ArticleProceedings of the National Academy of Sciences of the United States of America1999
Xenopus laevis sperm receptor gp69/64 glycoprotein is a homolog of the mammalian sperm receptor ZP2.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 80 citations in OpenAlex.
- Article
- Mammalian egg coat modifications and the block to polyspermy.Molecular reproduction and development · 2020Review
- Egg Coat Proteins Across Metazoan Evolution.Current topics in developmental biology · 2018Review
- Sperm-Egg Interaction during Fertilization in Birds.The journal of poultry science · 2016Review
- Dicalcin, a zona pellucida protein that regulates fertilization competence of the egg coat in Xenopus laevis.The journal of physiological sciences : JPS · 2015Review
- Protein-Carbohydrate Interaction between Sperm and the Egg-Coating Envelope and Its Regulation by Dicalcin, a Xenopus laevis Zona Pellucida Protein-Associated Protein.Molecules (Basel, Switzerland) · 2015Review
- Phospholipase C and D regulation of Src, calcium release and membrane fusion during Xenopus laevis development.Developmental biology · 2015Review
- A single domain of the ZP2 zona pellucida protein mediates gamete recognition in mice and humans.The Journal of cell biology · 2014Article
- Proteomic characterization and evolutionary analyses of zona pellucida domain-containing proteins in the egg coat of the cephalochordate, Branchiostoma belcheri.BMC evolutionary biology · 2012Article
- Human sperm bind to the N-terminal domain of ZP2 in humanized zonae pellucidae in transgenic mice.The Journal of cell biology · 2012Article
- Ovastacin, a cortical granule protease, cleaves ZP2 in the zona pellucida to prevent polyspermy.The Journal of cell biology · 2012Article
- Article
- A newly identified zona pellucida glycoprotein, ZPD, and dimeric ZP1 of chicken egg envelope are involved in sperm activation on sperm-egg interaction.The Biochemical journal · 2004Article
- The zona pellucida in folliculogenesis, fertilization and early development.Reviews in endocrine & metabolic disorders · 2002Review
- Allurin, a 21-kDa sperm chemoattractant from Xenopus egg jelly, is related to mammalian sperm-binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Little is known about sperm-binding proteins in the egg envelope of nonmammalian vertebrate species. We report here the molecular cloning and characterization of a recently identified sperm receptor (gp69/64) in the Xenopus laevis egg vitelline envelope. Our data indicate that the gp69 and gp64 glycoproteins are two glycoforms of the receptor and have the same number of N-linked oligosaccharide chains but differ in the extent of O-glycosylation. The amino acid sequence of the receptor is closely related to that of the mouse zona pellucida protein ZP2. Most of the sequence conservation, including a ZP domain, a potential furin cleavage site, and a putative transmembrane domain are located in the C-terminal half of the receptor. Proteolytic cleavage of the gp69/64 protein by a cortical granule protease during fertilization removes 27 amino acid residues from the N terminus of gp69/64 and results in loss of sperm binding to the activated eggs. Similarly, we find that treatment of eggs with type I collagenase removes 31 residues from the N terminus of gp69/64 and has the same effect on sperm binding. The isolated and purified N terminus-truncated receptor protein is inactive as an inhibitor of sperm-egg binding. Earlier studies on the effect of Pronase digestion on receptor activity suggest that this N-terminal peptide may contain an O-linked glycan that is involved in the binding process. Based on these results and the findings on the primary structure of the receptor, a pathway for the maturation and secretion of gp69/64, as well as its inactivation following fertilization, is proposed.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.