By Eveline S. Litscher, Paul M. Wassarman

This publication offers a coherent, transparent, and uniform presentation of structural, genetic, molecular, and biochemical info on hand for the zona pellucida area protein kinfolk, which influence pathologies akin to infertility, deafness, and melanoma. moreover it:

  • Details information regarding the constitution and serve as of the ZP area in ZPDC-proteins
  • Provides illustrations of the association of ZPDC-proteins, the genes that encode the proteins, and examples of mutations within the ZP area that reason diseases
  • Speculates as to the evolution of the ZP area and power therapeutics for illnesses stemming from ZP area mutations
  • Addresses mammalian and non-mammalian systems

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Additional info for A Guide to Zona Pellucida Domain Proteins

Sample text

Messenger‐ RNA encoding mouse ZP proteins is undetectable in non‐growing oocytes but appears in small oocytes that have entered the growth phase. For example, messenger‐RNA encoding mZP3 is undetectable in non‐growing oocytes but increases to ≃300,000 copies/oocyte in mid‐stage growing oocytes, falls to ≃240,000 copies/oocyte in fully‐grown oocytes, and decreases to undetectable levels in fertilized eggs (<1000 copies/egg). During oocyte growth, a period of ≃2–3 weeks in mice, ZP protein synthesis represents ≃5% of total protein synthesis by the oocyte.

ZP1–4 are found in mammals and other vertebrates, ZPd in amphibians and birds, and ZPax in fish, amphibians, and birds. , comparable locations are referred to as synteny). In addition, several ZP pseudogenes have been identified in mammals, for example, a ZP4 pseudogene in mice and ZP1 pseudogene in dogs and cows. Highly divergent sequences have been identified in ZP2 and 3. In mZP3, there are two clusters of sites—N‐terminal (aa 25–50) and C‐terminal (aa 331–373)—to the 20 ZONA PELLUCIDA DOMAIN PROTEINS ZPD that are under positive selection.

P......... DQSYQRPY a Shown are partial sequences from trout (Oncorhynchus mykiss) ZP1α/ZP1β with Cx and Cy and partial sequences of mZP1/mZP2 for comparison. 9). However, no disulfide assignments have been made for the extra Cys residues of these ZP1/2‐like proteins. Cys residue clustering in ZP‐C sub‐domains is variable in chicken and pig ZP3; there is a disulfide linkage to a Cys residue C‐terminal to the ZPD, 6,11 and 8,9, whereas in mZP3 it is 6,8 and 9,11. It is likely that these two ­different disulfide bonding patterns cause the polypeptides to adopt different conformations that may determine the specificity of egg coat assembly in ­different species.

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