Participation of epididymal cysteine-rich secretory proteins in sperm-egg fusion and their potential use for male fertility regulation
Rat protein DE is an androgen-dependent cysteine-rich secretory protein (CRISP) synthesized by proximal epididymal regions. DE, also known as CRISP-1, is localized on the equatorial segment of acrosome-reacted spermatozoa and participates in gamete fusion through binding to egg complementary sites....
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2007
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1008682X_v9_n4_p528_Cohen http://hdl.handle.net/20.500.12110/paper_1008682X_v9_n4_p528_Cohen |
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paper:paper_1008682X_v9_n4_p528_Cohen2023-06-08T15:59:23Z Participation of epididymal cysteine-rich secretory proteins in sperm-egg fusion and their potential use for male fertility regulation Contraception Cysteine-rich secretory protein Epididymis Gamete fusion Sperm amino acid androgen cell protein contraceptive agent cysteine egg protein epididymal secretory protein synthetic peptide acrosome reaction amino acid sequence amino acid substitution cell fusion drug targeting egg epididymis fertilization gamete genetic conservation lizard male fertility molecular mechanics nonhuman protein binding protein localization protein motif protein synthesis regulatory mechanism review saliva sequence homology spermatozoon Animals Cell Fusion Epididymis Female Germ Cells Glycoproteins Humans Male Membrane Glycoproteins Ovum Rats Sperm Capacitation Sperm-Ovum Interactions Spermatozoa Rat protein DE is an androgen-dependent cysteine-rich secretory protein (CRISP) synthesized by proximal epididymal regions. DE, also known as CRISP-1, is localized on the equatorial segment of acrosome-reacted spermatozoa and participates in gamete fusion through binding to egg complementary sites. Immunization of rats with DE inhibits fertility and sperm fusion ability, suggesting that DE represents a good epididymal contraceptive target. Recombinant DE fragments and synthetic peptides revealed that DE binds to the egg via a 12-amino acid region of an evolutionarily conserved motif, Signature 2 (S2). The ability of other CRISP to bind to the rat egg was correlated with their S2 amino acid sequences. Although testicular protein Tpx-1 (CRISP-2) was capable of binding to rodent eggs, human epididymal AEG-related protein (ARP) and helothermine (from lizard saliva) were not. The S2 region presented only two substitutions in Tpx-1 and four in ARP and helothermine, compared with the DE S2, suggesting that this amino acid sequence was relevant for egg interaction. Studies with Tpx-1 and anti-Tpx-1 revealed the participation of this protein in gamete fusion through binding to complementary sites in the egg. In competition studies, DE reduced binding of Tpx-1 dose-dependently, indicating that both CRISP share the egg complementary sites. That anti-DE and anti-Tpx-1 inhibit sperm-egg fusion while recognizing only the corresponding proteins, suggests functional cooperation between these homologous CRISP to ensure fertilization success. These results increase our understanding of the molecular mechanisms of gamete fusion and contribute to the development of new and safer fertility regulating methods. © 2007 Asian Journal of Andrology, Shanghai Institute of Materia Medica, Chinese Academy of Sciences. 2007 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1008682X_v9_n4_p528_Cohen http://hdl.handle.net/20.500.12110/paper_1008682X_v9_n4_p528_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 |
Contraception Cysteine-rich secretory protein Epididymis Gamete fusion Sperm amino acid androgen cell protein contraceptive agent cysteine egg protein epididymal secretory protein synthetic peptide acrosome reaction amino acid sequence amino acid substitution cell fusion drug targeting egg epididymis fertilization gamete genetic conservation lizard male fertility molecular mechanics nonhuman protein binding protein localization protein motif protein synthesis regulatory mechanism review saliva sequence homology spermatozoon Animals Cell Fusion Epididymis Female Germ Cells Glycoproteins Humans Male Membrane Glycoproteins Ovum Rats Sperm Capacitation Sperm-Ovum Interactions Spermatozoa |
| spellingShingle |
Contraception Cysteine-rich secretory protein Epididymis Gamete fusion Sperm amino acid androgen cell protein contraceptive agent cysteine egg protein epididymal secretory protein synthetic peptide acrosome reaction amino acid sequence amino acid substitution cell fusion drug targeting egg epididymis fertilization gamete genetic conservation lizard male fertility molecular mechanics nonhuman protein binding protein localization protein motif protein synthesis regulatory mechanism review saliva sequence homology spermatozoon Animals Cell Fusion Epididymis Female Germ Cells Glycoproteins Humans Male Membrane Glycoproteins Ovum Rats Sperm Capacitation Sperm-Ovum Interactions Spermatozoa Participation of epididymal cysteine-rich secretory proteins in sperm-egg fusion and their potential use for male fertility regulation |
| topic_facet |
Contraception Cysteine-rich secretory protein Epididymis Gamete fusion Sperm amino acid androgen cell protein contraceptive agent cysteine egg protein epididymal secretory protein synthetic peptide acrosome reaction amino acid sequence amino acid substitution cell fusion drug targeting egg epididymis fertilization gamete genetic conservation lizard male fertility molecular mechanics nonhuman protein binding protein localization protein motif protein synthesis regulatory mechanism review saliva sequence homology spermatozoon Animals Cell Fusion Epididymis Female Germ Cells Glycoproteins Humans Male Membrane Glycoproteins Ovum Rats Sperm Capacitation Sperm-Ovum Interactions Spermatozoa |
| description |
Rat protein DE is an androgen-dependent cysteine-rich secretory protein (CRISP) synthesized by proximal epididymal regions. DE, also known as CRISP-1, is localized on the equatorial segment of acrosome-reacted spermatozoa and participates in gamete fusion through binding to egg complementary sites. Immunization of rats with DE inhibits fertility and sperm fusion ability, suggesting that DE represents a good epididymal contraceptive target. Recombinant DE fragments and synthetic peptides revealed that DE binds to the egg via a 12-amino acid region of an evolutionarily conserved motif, Signature 2 (S2). The ability of other CRISP to bind to the rat egg was correlated with their S2 amino acid sequences. Although testicular protein Tpx-1 (CRISP-2) was capable of binding to rodent eggs, human epididymal AEG-related protein (ARP) and helothermine (from lizard saliva) were not. The S2 region presented only two substitutions in Tpx-1 and four in ARP and helothermine, compared with the DE S2, suggesting that this amino acid sequence was relevant for egg interaction. Studies with Tpx-1 and anti-Tpx-1 revealed the participation of this protein in gamete fusion through binding to complementary sites in the egg. In competition studies, DE reduced binding of Tpx-1 dose-dependently, indicating that both CRISP share the egg complementary sites. That anti-DE and anti-Tpx-1 inhibit sperm-egg fusion while recognizing only the corresponding proteins, suggests functional cooperation between these homologous CRISP to ensure fertilization success. These results increase our understanding of the molecular mechanisms of gamete fusion and contribute to the development of new and safer fertility regulating methods. © 2007 Asian Journal of Andrology, Shanghai Institute of Materia Medica, Chinese Academy of Sciences. |
| title |
Participation of epididymal cysteine-rich secretory proteins in sperm-egg fusion and their potential use for male fertility regulation |
| title_short |
Participation of epididymal cysteine-rich secretory proteins in sperm-egg fusion and their potential use for male fertility regulation |
| title_full |
Participation of epididymal cysteine-rich secretory proteins in sperm-egg fusion and their potential use for male fertility regulation |
| title_fullStr |
Participation of epididymal cysteine-rich secretory proteins in sperm-egg fusion and their potential use for male fertility regulation |
| title_full_unstemmed |
Participation of epididymal cysteine-rich secretory proteins in sperm-egg fusion and their potential use for male fertility regulation |
| title_sort |
participation of epididymal cysteine-rich secretory proteins in sperm-egg fusion and their potential use for male fertility regulation |
| publishDate |
2007 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1008682X_v9_n4_p528_Cohen http://hdl.handle.net/20.500.12110/paper_1008682X_v9_n4_p528_Cohen |
| _version_ |
1768542373978046464 |