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  • 1
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biochemistry 74 (2005), S. 83-114 
    ISSN: 0066-4154
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Chemistry and Pharmacology , Biology
    Notes: Many eukaryotic proteins share a sequence designated as the zona pellucida (ZP) domain. This structural element, present in extracellular proteins from a wide variety of organisms, from nematodes to mammals, consists of Đ♯260 amino acids with eight conserved cysteine (Cys) residues and is located close to the C terminus of the polypeptide. ZP domain proteins are often glycosylated, modular structures consisting of multiple types of domains. Predictions can be made about some of the structural features of the ZP domain and ZP domain proteins. The functions of ZP domain proteins vary tremendously, from serving as structural components of egg coats, appendicularian mucous houses, and nematode dauer larvae, to serving as mechanotransducers in flies and receptors in mammals and nonmammals. Generally, ZP domain proteins are present in filaments and/or matrices, which is consistent with the role of the domain in protein polymerization. A general mechanism for assembly of ZP domain proteins has been presented. It is likely that the ZP domain plays a common role despite its presence in proteins of widely diverse functions.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-9368
    Keywords: β-casein gene promoter ; early development ; milk‐mZP3 ; mZP3 gene ; transgenic mice
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mouse egg zona pellucida glycoprotein mZP3 (∼83 kDa Mr) serves as a species‐specific sperm receptor and acrosome reaction‐inducer during fertilization in mice. These biological activities are dependent on certain mZP3 serine/threonine‐ (O‐) linked oligosaccharides present at the combining‐site for sperm. In an attempt to produce large amounts of biologically active mZP3, we generated several transgenic mouse lines carrying the full‐length mZP3 gene fused to the β‐casein gene promoter and transcription termination sequence. We found that different transgenic mouse lines have different amounts of recombinant mZP3 (∼63 kDa Mr) in milk of lactating females, from ∼0.3 to 3.5 μg/μl of milk. In all cases, purified milk-mZP3 is active as a sperm receptor and acrosome reaction-inducer in vitro. Unexpectedly, we also found that development of litters from these transgenic mice is related to the amount of mZP3 in the mother's milk. In the most extreme case, litters from the highest expressers fail to live beyond about day-7 post partum unless placed immediately after birth with surrogate wild-type mothers. Litters from lower expressers initially display a complex phenotype that includes effects on hair and body growth, but some of the mice survive and, in time, are restored to a wild-type phenotype. These results demonstrate that relatively large amounts of biologically active mZP3 can be produced in transgenic mouse milk for structural and other studies, but that the presence of mZP3 in milk has dramatic developmental effects on litters, ranging from retarded hair and body growth to death of newborn pups.
    Type of Medium: Electronic Resource
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