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Molecular cloning and characterization of three distinct choriogenins in masu salmon, Oncorhynchus masou
Author(s) -
Fujita Toshiaki,
Fukada Haruhisa,
Shimizu Munetaka,
Hiramatsu Naoshi,
Hara Akihiko
Publication year - 2008
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/mrd.20857
Subject(s) - biology , complementary dna , oncorhynchus , cloning (programming) , molecular cloning , gene , recombinant dna , cdna library , molecular mass , microbiology and biotechnology , clone (java method) , genetics , biochemistry , fish <actinopterygii> , enzyme , fishery , computer science , programming language
Three cDNAs, each encoding a different choriogenin (Chg), were isolated from a female masu salmon ( Oncorhynchus masou ) liver cDNA library. Two of the cDNA clones, Chg Hα and Chg Hβ , showed a close relationship and contained the typical domains of zona pellucida (ZP) B genes in fish, namely proline and glutamine rich repeats, a trefoil factor family domain, and a ZP domain. Specific antibodies against recombinant Chg H products ( rmHα and rmHβ ) were generated to elucidate the relationship between the Chg H cDNAs and two types of serum Chg H protein, which were previously purified and characterized, and designated as very‐high‐molecular‐weight vitelline envelope‐related protein ( vhVERP ) and Chg H of masu salmon. The immunobiochemical analyses revealed that the Chg Hα and Chg Hβ clones encoded vhVERP and Chg H proteins, respectively. The third cDNA clone (Chg L) appeared to be a ZPC gene and, by mapping the N‐terminal sequence of purified Chg L, was shown to encode serum Chg L protein. Various types of heteromultimer of the three Chgs were identified immunologically as high molecular weight chorion components, indicating the involvement of complex heterodimerization of multiple Chgs in the construction of chorion architecture in masu salmon. Mol. Reprod. Dev. 75: 1217–1228, 2008. © 2008 Wiley‐Liss, Inc.