Abstract

The long-term objective of this research is to define the molecular mechanisms of sperm and egg interactions operative in fertilization.
The specific aims during this grant period are: 1) Identify and define the molecular mechanism responsible for egg envelope transformations that underlie the ultrastructural and sperm penetrability changes in egg envelopes isolated from the frog, Xenopus laevis. The oviducal and egg cortical granule constituents responsible for these changes, presumably enzymes, will be isolated. In vitro envelope transformations will be effected using the isolated enzymes. 2) The glycoprotein envelope components that function as ligands for sperm receptors will be identified. Methodologically, binding of isolated 125I-envelope components and chemical cross-linking of sperm receptor-envelope ligand using bifunctional protein reagents will be used to ascertain the binding partners. Gametes from Xenopus laevis and from the domestic pig, Sous crofa, will be used. 3) We will continue the chemical characterization of the glycoproteins composing the pig zona pellucida and identify which components are antigenic. The zona pellucida components will be isolated and their antigenicity determined using monoclonal antibody techniques. Correlation of the structural and functional properties of the zona pellucida glycoproteins will provide information that can be used to control sperm-egg interactions.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
Eunice Kennedy Shriver National Institute of Child Health & Human Development (NICHD)
Type
Research Project (R01)
Project #
5R01HD004906-16
Application #
3310336
Study Section
Cellular Biology and Physiology Subcommittee 1 (CBY)
Project Start
1975-05-01
Project End
1988-06-30
Budget Start
1985-07-01
Budget End
1986-06-30
Support Year
16
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of California Davis
Department
Type
Earth Sciences/Resources
DUNS #
094878337
City
Davis
State
CA
Country
United States
Zip Code
95618

  Publications

Chang, Betty Y; Peavy, Thomas R; Wardrip, Nathan J et al. (2004) The Xenopus laevis cortical granule lectin: cDNA cloning, developmental expression, and identification of the eglectin family of lectins. Comp Biochem Physiol A Mol Integr Physiol 137:115-29
Lindsay, L L; Yang, J C; Hedrick, J L (1999) Ovochymase, a Xenopus laevis egg extracellular protease, is translated as part of an unusual polyprotease. Proc Natl Acad Sci U S A 96:11253-8
Lindsay, L L; Wieduwilt, M J; Hedrick, J L (1999) Oviductin, the Xenopus laevis oviductal protease that processes egg envelope glycoprotein gp43, increases sperm binding to envelopes, and is translated as part of an unusual mosaic protein composed of two protease and several CUB domains. Biol Reprod 60:989-95
Yang, J C; Hedrick, J L (1997) cDNA cloning and sequence analysis of the Xenopus laevis egg envelope glycoprotein gp43. Dev Growth Differ 39:457-67
Hedrick, J L (1996) Comparative structural and antigenic properties of zona pellucida glycoproteins. J Reprod Fertil Suppl 50:9-17
Quill, T A; Hedrick, J L (1996) The fertilization layer mediated block to polyspermy in Xenopus laevis: isolation of the cortical granule lectin ligand. Arch Biochem Biophys 333:326-32
Lindsay, L L; Hedrick, J L (1995) Isolation and characterization of ovochymase, a chymotrypsin-like protease released during Xenopus laevis egg activation. Dev Biol 167:513-6
Hardy, D M; Hedrick, J L (1992) Oviductin. Purification and properties of the oviductal protease that processes the molecular weight 43,000 glycoprotein of the Xenopus laevis egg envelope. Biochemistry 31:4466-72
Lindsay, L L; Larabell, C A; Hedrick, J L (1992) Localization of a chymotrypsin-like protease to the perivitelline space of Xenopus laevis eggs. Dev Biol 154:433-6
Hedrick, J L; Hardy, D M (1991) Isolation of extracellular matrix structures from Xenopus laevis oocytes, eggs, and embryos. Methods Cell Biol 36:231-47

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