Wu, Songfeng, additional, Jiang, Ying, additional, Aguilar, Marie-Isabel, additional, Ahmed, Nikhat, additional, Baker, Mark S., additional, Cai, Zongwei, additional, Chen, Yu-Ju, additional, Van Chi, Phan, additional, Chung, Maxey C. M., additional, He, Fuchu, additional, Len, Alice C. L., additional, Liao, Pao-Chi, additional, Nakamura, Kazuyuki, additional, Ngai, Sai Ming, additional, Paik, Young-Ki, additional, Pan, Tai-Long, additional, Poon, Terence C. W., additional, Hosseini Salekdeh, Ghasem, additional, Simpson, Richard J., additional, Sirdeshmukh, Ravi, additional, Srisomsap, Chantragan, additional, Svasti, Jisnuson, additional, Tyan, Yu-Chang, additional, Dreyer, Florian S., additional, McLauchlan, Danyl, additional, Rawson, Pisana, additional, and Jordan, T. William, additional

Published
2010
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16. Recommendations for mass spectrometry data quality metrics for open access data (corollary to the Amsterdam principles).

Author

Kinsinger, Christopher R., Apffel, James, Baker, Mark, Bian, Xiaopeng, Borchers, Christoph H., Bradshaw, Ralph, Brusniak, Mi-Youn, Chan, Daniel W., Deutsch, Eric W., Domon, Bruno, Gorman, Jeff, Grimm, Rudolf, Hancock, William, Hermjakob, Henning, Horn, David, Hunter, Christie, Kolar, Patrik, Kraus, Hans-Joachim, Langen, Hanno, and Linding, Rune

Published
2012
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18. Evaluation of blood collection tubes using selected reaction monitoring MS: implications for proteomic biomarker studies.

Author

Randall SA, McKay MJ, Baker MS, and Molloy MP

Subjects
Biomarkers blood, Humans, Blood Specimen Collection, Mass Spectrometry methods, Proteomics methods
Abstract

An emphasis of current proteomic research is the validation of plasma protein biomarkers. The process of blood collection itself is critical to the accuracy and reproducibility of quantitative biomarker assays. We have developed selected reaction monitoring (SRM) assays to analyse thirteen abundant plasma proteins and evaluated the impact of three different blood collection tubes on the levels of these proteins. We also assessed the implications of the time taken to analyse plasma samples by evaluating the recovery of these proteins. We showed that SRM detects minor differences in the levels of some proteins which can be attributed to collection tube type. The average recovery for 12 of 18 assays was higher for proteins that were collected in tubes containing protease inhibitors compared to conventional collection tubes. For five of the assays, the differential recovery was statistically significant. Delaying MS analysis of a freeze-thawed sample for 1 hour showed greatly reduced recovery of these analytes; however differences attributed to tube type were only evident at the baseline timepoint. Finally, we assessed the natural variation of circulating levels of these proteins in a cohort of seven healthy individuals. This study provides useful information for researchers contemplating blood collection for undertaking protein biomarker studies.

Published
2010
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