Cyclic QDE peptide increases fertilization rates and provides healthy pups in mouse

Barraud-Lange, Virginie; Naud-Barriant, Nathalie; Ducot, B.; Chambris, Stéphane; Bomsel, Morgane; Wolf, Jean-Philippe; Ziyyat, Ahmed

doi:10.1016/j.fertnstert.2008.05.088

Cited by 6 publications

(8 citation statements)

References 34 publications

(47 reference statements)

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“…While the cFEE peptide (phenylalanine, glutamic acid; glutamic acid) is active in human, mouse gametes require the cQDE peptide (glutamine; aspartic acid; glutamic acid). In mouse, we have previously shown that cQDE significantly increases the IVF fertilization rate [6]. Sperm from mice lacking fertilin β were shown to be deficient in sperm-egg membrane adhesion, sperm-egg fusion, migration from the uterus into the oviduct, and binding to the egg zona pellucida [7].…”

Section: Introductionmentioning

confidence: 99%

Cyclic FEE Peptide Improves Human Sperm Movement Parameters without Modification of Their Energy Metabolism

Foll

Pont

L’Hostis

et al. 2021

IJMS

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Cyclic fertilin peptide (cFEE: phenylalanine, glutamic acid; glutamic acid) improves gamete interaction in humans. We investigate whether it could be via improvement of sperm movement parameters and their mitochondrial ATP production. Sperm movement parameters were studied using computer-assisted sperm analysis (CASA) in sperm samples from 38 patients with normal sperm in medium supplemented with cyclic fertilin against a control group. Sperm mitochondrial functions were studied using donor’s sperm, incubated or not with cFEE. It was evaluated by the measurement of their ATP production using bioluminescence, their respiration by high resolution oxygraphy, and of mitochondrial membrane potential (MMP) using potentiometric dyes and flow cytometry. cFEE significantly improved sperm movement parameters and percentage of hyperactivated sperm. Impact of inhibitors showed OXPHOS as the predominant energy source for sperm movement. However, cFEE had no significant impact on any of the analyzed mitochondrial bioenergetic parameters, suggesting that it could act via a more efficient use of its energy resources.

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Section: Introductionmentioning

confidence: 99%

Cyclic FEE Peptide Improves Human Sperm Movement Parameters without Modification of Their Energy Metabolism

Foll

Pont

L’Hostis

et al. 2021

IJMS

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“…The cFEE peptide was synthesized by SYNP-ROSIS SA (Fuveau, France) to Good Manufacturing Practice standards for human use. Previous studies were performed using the cFEE peptide at 100 mM (14,15), but a recent doseresponse study on in vitro human embryo development that we performed (16) showed that probably 1 mM would give best results, whereas the concentration of 0.1 mM was ineffective. This is the reason why these 2 concentrations were used.…”

Section: In Vitro Maturation Studymentioning

confidence: 90%

“…We previously described a synthetic cyclic tripeptide (cFEE) derived from the integrinbinding domain of human fertilin b. cFEE binds to the oocyte membrane and increases the human gamete fusion index in vitro by 94% using zona-free eggs (14). The equivalent peptide derived from the mouse fertilin cQDE increases the fertilization rate of mouse oocytes in vitro by 88%, and transfer of the resulting embryos into pseudopregnant females provided 3 generations of healthy pups (15). To evaluate the possibility of using the cFEE peptide to improve the success of ART in the clinic, here, we characterized further its effects on human oocyte maturation.…”

mentioning

confidence: 99%

A fertilin-derived peptide improves in vitro maturation and ploidy of human oocytes

et al. 2022

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“…The ability to select sperm with optimal localization patterns and expression levels of ADAMs or develop agonists that promote ADAM function could lead to improved IVF outcomes. 107 The reproductive ADAM system is one of the most clinically useful models for studying the orchestrated regulation and organization of sperm surface proteins and the assembly of sperm proteins into functional complexes that are critical for fertilization. Continuing studies on sperm ADAMs should provide important information regarding the molecular mechanisms that underlie mammalian fertilization.…”

Section: Role Of Adams In Fertilizationmentioning

confidence: 99%

Testicular and epididymal ADAMs: expression and function during fertilization

Cho

2012

Nat Rev Urol

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The disintegrin and metalloprotease domain-containing protein (ADAM) family of multidomain membrane proteins comprises at least 34 members in mammals. More than half of these proteins are expressed specifically or predominantly in mammalian testes and epididymis, implying their prominence in male reproduction. These reproductive ADAMs can be classified into three phylogenetic groups; designated I, II, and III. Each group displays remarkably contrasting features. Group I contains 11 ADAMs expressed in the testis. The genes that encode these proteins lack introns in their coding sequences and most of the proteins are processed into prodomain-lacking forms in mature sperm. Five ADAMs--encoded by genes with multiple exons and introns--belong to phylogenetic group II. These ADAMs are also expressed in testicular germ cells, but both prodomains and metalloprotease domains are lacking in mature sperm. Two phylogenetic group III ADAMs are synthesized in the epididymis; one of which is secreted and transferred to the sperm surface. Some of these sperm ADAMs are assembled into potentially functional complexes, including ADAM1B-ADAM2, ADAM2-ADAM3-ADAM4, ADAM2-ADAM3-ADAM5, and ADAM2-ADAM3-ADAM6. It has been suggested that ADAM2 and ADAM3 have roles in sperm-egg interactions. Mouse knockout studies have revealed that the ADAM2-ADAM3 complex is critical for in vivo sperm migratory function in the female reproductive tract.

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Cyclic QDE peptide increases fertilization rates and provides healthy pups in mouse

Cited by 6 publications

References 34 publications

Cyclic FEE Peptide Improves Human Sperm Movement Parameters without Modification of Their Energy Metabolism

Cyclic FEE Peptide Improves Human Sperm Movement Parameters without Modification of Their Energy Metabolism

A fertilin-derived peptide improves in vitro maturation and ploidy of human oocytes

Testicular and epididymal ADAMs: expression and function during fertilization

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