Phosphoproteomics for the identification of new mechanisms of cryodamage: the role of SPATA18 in the control of stallion sperm function
Although recent research has addressed the impact of cryopreservation on the stallion sperm proteome, studies addressing the stallion sperm phosphoproteome are lacking. In the present study, the data set of proteomes of fresh and cryopreserved spermatozoa were reanalyzed, showing that cryopreservati...
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| Veröffentlicht in: | Biology of reproduction 2023-02, Vol.108 (2), p.1-14 |
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| creator | Gaitskell-Phillips, Gemma Martín-Cano, Francisco E. da Silva-Álvarez, Eva Tapia, José A Silva, Antonio Gil, María C. Ortega-Ferrusola, Cristina Peña, Fernando J. |
| description | Although recent research has addressed the impact of cryopreservation on the stallion sperm proteome, studies addressing the stallion sperm phosphoproteome are lacking. In the present study, the data set of proteomes of fresh and cryopreserved spermatozoa were reanalyzed, showing that cryopreservation caused significant changes in the phosphoproteome. The phosphoproteins reduced most significantly by cryopreservation were Ca2+ binding tyrosine phosphorylation regulated, protein kinase cAMP-activated catalytic subunit beta (CABYR), mitochondria eating protein (SPATA18), A kinase anchoring protein 4 (AKAP4), A-kinase anchoring protein 3 (AKAP3) and the Family with sequence similarity 71 member B (FAM71B). These proteins belong to the gene ontology (GO) terms sperm fibrous sheath (GO: 0035686), and sperm principal piece (GO: 0097228). The regulatory interactions between kinases and phosphorylation sites on the proteins that were affected most were also investigated, and the potential kinases (based on human orthologs) involved in the regulation of these phosphoproteins identified were: PKCß for SPATA18 and GSK3ß for CABYR. Kinase inhibition assays were also conducted showing that kinases phosphorylating the above-mentioned proteins play an important role in their activity and thus, phosphorylation controls the activity of these proteins and their role in the regulation of the functionality and viability of stallion spermatozoa. In conclusion, the data reported here contribute to the understanding of the fact that the dephosphorylation of certain proteins is a molecular lesion induced by cryopreservation in the stallion spermatozoa. Graphical Abstract |
| doi_str_mv | 10.1093/biolre/ioac211 |
| format | Article |
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In the present study, the data set of proteomes of fresh and cryopreserved spermatozoa were reanalyzed, showing that cryopreservation caused significant changes in the phosphoproteome. The phosphoproteins reduced most significantly by cryopreservation were Ca2+ binding tyrosine phosphorylation regulated, protein kinase cAMP-activated catalytic subunit beta (CABYR), mitochondria eating protein (SPATA18), A kinase anchoring protein 4 (AKAP4), A-kinase anchoring protein 3 (AKAP3) and the Family with sequence similarity 71 member B (FAM71B). These proteins belong to the gene ontology (GO) terms sperm fibrous sheath (GO: 0035686), and sperm principal piece (GO: 0097228). The regulatory interactions between kinases and phosphorylation sites on the proteins that were affected most were also investigated, and the potential kinases (based on human orthologs) involved in the regulation of these phosphoproteins identified were: PKCß for SPATA18 and GSK3ß for CABYR. Kinase inhibition assays were also conducted showing that kinases phosphorylating the above-mentioned proteins play an important role in their activity and thus, phosphorylation controls the activity of these proteins and their role in the regulation of the functionality and viability of stallion spermatozoa. In conclusion, the data reported here contribute to the understanding of the fact that the dephosphorylation of certain proteins is a molecular lesion induced by cryopreservation in the stallion spermatozoa. Graphical Abstract</description><identifier>ISSN: 0006-3363</identifier><identifier>EISSN: 1529-7268</identifier><identifier>DOI: 10.1093/biolre/ioac211</identifier><identifier>PMID: 36468681</identifier><language>eng</language><publisher>United States: Society for the Study of Reproduction</publisher><subject>A Kinase Anchor Proteins ; A kinase-anchoring protein ; Animals ; Cryopreservation ; Cryopreservation - veterinary ; Dephosphorylation ; Horses ; Humans ; Kinases ; Male ; Phosphoproteins ; Phosphoproteins - genetics ; Phosphoproteins - metabolism ; phosphoproteomics ; Phosphorylation ; Protein kinase C ; Proteins ; Proteomes ; reproduction ; RESEARCH ARTICLE ; Semen - metabolism ; Semen Preservation - veterinary ; Sperm ; Sperm Motility - physiology ; Sperm Tail - metabolism ; spermatozoa ; Spermatozoa - metabolism ; Tyrosine</subject><ispartof>Biology of reproduction, 2023-02, Vol.108 (2), p.1-14</ispartof><rights>The Author(s) 2022. 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) 2022. 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 2022</rights><rights>The Author(s) 2022. 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) 2022. 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><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-b394t-f4287f9c1c945a265c3280d9e745e5705255987f9124786f46dff0bd176592843</citedby><cites>FETCH-LOGICAL-b394t-f4287f9c1c945a265c3280d9e745e5705255987f9124786f46dff0bd176592843</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1578,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36468681$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gaitskell-Phillips, Gemma</creatorcontrib><creatorcontrib>Martín-Cano, Francisco E.</creatorcontrib><creatorcontrib>da Silva-Álvarez, Eva</creatorcontrib><creatorcontrib>Tapia, José A</creatorcontrib><creatorcontrib>Silva, Antonio</creatorcontrib><creatorcontrib>Gil, María C.</creatorcontrib><creatorcontrib>Ortega-Ferrusola, Cristina</creatorcontrib><creatorcontrib>Peña, Fernando J.</creatorcontrib><title>Phosphoproteomics for the identification of new mechanisms of cryodamage: the role of SPATA18 in the control of stallion sperm function</title><title>Biology of reproduction</title><addtitle>Biol Reprod</addtitle><description>Although recent research has addressed the impact of cryopreservation on the stallion sperm proteome, studies addressing the stallion sperm phosphoproteome are lacking. In the present study, the data set of proteomes of fresh and cryopreserved spermatozoa were reanalyzed, showing that cryopreservation caused significant changes in the phosphoproteome. The phosphoproteins reduced most significantly by cryopreservation were Ca2+ binding tyrosine phosphorylation regulated, protein kinase cAMP-activated catalytic subunit beta (CABYR), mitochondria eating protein (SPATA18), A kinase anchoring protein 4 (AKAP4), A-kinase anchoring protein 3 (AKAP3) and the Family with sequence similarity 71 member B (FAM71B). These proteins belong to the gene ontology (GO) terms sperm fibrous sheath (GO: 0035686), and sperm principal piece (GO: 0097228). The regulatory interactions between kinases and phosphorylation sites on the proteins that were affected most were also investigated, and the potential kinases (based on human orthologs) involved in the regulation of these phosphoproteins identified were: PKCß for SPATA18 and GSK3ß for CABYR. Kinase inhibition assays were also conducted showing that kinases phosphorylating the above-mentioned proteins play an important role in their activity and thus, phosphorylation controls the activity of these proteins and their role in the regulation of the functionality and viability of stallion spermatozoa. In conclusion, the data reported here contribute to the understanding of the fact that the dephosphorylation of certain proteins is a molecular lesion induced by cryopreservation in the stallion spermatozoa. Graphical Abstract</description><subject>A Kinase Anchor Proteins</subject><subject>A kinase-anchoring protein</subject><subject>Animals</subject><subject>Cryopreservation</subject><subject>Cryopreservation - veterinary</subject><subject>Dephosphorylation</subject><subject>Horses</subject><subject>Humans</subject><subject>Kinases</subject><subject>Male</subject><subject>Phosphoproteins</subject><subject>Phosphoproteins - genetics</subject><subject>Phosphoproteins - metabolism</subject><subject>phosphoproteomics</subject><subject>Phosphorylation</subject><subject>Protein kinase C</subject><subject>Proteins</subject><subject>Proteomes</subject><subject>reproduction</subject><subject>RESEARCH ARTICLE</subject><subject>Semen - metabolism</subject><subject>Semen Preservation - veterinary</subject><subject>Sperm</subject><subject>Sperm Motility - physiology</subject><subject>Sperm Tail - metabolism</subject><subject>spermatozoa</subject><subject>Spermatozoa - metabolism</subject><subject>Tyrosine</subject><issn>0006-3363</issn><issn>1529-7268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkU1rFTEUhoMo9rZ161IG3Cg4bb4_3F2KtULBQut6yM2ceFNmkjGZQfoL_Nud6VxduOkq8J7nPOTwIvSW4DOCDTvfhdRlOA_JOkrIC7QhgppaUalfog3GWNaMSXaEjku5x5hwRtlrdMQkl1pqskF_bvapDPs05DRC6oMrlU-5GvdQhRbiGHxwdgwpVslXEX5XPbi9jaH0ZUlcfkit7e1P-Py0k1MHS357s73bEl2F-BS7FMd5tEzKaLtu8ZUBcl_5KbpFf4peedsVeHN4T9CPyy93F1f19fev3y621_WOGT7WnlOtvHHEGS4slcIxqnFrQHEBQmFBhTALQShXWnouW-_xriVKCkM1Zyfow-qdD_41QRmbPhQHXWcjpKk0VHGFMROGzej7_9D7NOU4_66hmjLNjMJ0ps5WyuVUSgbfDDn0Nj80BDdLRc1aUXOoaF54d9BOux7af_jfTmbg4wqkaXhe9mll5zxFeA5_BGfYrCA</recordid><startdate>20230213</startdate><enddate>20230213</enddate><creator>Gaitskell-Phillips, Gemma</creator><creator>Martín-Cano, Francisco E.</creator><creator>da Silva-Álvarez, Eva</creator><creator>Tapia, José A</creator><creator>Silva, Antonio</creator><creator>Gil, María C.</creator><creator>Ortega-Ferrusola, Cristina</creator><creator>Peña, Fernando J.</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>20230213</creationdate><title>Phosphoproteomics for the identification of new mechanisms of cryodamage: the role of SPATA18 in the control of stallion sperm function</title><author>Gaitskell-Phillips, Gemma ; 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In the present study, the data set of proteomes of fresh and cryopreserved spermatozoa were reanalyzed, showing that cryopreservation caused significant changes in the phosphoproteome. The phosphoproteins reduced most significantly by cryopreservation were Ca2+ binding tyrosine phosphorylation regulated, protein kinase cAMP-activated catalytic subunit beta (CABYR), mitochondria eating protein (SPATA18), A kinase anchoring protein 4 (AKAP4), A-kinase anchoring protein 3 (AKAP3) and the Family with sequence similarity 71 member B (FAM71B). These proteins belong to the gene ontology (GO) terms sperm fibrous sheath (GO: 0035686), and sperm principal piece (GO: 0097228). The regulatory interactions between kinases and phosphorylation sites on the proteins that were affected most were also investigated, and the potential kinases (based on human orthologs) involved in the regulation of these phosphoproteins identified were: PKCß for SPATA18 and GSK3ß for CABYR. Kinase inhibition assays were also conducted showing that kinases phosphorylating the above-mentioned proteins play an important role in their activity and thus, phosphorylation controls the activity of these proteins and their role in the regulation of the functionality and viability of stallion spermatozoa. In conclusion, the data reported here contribute to the understanding of the fact that the dephosphorylation of certain proteins is a molecular lesion induced by cryopreservation in the stallion spermatozoa. Graphical Abstract</abstract><cop>United States</cop><pub>Society for the Study of Reproduction</pub><pmid>36468681</pmid><doi>10.1093/biolre/ioac211</doi><tpages>14</tpages></addata></record> |
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| ispartof | Biology of reproduction, 2023-02, Vol.108 (2), p.1-14 |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | A Kinase Anchor Proteins A kinase-anchoring protein Animals Cryopreservation Cryopreservation - veterinary Dephosphorylation Horses Humans Kinases Male Phosphoproteins Phosphoproteins - genetics Phosphoproteins - metabolism phosphoproteomics Phosphorylation Protein kinase C Proteins Proteomes reproduction RESEARCH ARTICLE Semen - metabolism Semen Preservation - veterinary Sperm Sperm Motility - physiology Sperm Tail - metabolism spermatozoa Spermatozoa - metabolism Tyrosine |
| title | Phosphoproteomics for the identification of new mechanisms of cryodamage: the role of SPATA18 in the control of stallion sperm function |
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