Participation of cysteine-rich secretory proteins (CRISP) in mammalian sperm-egg interaction
Mammalian fertilization is a complex multi-step process mediated by different molecules present on both gametes. CRISP1 (cysteine-rich secretory protein 1) is an epididymal protein thought to participate in gamete fusion through its binding to egg-complementary sites. Structure-function studies usin...
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2008
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02146282_v52_n5-6_p737_Cohen http://hdl.handle.net/20.500.12110/paper_02146282_v52_n5-6_p737_Cohen |
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paper:paper_02146282_v52_n5-6_p737_Cohen2023-06-08T15:20:54Z Participation of cysteine-rich secretory proteins (CRISP) in mammalian sperm-egg interaction Capacitation Fertilization Fusion Gamete Oocyte cysteine rich secretory protein 1 cysteine rich secretory protein 2 egg protein epididymal secretory protein unclassified drug amino acid sequence article fertility fertilization gamete gamete fusion human human versus animal comparison membrane fusion nonhuman oocyte priority journal protein binding protein expression protein function protein interaction protein motif sequence analysis sperm zona pellucida Animals Cysteine Female Glycoproteins Guinea Pigs Humans Male Membrane Glycoproteins Mice Models, Biological Protein Binding Rats Sperm-Ovum Interactions Spermatozoa Mammalia Rattus Mammalian fertilization is a complex multi-step process mediated by different molecules present on both gametes. CRISP1 (cysteine-rich secretory protein 1) is an epididymal protein thought to participate in gamete fusion through its binding to egg-complementary sites. Structure-function studies using recombinant fragments of CRISP1 as well as synthetic peptides reveal that its egg-binding ability resides in a 12 amino acid region corresponding to an evolutionary conserved motif of the CRISP family, named Signature 2 (S2). Further experiments analyzing both the ability of other CRISP proteins to bind to the rat egg and the amino acid sequence of their S2 regions show that the amino acid sequence of the S2 is needed for CRISP1 to interact with the egg. CRISP1 appears to be involved in the first step of sperm binding to the zona pellucida, identifying a novel role for this protein in fertilization. The observation that sperm testicular CRISP2 is also able to bind to the egg surface suggests a role for this protein in gamete fusion. Subsequent experiments confirmed the participation of CRISP2 in this step of fertilization and revealed that CRISP1 and CRISP2 interact with common egg surface binding sites. Together, these results suggest a functional cooperation between CRISP1 and CRISP2 to ensure the success of fertilization. These observations contribute to a better understanding of the molecular mechanisms underlying mammalian fertilization. © UBC Press. 2008 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02146282_v52_n5-6_p737_Cohen http://hdl.handle.net/20.500.12110/paper_02146282_v52_n5-6_p737_Cohen |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Capacitation Fertilization Fusion Gamete Oocyte cysteine rich secretory protein 1 cysteine rich secretory protein 2 egg protein epididymal secretory protein unclassified drug amino acid sequence article fertility fertilization gamete gamete fusion human human versus animal comparison membrane fusion nonhuman oocyte priority journal protein binding protein expression protein function protein interaction protein motif sequence analysis sperm zona pellucida Animals Cysteine Female Glycoproteins Guinea Pigs Humans Male Membrane Glycoproteins Mice Models, Biological Protein Binding Rats Sperm-Ovum Interactions Spermatozoa Mammalia Rattus |
| spellingShingle |
Capacitation Fertilization Fusion Gamete Oocyte cysteine rich secretory protein 1 cysteine rich secretory protein 2 egg protein epididymal secretory protein unclassified drug amino acid sequence article fertility fertilization gamete gamete fusion human human versus animal comparison membrane fusion nonhuman oocyte priority journal protein binding protein expression protein function protein interaction protein motif sequence analysis sperm zona pellucida Animals Cysteine Female Glycoproteins Guinea Pigs Humans Male Membrane Glycoproteins Mice Models, Biological Protein Binding Rats Sperm-Ovum Interactions Spermatozoa Mammalia Rattus Participation of cysteine-rich secretory proteins (CRISP) in mammalian sperm-egg interaction |
| topic_facet |
Capacitation Fertilization Fusion Gamete Oocyte cysteine rich secretory protein 1 cysteine rich secretory protein 2 egg protein epididymal secretory protein unclassified drug amino acid sequence article fertility fertilization gamete gamete fusion human human versus animal comparison membrane fusion nonhuman oocyte priority journal protein binding protein expression protein function protein interaction protein motif sequence analysis sperm zona pellucida Animals Cysteine Female Glycoproteins Guinea Pigs Humans Male Membrane Glycoproteins Mice Models, Biological Protein Binding Rats Sperm-Ovum Interactions Spermatozoa Mammalia Rattus |
| description |
Mammalian fertilization is a complex multi-step process mediated by different molecules present on both gametes. CRISP1 (cysteine-rich secretory protein 1) is an epididymal protein thought to participate in gamete fusion through its binding to egg-complementary sites. Structure-function studies using recombinant fragments of CRISP1 as well as synthetic peptides reveal that its egg-binding ability resides in a 12 amino acid region corresponding to an evolutionary conserved motif of the CRISP family, named Signature 2 (S2). Further experiments analyzing both the ability of other CRISP proteins to bind to the rat egg and the amino acid sequence of their S2 regions show that the amino acid sequence of the S2 is needed for CRISP1 to interact with the egg. CRISP1 appears to be involved in the first step of sperm binding to the zona pellucida, identifying a novel role for this protein in fertilization. The observation that sperm testicular CRISP2 is also able to bind to the egg surface suggests a role for this protein in gamete fusion. Subsequent experiments confirmed the participation of CRISP2 in this step of fertilization and revealed that CRISP1 and CRISP2 interact with common egg surface binding sites. Together, these results suggest a functional cooperation between CRISP1 and CRISP2 to ensure the success of fertilization. These observations contribute to a better understanding of the molecular mechanisms underlying mammalian fertilization. © UBC Press. |
| title |
Participation of cysteine-rich secretory proteins (CRISP) in mammalian sperm-egg interaction |
| title_short |
Participation of cysteine-rich secretory proteins (CRISP) in mammalian sperm-egg interaction |
| title_full |
Participation of cysteine-rich secretory proteins (CRISP) in mammalian sperm-egg interaction |
| title_fullStr |
Participation of cysteine-rich secretory proteins (CRISP) in mammalian sperm-egg interaction |
| title_full_unstemmed |
Participation of cysteine-rich secretory proteins (CRISP) in mammalian sperm-egg interaction |
| title_sort |
participation of cysteine-rich secretory proteins (crisp) in mammalian sperm-egg interaction |
| publishDate |
2008 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02146282_v52_n5-6_p737_Cohen http://hdl.handle.net/20.500.12110/paper_02146282_v52_n5-6_p737_Cohen |
| _version_ |
1768545970281250816 |