A Guide to Zona Pellucida Domain Proteins by Eveline S. Litscher, Paul M. Wassarman

By Eveline S. Litscher, Paul M. Wassarman

This ebook offers a coherent, transparent, and uniform presentation of structural, genetic, molecular, and biochemical info to be had for the zona pellucida area protein relatives, which influence pathologies comparable to infertility, deafness, and melanoma. additionally 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 strength therapeutics for illnesses stemming from ZP area mutations
  • Addresses mammalian and non-mammalian systems

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Additional resources for A Guide to Zona Pellucida Domain Proteins

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1 Transmission electron micrographs of mouse ZP fibrils. Shown are (a) adsorbed, negatively stained, (b) sprayed, unidirectionally‐shadowed, and (c) freeze‐dried, unidirectionally‐ shadowed enzyme‐solubilized preparations of ZP fibrils. Reproduced with permission from Wassarman (1991). © Springer. proteins only occurs shortly before or just after the release of nascent mZP1–3 into the extracellular space. Nascent mZP2 and 3 are associated only with the innermost region of the thickening ZP, proximal to the oocyte’s plasma membrane.

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Mol Cell Biol 13, 530–541 (2002). Roller RJ, Wassarman PM. Role of asparagine‐linked oligosaccharides in secretion of ­glycoproteins of the mouse egg’s extracellular coat. J Biol Chem 258, 13243–13249 (1983). Salzmann GS, Greve JM, Roller RJ, Wassarman PM. Biosynthesis of the sperm receptor ­during oogenesis in the mouse. EMBO J 2, 1451–1456 (1983). Shimizu S, Tsuji M, Dean J. In vitro biosynthesis of three sulfated glycoproteins of murine zonae pellucidae by oocytes grown in follicle culture. J Biol Chem 258, 5858–5863 (1983).

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