Gutenberg Open Science: Substrate profiling of the metalloproteinase ovastacin uncovers specific enzyme–substrate interactions and discloses fertilization-relevant substrates

Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-9911

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DC Field	Value	Language
dc.contributor.author	Felten, Matthias	-
dc.contributor.author	Distler, Ute	-
dc.contributor.author	Wiegen, Nele von	-
dc.contributor.author	Łacki, Mateusz	-
dc.contributor.author	Behl, Christian	-
dc.contributor.author	Tenzer, Stefan	-
dc.contributor.author	Stöcker, Walter	-
dc.contributor.author	Körschgen, Hagen	-
dc.date.accessioned	2024-01-08T08:51:52Z	-
dc.date.available	2024-01-08T08:51:52Z	-
dc.date.issued	2023	-
dc.identifier.uri	https://openscience.ub.uni-mainz.de/handle/20.500.12030/9929	-
dc.description.abstract	The metalloproteinase ovastacin is released by the mammalian egg upon fertilization and cleaves a distinct peptide bond in zona pellucida protein 2 (ZP2), a component of the enveloping extracellular matrix. This limited proteolysis causes zona pellucida hardening, abolishes sperm binding, and thereby regulates fertility. Accordingly, this process is tightly controlled by the plasma protein fetuin-B, an endogenous competitive inhibitor. At present, little is known about how the cleavage characteristics of ovastacin differ from closely related proteases. Physiological implications of ovastacin beyond ZP2 cleavage are still obscure. In this study, we employed N-terminal amine isotopic labeling of substrates (N-TAILS) contained in the secretome of mouse embryonic fibroblasts to elucidate the substrate specificity and the precise cleavage site specificity. Furthermore, we were able to unravel the physicochemical properties governing ovastacin–substrate interactions as well as the individual characteristics that distinguish ovastacin from similar proteases, such as meprins and tolloid. Eventually, we identified several substrates whose cleavage could affect mammalian fertilization. Consequently, these substrates indicate newly identified functions of ovastacin in mammalian fertilization beyond zona pellucida hardening.	en_GB
dc.language.iso	eng	de
dc.rights	CC BY	*
dc.rights.uri	https://creativecommons.org/licenses/by/4.0/	*
dc.subject.ddc	610 Medizin	de_DE
dc.subject.ddc	610 Medical sciences	en_GB
dc.title	Substrate profiling of the metalloproteinase ovastacin uncovers specific enzyme–substrate interactions and discloses fertilization-relevant substrates	en_GB
dc.type	Zeitschriftenaufsatz	de
dc.identifier.doi	http://doi.org/10.25358/openscience-9911	-
jgu.type.dinitype	article	en_GB
jgu.type.version	Published version	de
jgu.type.resource	Text	de
jgu.organisation.department	FB 04 Medizin	de
jgu.organisation.number	2700	-
jgu.organisation.name	Johannes Gutenberg-Universität Mainz	-
jgu.rights.accessrights	openAccess	-
jgu.journal.title	The FEBS journal	de
jgu.journal.volume	291	de
jgu.journal.issue	1	de
jgu.pages.start	114	de
jgu.pages.end	131	de
jgu.publisher.year	2024	-
jgu.publisher.name	Wiley-Blackwell	de
jgu.publisher.place	Oxford u.a.	de
jgu.publisher.issn	1742-464X	de
jgu.organisation.place	Mainz	-
jgu.subject.ddccode	610	de
jgu.publisher.doi	10.1111/febs.16954	de
jgu.organisation.ror	https://ror.org/023b0x485	-
Appears in collections:	DFG-491381577-H

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