Sperm-zona pellucida (ZP) interaction, involving the binding of sperm surface ligands to complementary carbohydrates of ZP, is the first direct gamete contact event crucial for subsequent gamete fusion and successful fertilization in mammals. It is a complex process mediated by the coordinated engagement of multiple ZP receptors forming high-molecular-weight (HMW) protein complexes at the acrosomal region of the sperm surface. The present article aims to review the current understanding of sperm-ZP binding in the four most studied mammalian models, i.e., murine, porcine, bovine, and human, and summarizes the candidate ZP receptors with established ZP affinity, including their origins and the mechanisms of ZP binding. Further, it compares and contrasts the ZP structure and carbohydrate composition in the aforementioned model organisms. The comprehensive understanding of sperm-ZP interaction mechanisms is critical for the diagnosis of infertility and thus becomes an integral part of assisted reproductive therapies/technologies.

• Keywords
• ZP-ligands, gamete interaction, sperm-ZP receptors, spermatozoa, zona pellucida,
• MeSH
• Humans MeSH
• Ligands MeSH
• Membrane Glycoproteins metabolism   MeSH
• Cell Communication * MeSH
• Receptors, Cell Surface metabolism   MeSH
• Mammals metabolism   MeSH
• Spermatozoa cytology   metabolism   MeSH
• Zona Pellucida metabolism   MeSH
• Animals MeSH
• Check Tag
• Humans MeSH
• Male MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Review MeSH
• Research Support, U.S. Gov't, Non-P.H.S. MeSH
• Names of Substances
• Ligands MeSH
• Membrane Glycoproteins MeSH
• Receptors, Cell Surface MeSH

Glutamate carboxypeptidase II (GCPII) is a membrane peptidase expressed in the prostate, central and peripheral nervous system, kidney, small intestine, and tumor-associated neovasculature. The GCPII form expressed in the central nervous system, termed NAALADase, is responsible for the cleavage of N-acetyl-L-aspartyl-L-glutamate (NAAG) yielding free glutamate in the synaptic cleft, and is implicated in various pathologic conditions associated with glutamate excitotoxicity. The prostate form of GCPII, termed prostate-specific membrane antigen (PSMA), is up-regulated in cancer and used as an effective prostate cancer marker. Little is known about the structure of this important pharmaceutical target. As a type II membrane protein, GCPII is heavily glycosylated. In this paper we show that N-glycosylation is vital for proper folding and subsequent secretion of human GCPII. Analysis of the predicted N-glycosylation sites also provides evidence that these sites are critical for GCPII carboxypeptidase activity. We confirm that all predicted N-glycosylation sites are occupied by an oligosaccharide moiety and show that glycosylation at sites distant from the putative catalytic domain is critical for the NAAG-hydrolyzing activity of GCPII calling the validity of previously described structural models of GCPII into question.

• MeSH
• Antigens, Surface chemistry   genetics   metabolism   MeSH
• Cell Line MeSH
• Gene Expression MeSH
• Glutamate Carboxypeptidase II chemistry   genetics   metabolism   MeSH
• Glycosylation MeSH
• Insecta MeSH
• Hydrolysis MeSH
• Catalysis MeSH
• Kinetics MeSH
• Humans MeSH
• Mutagenesis, Site-Directed genetics   MeSH
• Binding Sites MeSH
• Animals MeSH
• Check Tag
• Humans MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Antigens, Surface MeSH
• FOLH1 protein, human MeSH Browser
• Glutamate Carboxypeptidase II MeSH

A total of 307 new compounds, natural, semisynthetic or synthetic, were isolated at the Institute of microbiology during the last twelve years. Due to the development of separation (chromatographic) methods and of analytical methods used to determine the chemical structure of these compounds, i.e. NMR, MS and X-ray diffraction, many new metabolites could be described.

• MeSH
• Biological Factors chemistry   isolation & purification   MeSH
• Peptides, Cyclic chemistry   isolation & purification   MeSH
• Enzymes chemistry   isolation & purification   MeSH
• Molecular Sequence Data MeSH
• Ergot Alkaloids chemistry   isolation & purification   MeSH
• Carbohydrate Sequence MeSH
• Carbohydrates chemistry   isolation & purification   MeSH
• Amino Acid Sequence MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Review MeSH
• Names of Substances
• Biological Factors MeSH
• Peptides, Cyclic MeSH
• Enzymes MeSH
• Ergot Alkaloids MeSH
• Carbohydrates MeSH