{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,7,30]],"date-time":"2025-07-30T11:43:59Z","timestamp":1753875839862,"version":"3.41.2"},"reference-count":76,"publisher":"Oxford University Press (OUP)","license":[{"start":{"date-parts":[[2022,9,2]],"date-time":"2022-09-02T00:00:00Z","timestamp":1662076800000},"content-version":"am","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004543","name":"China Scholarship Council","doi-asserted-by":"publisher","award":["201606170117"],"award-info":[{"award-number":["201606170117"]}],"id":[{"id":"10.13039\/501100004543","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:title>Abstract<\/jats:title><jats:p>In a previous study, we reported that porcine sperm cysteine-rich secretory protein 2 (CRISP2) is localized in the post-acrosomal sheath-perinuclear theca (PT) as reduction-sensitive oligomers. In the current study, the decondensation and removal of CRISP2 was investigated during in vitro sperm capacitation, after both the induction of the acrosome reaction and in vitro fertilization. Confocal immunofluorescent imaging revealed that additional CRISP2 fluorescence appeared on the apical ridge and on the equatorial segment (EqS) of the sperm head following capacitation, likely due to cholesterol removal. After an ionophore A23187-induced acrosome reaction, CRISP2 immunofluorescence disappeared from the apical ridge and the EqS area partly not only owing to the removal of the acrosomal shroud vesicles, but to its presence in a subdomain of EqS. The fate of sperm head CRISP2 was further examined post-fertilization. In vitro matured porcine oocytes were co-incubated with boar sperm cells for 6\u20138\u00a0h and the zygotes were processed for CRISP2 immunofluorescent staining. Notably, decondensation of CRISP2, and thus of the sperm PT, occurred while the sperm nucleus was still fully condensed. CRISP2 was no longer detectable in fertilized oocytes in which sperm nuclear decondensation and paternal pronucleus formation were apparent. This rapid dispersal of CRISP2 in the PT is likely regulated by redox reactions for which its cysteine-rich domain is sensitive. Reduction of disulfide bridges within CRISP2 oligomers may be instrumental for PT dispersal and elimination.<\/jats:p>","DOI":"10.1093\/biolre\/ioac169","type":"journal-article","created":{"date-parts":[[2022,9,2]],"date-time":"2022-09-02T17:59:15Z","timestamp":1662141555000},"source":"Crossref","is-referenced-by-count":0,"title":["The fate of porcine sperm CRISP2 from the perinuclear theca before and after in vitro fertilization"],"prefix":"10.1093","author":[{"given":"Min","family":"Zhang","sequence":"first","affiliation":[{"name":"Department of Biomolecular Health Sciences , Faculty of Veterinary Medicine, , the Netherlands"},{"name":"Utrecht University , Faculty of Veterinary Medicine, , the Netherlands"},{"name":"Department of Farm Animal Health , Faculty of Veterinary Medicine, , Utrecht , the Netherlands"},{"name":"Utrecht University , Faculty of Veterinary Medicine, , Utrecht , the Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Elizabeth G","family":"Bromfield","sequence":"additional","affiliation":[{"name":"Department of Biomolecular Health Sciences , Faculty of Veterinary Medicine, , the Netherlands"},{"name":"Utrecht University , Faculty of Veterinary Medicine, , the Netherlands"},{"name":"Priority Research Centre for Reproductive Science, The University of Newcastle , New South Wales , Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J Bernd","family":"Helms","sequence":"additional","affiliation":[{"name":"Department of Biomolecular Health Sciences , Faculty of Veterinary Medicine, , the Netherlands"},{"name":"Utrecht University , Faculty of Veterinary Medicine, , the Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bart M","family":"Gadella","sequence":"additional","affiliation":[{"name":"Department of Biomolecular Health Sciences , Faculty of Veterinary Medicine, , the Netherlands"},{"name":"Utrecht University , Faculty of Veterinary Medicine, , the Netherlands"},{"name":"Department of Farm Animal Health , Faculty of Veterinary Medicine, , Utrecht , the Netherlands"},{"name":"Utrecht University , Faculty of Veterinary Medicine, , Utrecht , the Netherlands"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2022,9,2]]},"reference":[{"key":"2022100413002180500_ref1","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1038\/181851a0","article-title":"Capacitation of mammalian spermatozoa","volume":"181","author":"Austin","year":"1958","journal-title":"Nature"},{"key":"2022100413002180500_ref2","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1038\/200281b0","article-title":"Fertilization of hamster eggs in vitro","volume":"200","author":"Yanagimachi","year":"1963","journal-title":"Nature"},{"key":"2022100413002180500_ref3","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1073\/pnas.0811895106","article-title":"Understanding the molecular basis of sperm capacitation through kinase design","volume":"106","author":"Visconti","year":"2009","journal-title":"Proc Natl Acad Sci USA"},{"key":"2022100413002180500_ref4","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1007\/978-94-007-0763-4_5","article-title":"Membrane fusions during mammalian fertilization","volume":"713","author":"Gadella","year":"2011","journal-title":"Adv Exp Med Biol"},{"key":"2022100413002180500_ref5","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1242\/jcs.108.3.935","article-title":"Glycolipid migration from the apical to the equatorial subdomains of the sperm head plasma membrane precedes the acrosome reaction. 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