Role of lipoxygenase in the mechanism of acrosome reaction in mammalian spermatozoa

1990 ◽  
Vol 1043 (1) ◽  
pp. 12-18 ◽  
Author(s):  
Y. Lax ◽  
S. Grossman ◽  
S. Rubinstein ◽  
N. Magid ◽  
H. Breitbart
Keyword(s):  
Acrosome Reaction ◽  
Mammalian Spermatozoa

scholarly journals Effect of calmodulin on the stimulation of capacitation and acrosome reaction of frozen thawed bull spermatozoa

2017 ◽  
Vol 45 (3) ◽  
pp. 1-9
Author(s):  
QS Akter ◽  
KMA Tareq ◽  
K Hamano ◽  
RB Gilchrist
Keyword(s):  
Acrosome Reaction ◽  
Specific Binding ◽  
Staining Technique ◽  
Inhibitory Effect ◽  
Free Medium ◽  
Inhibitory Effects ◽  
Specific Binding Protein ◽  
Bovine Spermatozoa ◽  
Mammalian Spermatozoa

Capacitation and acrosome reaction (AR) are the prerequisites for successful fertilization by mammalian spermatozoa. Intracellular calcium (Ca2+) has a regulatory role in sperm motility, capacitation, and AR. Calmodulin (CaM) antagonists calmidazolium (CZ) and N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W7) were used to investigate the possible role of CaM, a Ca2+ specific binding protein, on motility, capacitation and AR of frozen-thawed bovine spermatozoa. Capacitation and AR in sperm were evaluated by using chlortetracycline (CTC) staining technique. Addition of the 1 mM dibutyryl cAMP (dbcAMP) and 100 ?M 1-methy l-3-isobutylxanthine (IBMX) to CaM antagonists treated sperm incubated in the presence of NaHCO3 and CaCl2 in media overcome the inhibitory effects of these antagonists to support capacitation and AR at 4 h of incubation period. In contrast, addition of dbcAMP with IBMX induced AR in spermatozoa incubated with NaHCO3-free medium but these compounds did not induce AR in cells incubated in CaCl2-free medium. However, the addition of dbcAMP and IBMX partially, but significantly (p<0.01) reversed the inhibitory effect of W7 and CZ on the sperm capacitation and AR. These results suggest that CaM may play an important role in the regulation of capacitation and AR in frozen-thawed bovine spermatozoa.Bang. J. Anim. Sci. 2016. 45 (3): 1-9

scholarly journals Stimulation of platelet-activating factor synthesis by progesterone and A23187 in human spermatozoa

1993 ◽  
Vol 292 (1) ◽  
pp. 209-216 ◽  
Author(s):  
E Baldi ◽  
C Falsetti ◽  
C Krausz ◽  
G Gervasi ◽  
V Carloni ◽  
...  
Keyword(s):  
Acrosome Reaction ◽  
Platelet Activating Factor ◽  
Human Sperm ◽  
Human Spermatozoa ◽  
Acetate Incorporation ◽  
Acid Release ◽  
Similar Kinetic ◽  
Mammalian Spermatozoa ◽  
Stimulation Of

The presence of platelet-activating factor (PAF) has been demonstrated recently in mammalian spermatozoa, together with evidence for a role of this phospholipid in enhancing sperm motility and fertilizing ability. To investigate whether PAF synthesis and release occurs in human spermatozoa following incubation with stimuli that induce acrosome reaction, spermatozoa were incubated with progesterone and A23187, two known inducers of the exocytotic event. PAF synthesis (remodelling pathway) was assessed by [3H]acetate incorporation into PAF. Treatment of spermatozoa with progesterone and A23187 resulted in an increase of [3H]acetate incorporation into PAF. Most of the newly synthesized [3H]PAF formed in response to acrosome reaction was found in the supernatant, suggesting a release of the phospholipid from spermatozoa. PAF-like material extracted from human spermatozoa was able to induce aggregation of rabbit platelets and showed identical retention time and the same ion m/e values as authentic PAF when analysed with g.c.-m.s. Lyso-PAF:acetyl-CoA acetyltransferase (EC 2.3.1.67) activity in human spermatozoa was also studied and showed similar kinetic parameters to those described for other cell systems. Stimulation of spermatozoa with progesterone and A23187 induced an increase of [3H]arachidonic acid release, suggesting an activation of phospholipase A. In conclusion, our results demonstrated increased production and release of PAF in human sperm following stimulation with progesterone and A23187 and suggest a role for this phospholipid in the activation of spermatozoa.

scholarly journals PACAP-mediated sperm–cumulus cell interaction promotes fertilization

Reproduction ◽  
2011 ◽  
Vol 141 (2) ◽  
pp. 163-171 ◽  
Author(s):  
Ichiro Tanii ◽  
Tadashi Aradate ◽  
Kouhei Matsuda ◽  
Akira Komiya ◽  
Hideki Fuse
Keyword(s):  
Sperm Motility ◽  
Acrosome Reaction ◽  
Cumulus Cell ◽  
Cumulus Cells ◽  
Cell Interaction ◽  
Fertilization Rate ◽  
Type I ◽  
Dependent Manner ◽  
Sperm Penetration

The developing acrosome in spermatids contains pituitary adenylate cyclase-activating polypeptide (PACAP). However, the role of the acrosomal PACAP remains unclear because it has not been detected in mature spermatids and sperm. We reinvestigated whether the sperm acrosome contains PACAP. An antiserum produced against PACAP reacted to the anterior acrosome in epididymal sperm fixed under mild conditions, suggesting that PACAP acts on oocytes and/or cumulus cells at the site of fertilization. Immunolabeling and RT-PCR demonstrated the presence of PACAP type I receptor, a PACAP-specific receptor, in postovulatory cumulus cells. To investigate the role of PACAP in fertilization, we pretreated cumulus–oocyte complexes with the polypeptide. At a low concentration of sperm, the fertilization rate was significantly enhanced by PACAP in a dose-dependent manner. Sperm penetration through the oocyte investment, cumulus layer, and zona pellucida was also enhanced by PACAP. The enhancement was probably due to an enhancement in sperm motility and the zona-induced acrosome reaction, which were stimulated by a cumulus cell-releasing factor. Indeed, PACAP treatment increased the secretion of progesterone from the cumulus–oocyte complexes. These results strongly suggest that in response to PACAP, cumulus cells release a soluble factor that probably stimulates sperm motility and the acrosome reaction, thereby promoting fertilization.

scholarly journals Antioxidant effect of Mn2+ on capacitation and acrosome reaction of fresh and chilled cattle bull semen

2012 ◽  
Vol 1 (1) ◽  
pp. 18
Author(s):  
Amrit Kaur Bansal ◽  
Ranjna Sundhey Cheema ◽  
Vinod Kumar Gandotra
Keyword(s):  
Reactive Oxygen Species ◽  
Lipid Peroxidation ◽  
Acrosome Reaction ◽  
Reactive Oxygen ◽  
Antioxidant Effect ◽  
Oxygen Species ◽  
Sperm Capacitation ◽  
Bull Semen

The aim of this paper was to investigate the antioxidant effect of Mn2+ (200 mM) on the sperm capacitation and acrosome reaction of fresh and chilled cattle bull semen. It has been found that Mn2+ supplementation improves (P≤0.05) the motility at 0, 2, 4 and 6 h of incubation. MDA (malondialdehyde), end product of lipid peroxidation, decreases significantly (P≤0.05) with the supplementation of manganese at 0- and 6-hr of incubation both in fresh and chilled semen. Manganese also increases acrosome reaction significantly (P≤0.05) both in fresh and chilled semen at 0, 4 and 6 h of incubation. Therefore, our findings suggest the role of Mn2+supplementation in improving the quality of cattle bull semen by its scavenging property<em> i.e.</em> reduction in the production of reactive oxygen species during its storage at 4°C or incubation at 37°C for capacitation.

scholarly journals Mechanism of sperm capacitation and the acrosome reaction: role of protein kinases

2012 ◽  
Vol 14 (6) ◽  
pp. 816-821 ◽  
Author(s):  
Debby Ickowicz ◽  
Maya Finkelstein ◽  
Haim Breitbart
Keyword(s):  
Protein Kinases ◽  
Acrosome Reaction ◽  
Sperm Capacitation

scholarly journals Sperm binding to ZP2-coated beads improve the efficiency of porcine in vitro fertilisation

Reproduction ◽  
2020 ◽  
Vol 160 (5) ◽  
pp. 725-735
Author(s):  
Julieta Gabriela Hamze ◽  
María Jiménez-Movilla ◽  
Raquel Romar
Keyword(s):  
Acrosome Reaction ◽  
Cumulus Cell ◽  
Cumulus Cells ◽  
In Vitro Fertilisation ◽  
Sperm Binding ◽  
Fertilisation Rate ◽  
Gamete Recognition ◽  
Boar Spermatozoa

The role of specific zona pellucida (ZP) glycoproteins in gamete interaction has not yet been elucidated in many species. A recently developed 3D model based on magnetic sepharose beads (B) conjugated to recombinant ZP glycoproteins (BZP) and cumulus cells (CBZP) allows the study of isolated ZP proteins in gamete recognition studies. The objective of this work was to study the role of porcine ZP2, ZP3 and ZP4 proteins in sperm binding, cumulus cell adhesion and acrosome reaction triggering. ZP protein-bound beads were incubated with fresh ejaculated boar spermatozoa and isolated cumulus cells for 24 h. The number of sperm bound to the beads, the acrosomal shrouds (presence of acrosomal content) on the bead’s surface, and the acrosome integrity (by means of PNA-FITC lectin) in bound and unbound sperm were studied. Finally, in vitro matured porcine oocytes mixed with BZP2 were inseminated in vitro using fresh sperm and fertilisation results evaluated. Over 60% of beads had at least one sperm bound after 2 h of coincubation. ZP2-beads (BZP2) and cumulus-ZP2-bead complexes (CBZP2) reached the highest number of sperm per bead, whereas BZP3 and BZP4 models showed the highest number of unbound reacted sperm cells and acrosomal shrouds. Fertilisation efficiency and monospermy rate increased when oocytes were fertilised in the presence of BZP2. We, therefore, conclude that in pigs, it is mainly ZP2 that is involved in sperm-ZP binding whereas ZP3 and ZP4 induce acrosome reaction. Using magnetic sepharose ZP2-bound beads might be a valuable tool to improve the fertilisation rate in pigs.

scholarly journals 436. Investigation of the role of SRC in capacitation associated tyrosine phosphorylation of human spermatozoa

2008 ◽  
Vol 20 (9) ◽  
pp. 116
Author(s):  
L. A. Mitchell ◽  
B. Nixon ◽  
M. A. Baker ◽  
R. J. Aitken
Keyword(s):  
Tyrosine Kinase ◽  
Tyrosine Phosphorylation ◽  
Signal Transduction Pathway ◽  
Human Sperm ◽  
Complex Signal ◽  
Phosphorylation Cascade ◽  
A Site ◽  
Signalling Cascade ◽  
Mammalian Spermatozoa

Capacitation is a pre-requisite for mammalian spermatozoa allowing them to gain the ability to fertilise an oocyte. A fundamental part of this mechanism is a dramatic increase in tyrosine phosphorylation. Implicated in this process in the mouse is a unique cAMP/PKA-mediated pathway involving a PKA-activated tyrosine kinase suggested to be pp60c-src (SRC). The Src kinases examined were predominantly expressed in the human sperm tail, a site compatible with a role in mediating the capacitation-associated tyrosine phosphorylation cascade. Co-immunoprecipitation revealed that PKA-c could be isolated from sperm and this interaction was restricted to capacitated cells, suggesting PKA-mediated activation of SRC forms an integral part of the signalling cascade assembled during capacitation. Upon activation, SRC undergoes autophosphorylation of Y416 and thus phosphorylation of this residue indicates the presence of active SRC kinase. The phosphorylation status of SRC was compared using both 2D-immunoblotting and immunocytochemical studies, both revealing a significant increase in SRC activation during capacitation. Furthermore, suppression of PKA and SRC through application of SU6656, or H89, a PKA inhibitor, led to a dramatic decrease in tyrosine phosphorylation and SRC activity. In conclusion, this study has provided evidence for the involvement of non-receptor tyrosine kinase, SRC, in regulating tyrosine phosphorylation associated with capacitation. Inhibition of SRC did not completely suppress tyrosine phosphorylation suggesting this complex signal transduction pathway exhibits a degree of functional redundancy.

Corrigendum to: IQ motif containing D (IQCD), a new acrosomal protein involved in the acrosome reaction and fertilisation

2019 ◽  
Vol 31 (5) ◽  
pp. 1033
Author(s):  
Peng Zhang ◽  
Wanjun Jiang ◽  
Na Luo ◽  
Wenbing Zhu ◽  
Liqing Fan
Keyword(s):  
Acrosome Reaction ◽  
Development Stage ◽  
Seminiferous Tubules ◽  
Testicular Development ◽  
Dependent Manner ◽  
Iq Motif ◽  
C Elegans ◽  
Fertilisation Rate ◽  
Age Dependent ◽  
Mammalian Spermatozoa

The acrosome is single, large, dense-core secretory granule overlying the nucleus of most mammalian spermatozoa. Its exocytosis, the acrosome reaction, is a crucial event during fertilisation. In this study we identified a new acrosome-associated gene, namely IQ motif containing D (IQCD), expressed nearly in multiple tissues with highest expression levels in the testis. In mouse testis, Iqcd transcript accumulated from Postnatal Day (PND) 1 to adulthood. However, expression of IQCD protein at the testicular development stage started primarily from PND 18 and increased in an age-dependent manner until plateauing in adulthood. IQCD was primarily accumulated in the acrosome area of round and elongating spermatids within seminiferous tubules of the testes during the late stage of spermiogenesis; this immunolocalisation pattern is similar in mice and humans. IQCD levels in spermatozoa were significantly lower in IVF patients with total fertilisation failure or a low fertilisation rate than in healthy men. Anti-IQCD antibody significantly inhibited the acrosome reaction and slightly reduced protein tyrosine phosphorylation levels in human spermatozoa, but specifically blocked murine IVF. IQCD interacted with mammalian homolog of C. elegans uncoordinated gene 13 (Munc13) in spermatozoa and may participate in acrosome exocytosis. In conclusion, this study identified a new acrosomal protein, namely IQCD, which is involved in fertilisation and the acrosome reaction.

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