Enhancement of sperm-zona pellucida (ZP) binding capacity by activation of protein kinase A and C pathways in certain infertile men with defective sperm-ZP binding

Liu, D.Y.; Liu, M.L.; Baker, H.W. Gordon

doi:10.1093/humrep/den334

Cited by 10 publications

(10 citation statements)

References 37 publications

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“…In comparison with our previous study of normozoospermic infertile men with defective sperm-ZP binding, only about 13% or 33% of these men found to be associated with defective pathways of PKA or PKC (36). Although sperm-ZP binding and the ZP-induced AR are obviously different stages of sperm-ZP interaction, it is clear that defective PKA and PKC pathways are more frequently associated with DZPIAR than defective sperm-ZP binding in normozoospermic infertile men.…”

Section: Discussioncontrasting

confidence: 74%

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Defective protein kinase A and C pathways are common causes of disordered zona pellucida (ZP)–induced acrosome reaction in normozoospermic infertile men with normal sperm-ZP binding

Liu

Zhao

Baker

2013

Fertility and Sterility

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Section: Discussioncontrasting

confidence: 74%

“…Our previous studies showed that concentrations of 2 mM dbcAMP and 15 mM PMA had the maximum effect on sperm-ZP interaction without an impact on sperm motility (25,36). Therefore, we used 2mM dbcAMP and 15 mM PMA in this study.…”

Section: Effect Of Dbc-pma and Pma On The Zp-induced Ar Of Sperm In Dmentioning

confidence: 99%

Defective protein kinase A and C pathways are common causes of disordered zona pellucida (ZP)–induced acrosome reaction in normozoospermic infertile men with normal sperm-ZP binding

Liu

Zhao

Baker

2013

Fertility and Sterility

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“…Our findings with solubilized zona also highlight the role of PKC in zona induced acrosome reaction. The importance of both PKA and PKC pathways is further emphasised during fertilization by the observations of enhanced sperm-ZP binding in presence of PKA (dbcAMP) and PKC (PMA) activators [48]. …”

Section: Discussionmentioning

confidence: 99%

Delineation of downstream signalling components during acrosome reaction mediated by heat solubilized human zona pellucida

Bhandari

Bansal

Talwar

et al. 2010

Reprod Biol Endocrinol

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BackgroundHuman egg is enveloped by a glycoproteinaceous matrix, zona pellucida (ZP), responsible for binding of the human spermatozoa to the egg and induction of acrosomal exocytosis in the spermatozoon bound to ZP. In the present manuscript, attempts have been made to delineate the downstream signalling components employed by human ZP to induce acrosome reaction.MethodsHeat-solubilized human ZP (SIZP) was used to study the induction of acrosome reaction in capacitated human spermatozoa using tetramethylrhodamine isothiocyanate conjugated Pisum sativum agglutinin (TRITC-PSA) in absence or presence of various pharmacological inhibitors. In addition, intracellular calcium ([Ca2+]i) levels in sperm using Fluo-3 acetoxymethyl ester as fluorescent probe were also estimated in response to SIZP.ResultsSIZP induces acrosomal exocytosis in capacitated human sperm in a dose dependent manner accompanied by an increase in [Ca2+]i. Human SIZP mediated induction of acrosome reaction depends on extracellular Ca2+ and involves activation of Gi protein-coupled receptor, tyrosine kinase, protein kinases A & C and phosphoinositide 3 (PI3)- kinase. In addition, T-type voltage operated calcium channels and GABA-A receptor associated chloride (Cl-) channels play an important role in SIZP mediated induction of acrosome reaction.ConclusionsResults described in the present study provide a comprehensive account of the various downstream signalling components associated with human ZP mediated acrosome reaction.

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“…At the same time, the membrane surface is extensively remodeled. Of particular importance is the activation of the signal transduction pathway of sperm protein kinase A and protein kinase C [13][14][15] , making spermatozoa competent to bind the ZP and respond to this cell recognition event with the initiation of acrosome reaction. In mouse, the ZP is formed from three glycoproteins, ZP1, ZP2, and ZP3 [ 16 ] .…”

Section: Sperm-oocyte Interaction and Fusionmentioning

confidence: 99%

The Choreography of Fertilization

Coticchio

Brambillasca

2012

Oogenesis

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At fertilization, a continuum is established between the fi nal phases of oogenesis and the formation of a new individual. In mammals, the two processes are overlapped. The fertilizing spermatozoon represents the paternal contribution to zygote constitution and at the same time the trigger for the completion of meiosis. Oocytes can mimic fertilization, being able to recapitulate autonomously many of the events of early embryonic development. However, without the sperm contribution development to term cannot occur. The sperm, in fact, carries not only the paternal chromosomes, but also cytoskeletal elements and biochemical cues that are essential to complement and regulate the oocyte cellular legacy. Therefore, oocyte-sperm fusion creates a unique cellular machinery whose regulation in time and space in fl uences the long term destiny of the ensuing embryo.

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Enhancement of sperm-zona pellucida (ZP) binding capacity by activation of protein kinase A and C pathways in certain infertile men with defective sperm-ZP binding

Abstract: There is defective signalling in pathways upstream of PKC and PKA in some men with DSZPB and normal semen analysis. Stimulation of TP by dbcAMP does not enhance sperm-ZP binding capacity in DSZPB men with low TP, regardless of sperm morphology.

Cited by 10 publications

References 37 publications

Defective protein kinase A and C pathways are common causes of disordered zona pellucida (ZP)–induced acrosome reaction in normozoospermic infertile men with normal sperm-ZP binding

Defective protein kinase A and C pathways are common causes of disordered zona pellucida (ZP)–induced acrosome reaction in normozoospermic infertile men with normal sperm-ZP binding

Delineation of downstream signalling components during acrosome reaction mediated by heat solubilized human zona pellucida

The Choreography of Fertilization

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