scholarly journals Expression and Localization of δ-, κ-, and μ-Opioid Receptors in Human Spermatozoa and Implications for Sperm Motility

2006 ◽  
Vol 91 (12) ◽  
pp. 4969-4975 ◽  
Author(s):  
Ekaitz Agirregoitia ◽  
Asier Valdivia ◽  
Arkaitz Carracedo ◽  
Luis Casis ◽  
Javier Gil ◽  
...  
Keyword(s):  
Sperm Motility ◽  
Opioid Receptors ◽  
Receptor Agonist ◽  
Reproductive Tract ◽  
Human Sperm ◽  
Human Spermatozoa ◽  
Endogenous Opioid ◽  
Progressive Motility ◽  
Agonist And Antagonist ◽  
Μ Opioid Receptors

Abstract Context: Endogenous opioid peptides signal through δ-, κ-, and μ-opioid receptors. Some of these peptides such as endorphins and enkephalins are present in the male reproductive tract, but the presence of the corresponding receptors in human sperm cells has not yet been reported. Objective: Our objective was to study the expression and localization of δ-, κ-, and μ-opioid receptors on human spermatozoa and the implication in sperm motility. Methods: The expression of receptors was studied by RT-PCR, Western blot, and immunofluorescence techniques. We evaluated the effects of activation of each opioid receptor by specific agonist and antagonist. Results: Human spermatozoa express δ-, κ-, and μ-opioid receptors. These receptors were located in different parts of the head, in the middle region, and in the tail of the sperm. Progressive motility of spermatozoa, an important parameter to evaluate male fertility, was found to be significantly reduced after incubation with the μ-receptor agonist morphine, whereas this effect was antagonized in the presence of the corresponding antagonist naloxone. The δ-receptor antagonist naltrindole significantly reduced progressive motility immediately after its addition. However, the δ-receptor agonist DPDPE had no significant effect. Finally, neither the κ-receptor agonist U50488 nor its antagonist nor-binaltorphimine significantly affected the progressive motility of human spermatozoa. Conclusion: We report for first time the presence of functional δ-, κ-, and μ-opioid receptors in human sperm membranes. These findings are indicative of a role for the opioid system in the regulation of sperm physiology.

Testis developmental related gene 1 (TDRG1) encodes a progressive motility-associated protein in human spermatozoa

2020 ◽  
Author(s):  
Houyang Chen ◽  
Liang Tang ◽  
Qing Hong ◽  
Tingting Pan ◽  
Shiqi Weng ◽  
...  
Keyword(s):  
Sperm Motility ◽  
Conflicts Of Interest ◽  
Human Sperm ◽  
Human Spermatozoa ◽  
Mass Spectrometry Analysis ◽  
Human Testis ◽  
Specific Gene ◽  
Related Gene ◽  
Progressive Motility ◽  
Related Proteins

Abstract STUDY QUESTION Is there an association between the human testis-specific gene, testis developmental related gene 1 (TDRG1) and human sperm motility? SUMMARY ANSWER TDRG1 is associated with asthenozoospermia and involved in regulating human sperm motility. WHAT IS KNOWN ALREADY Many testis-specific proteins potentially regulate spermatogenesis and sperm motility. We have identified a novel human testis-specific gene, TDRG1, which encodes a 100-amino-acid protein localized in the human sperm tail, yet little is known about its role in human spermatozoa. STUDY DESIGN, SIZE, DURATION Sperm samples were obtained from normozoospermic men and asthenozoospermic men who visited the reproductive medical center at Jiangxi Maternal and Child Health Hospital, Nanchang, Jiangxi, China between February 2018 and January 2019. In total, 27 normozoospermic men and 25 asthenozoospermic men were recruited to participate in the study. PARTICIPANTS/MATERIALS, SETTING, METHODS The level of TDRG1 in sperm of normozoospermic and asthenozoospermic men was examined by immunoblotting and immunofluorescence assays. Progressive motility was examined by computer-aided sperm analysis. The correlation between the TDRG1 protein level and progressive motility was analyzed by linear regression. TDRG1 was imported into the sperm of normozoospermic and asthenozoospermic men using a cell-penetrating peptide (CPP)-fused TDRG1 recombinant protein (CPP-TDRG1), and the progressive motility was examined. Also, the altered proteins associated with TDRG1 in asthenozoospermic sperm were detected using label-free quantification method-based quantitative proteomic technology. TDRG1-interacting proteins were identified by co-immunoprecipitation coupled with tandem mass spectrometry analysis. MAIN RESULTS AND THE ROLE OF CHANCE The mean level of TDRG1 was significantly decreased in sperm of asthenozoospermic men compared with normozoospermic men (P < 0.05) and was positively correlated with percentage of progressively motile sperm (r2 = 0.75, P = 0.0001). The introduction of TDRG1 into human sperm, using CPP, significantly increased progressive motility (P < 0.05) and improved the progressive motility of sperm from asthenozoospermic men to the normal level. TDRG1 forms a protein complex with sperm-motility related proteins in human sperm and its downregulation was associated with a decrease in other motility-related proteins. LARGE SCALE DATA N/A. LIMITATIONS, REASONS FOR CAUTION The sample size was limited and larger cohorts are needed for verifying the positive effect of CPP-TDRG1 on human sperm motility. Furthermore, the caution should be paid that a comprehensive safety examination would be performed to evaluate whether CPP-TDRG1 is a possible treatment approach for asthenozoospermia. WIDER IMPLICATIONS OF THE FINDINGS Our results provide new insights into the mechanisms of sperm motility which may contribute to the diagnosis and treatment for asthenozoospermia. STUDY FUNDING/COMPETING INTEREST(S) National Natural Science Foundation of China (81501317 and 81871207 to H.C.; 81771644 to T.L.; 31671204 to X.Z.; 81571432 to Y.T.). The authors have no conflicts of interest to declare.

119. IDENTIFICATION AND CHARACTERISATION OF SURFACE PROTEIN COMPLEXES IN HUMAN SPERMATOZOA

2010 ◽  
Vol 22 (9) ◽  
pp. 37 ◽  
Author(s):  
K. A. Redgrove ◽  
B. Nixon ◽  
E. A. McLaughlin ◽  
M. K. O'Bryan ◽  
R. J. Aitken
Keyword(s):  
Zona Pellucida ◽  
Reproductive Tract ◽  
Protein Complexes ◽  
Polyacrylamide Gel Electrophoresis ◽  
Human Sperm ◽  
Female Reproductive Tract ◽  
Human Spermatozoa ◽  
Apical Region ◽  
Post Translational Modification ◽  
Cellular Mechanisms

A unique characteristic of mammalian spermatozoa is that upon ejaculation, they are unable to recognise and bind to an ovulated oocyte. These functional attributes are only realised following the sperms ascent of the female reproductive tract whereupon they undergo a myriad of biochemical and biophysical changes collectively referred to as ‘capacitation’. Since spermatozoa are both transcriptionally and translationally quiescent cells, this functional transformation must be engineered by a combination of post-translational modification and spatial reorganisation of existing sperm proteins. Indeed, evidence from our laboratory suggests that a key attribute of capacitation is the remodeling of the sperm surface architecture leading to the assembly and / or presentation of multimeric sperm-oocyte receptor complex(es). Through the novel application of Blue Native Polyacrylamide Gel Electrophoresis (BN-PAGE), we have secured the first direct evidence that human spermatozoa express a number of these protein complexes on their surface. Furthermore, we have demonstrated that a subset of these complexes harbour putative zona adhesion proteins and display strong affinity for solubilised zona pellucidae. In this study, we have extended our findings through the characterisation of one such complex containing arylsulfatase A (ASA), a protein with recognised affinity for sulfated ligands present within the zona pellucida. Through the application of immunohistochemistry and flow cytometry we revealed that ASA undergoes a capacitation-associated translocation to become expressed on the apical region of the human sperm head, a location compatible with a role in the mediation of sperm-zona pellucida interactions. This dramatic relocation was completely abolished by incubation of capacitating spermatozoa in exogenous cholesterol, suggesting that it may be driven in part by alteration in the membrane fluidity characteristics. Our current research is focused on confirming the role of ASA in human sperm-zona pellucida adhesion and elucidating the precise cellular mechanisms that underpin the proteins translocation to the cell surface.

Lysine glutarylation in human sperm is associated with progressive motility

2019 ◽  
Vol 34 (7) ◽  
pp. 1186-1194 ◽  
Author(s):  
Yi-min Cheng ◽  
Xiao-nian Hu ◽  
Zhen Peng ◽  
Ting-ting Pan ◽  
Fang Wang ◽  
...  
Keyword(s):  
Sperm Motility ◽  
Natural Science ◽  
Hot Spot ◽  
Human Sperm ◽  
Mature Sperm ◽  
Computer Assisted ◽  
Structured Illumination Microscopy ◽  
Progressive Motility ◽  
Wide Range

AbstractSTUDY QUESTIONIs there a role for lysine glutarylation (Kglu), a newly identified protein post-translational modification (PTM), in human sperm?SUMMARY ANSWERKglu occurs in several proteins located in the tail of human sperm, and it was reduced in asthenozoospermic (A) men and positively correlated with progressive motility of human sperm, indicating its important role in maintaining sperm motility.WHAT IS KNOWN ALREADYSince mature sperm are almost transcriptionally silent, PTM is regarded as an important pathway in regulating sperm function. However, only phosphorylation has been extensively studied in mature sperm to date. Protein lysine modification (PLM), a hot spot of PTMs, was rarely studied except for a few reports on lysine methylation and acetylation. As a newly identified PLM, Kglu has not been well characterized, especially in mature sperm.STUDY DESIGN, SIZE, DURATIONSperm samples were obtained from normozoospermic (N) men and A men who visited the reproductive medical center between February 2016 and January 2018. In total, 61 N men and 59 A men were recruited to participate in the study.PARTICIPANTS/MATERIALS, SETTING, METHODSKglu was examined by immunoblotting and immunofluorescence assays using a previously qualified pan-anti-glutaryllysine antibody that recognizes glutaryllysine in a wide range of sequence contexts (both in histones and non-histone substrates) but not the structurally similar malonyllysine and succinyllysine. The immunofluorescence assay was imaged using laser scanning confocal microscopy and super-resolution structured illumination microscopy. Sperm motility parameters were examined by computer-assisted sperm analysis.MAIN RESULTS AND THE ROLE OF CHANCEKglu occurs in several proteins (20–150 kDa) located in the tail of human sperm, especially in the middle piece and the latter part of the principal piece. Sperm Kglu was modulated by regulatory systems (enzymes and glutaryl-CoA) similar to those in HeLa cells. The mean level of sperm Kglu was significantly reduced in A men compared with N men (P < 0.001) and was positively correlated with progressive motility (P < 0.001). The sodium glutarate-induced elevation of Kglu levels in A men with lower Kglu levels in sperm significantly improved the progressive motility (P < 0.001). Furthermore, the reduced sperm Kglu levels in A men was accompanied by an increase in sperm glutaryl-CoA dehydrogenase (a regulatory enzyme of Kglu).LARGE SCALE DATAN/ALIMITATIONS, REASONS FOR CAUTIONAlthough the present study indicated the involvement of sperm Kglu in maintaining progressive motility of human sperm, the underlying mechanism needs to be investigated further.WIDER IMPLICATIONS OF THE FINDINGSThe findings of this study provide an insight into the novel role of Kglu in human sperm and suggest that abnormality of sperm PLMs may be one of the causes of asthenozoospermia.STUDY FUNDING/COMPETING INTEREST(S)National Natural Science Foundation of China (81 771 644 to T.L.; 31 671 204 to X.Z. and 81 871 207 to H.C.); National Basic Research Program of China (973 Program, 2015CB943003 to X.Z.); Natural Science Foundation of Jiangxi, China (20171ACB21006 and 20161BAB204167 to T.L.; 20165BCB18001 to X.Z.). The authors have no conflicts of interest to declare.

scholarly journals Current Insights and Latest Updates in Sperm Motility and Associated Applications in Assisted Reproduction

2020 ◽  
Author(s):  
Reyon Dcunha ◽  
Reda S. Hussein ◽  
Hanumappa Ananda ◽  
Sandhya Kumari ◽  
Satish Kumar Adiga ◽  
...  
Keyword(s):  
Sperm Motility ◽  
Reproductive Tract ◽  
Management Strategies ◽  
Human Sperm ◽  
Pharmacological Agents ◽  
Factors Affecting ◽  
Global Trend ◽  
Increased Risk

AbstractSpermatozoon is a motile cell with a special ability to travel through the woman’s reproductive tract and fertilize an oocyte. To reach and penetrate the oocyte, spermatozoa should possess progressive motility. Therefore, motility is an important parameter during both natural and assisted conception. The global trend of progressive reduction in the number and motility of healthy spermatozoa in the ejaculate is associated with increased risk of infertility. Therefore, developing approaches for maintaining or enhancing human sperm motility has been an important area of investigation. In this review we discuss the physiology of sperm, molecular pathways regulating sperm motility, risk factors affecting sperm motility, and the role of sperm motility in fertility outcomes. In addition, we discuss various pharmacological agents and biomolecules that can enhance sperm motility in vitro and in vivo conditions to improve assisted reproductive technology (ART) outcomes. This article opens dialogs to help toxicologists, clinicians, andrologists, and embryologists in understanding the mechanism of factors influencing sperm motility and various management strategies to improve treatment outcomes.

scholarly journals Co-incident signalling between μ-opioid and M3 muscarinic receptors at the level of Ca2+ release from intracellular stores: lack of evidence for Ins(1,4,5)P3 receptor sensitization

2003 ◽  
Vol 375 (3) ◽  
pp. 713-720 ◽  
Author(s):  
Damien S. K. SAMWAYS ◽  
Wen-hong LI ◽  
Stuart J. CONWAY ◽  
Andrew B. HOLMES ◽  
Martin D. BOOTMAN ◽  
...  
Keyword(s):  
Muscarinic Receptors ◽  
Opioid Receptors ◽  
Receptor Agonist ◽  
Flash Photolysis ◽  
Receptor Activation ◽  
Scanning Confocal Microscopy ◽  
Rate Of Decay ◽  
Μ Opioid Receptor ◽  
Μ Opioid Receptors ◽  
Insp3 Receptor

Activation of Gi/Go-coupled opioid receptors increases [Ca2+]i (intracellular free-Ca2+ concentration), but only if there is concomitant Gq-coupled receptor activation. This Gi/Go-coupled receptor-mediated [Ca2+]i increase does not appear to result from further production of InsP3 [Ins(1,4,5)P3] in SH-SY5Y cells. In the present study, fast-scanning confocal microscopy revealed that activation of μ-opioid receptors alone by 1 μM DAMGO ([d-Ala, NMe-Phe, Gly-ol]-enkephalin) did not stimulate the InsP3-dependent elementary Ca2+-signalling events (Ca2+ puffs), whereas DAMGO did evoke Ca2+ puffs when applied during concomitant activation of M3 muscarinic receptors with 1 μM carbachol. We next determined whether μ-opioid receptor activation might increase [Ca2+]i by sensitizing the InsP3 receptor to InsP3. DAMGO did not potentiate the amplitude of the [Ca2+]i increase evoked by flash photolysis of the caged InsP3 receptor agonist, caged 2,3-isopropylidene-InsP3, whereas the InsP3 receptor sensitizing agent, thimerosal (10 μM), did potentiate this response. DAMGO also did not prolong the rate of decay of the increase in [Ca2+]i evoked by flash photolysis of caged 2,3-isopropylidene-InsP3. Furthermore, DAMGO did not increase [Ca2+]i in the presence of the cell-membrane-permeable InsP3 receptor agonist, InsP3 hexakis(butyryloxymethyl) ester. Therefore it appears that μ-opioid receptors do not increase [Ca2+]i through either InsP3 receptor sensitization, enhancing the releasable pool of Ca2+ or inhibition of Ca2+ removal from the cytoplasm.

Properties of TAN-67, a nonpeptide δ-opioid receptor agonist, at cloned human δ-and μ-opioid receptors

1995 ◽  
Vol 291 (2) ◽  
pp. 129-134 ◽  
Author(s):  
Richard J. Knapp ◽  
Robert Landsman ◽  
Sue Waite ◽  
Ewa Malatynska ◽  
Eva Varga ◽  
...  
Keyword(s):  
Opioid Receptor ◽  
Opioid Receptors ◽  
Receptor Agonist ◽  
Opioid Receptor Agonist ◽  
Δ Opioid Receptor ◽  
Μ Opioid Receptors

scholarly journals Evaluation of the Efficiency of Two Different Freezing Media and Two Different Protocols to Preserve Human Spermatozoa from Cryoinjury

2016 ◽  
Vol 2016 ◽  
pp. 1-6 ◽  
Author(s):  
Gemma Fabozzi ◽  
Maria Flavia Starita ◽  
Emilia Rega ◽  
Alessandra Alteri ◽  
Antonio Colicchia ◽  
...  
Keyword(s):  
Sperm Quality ◽  
Human Sperm ◽  
Human Spermatozoa ◽  
Sperm Cryopreservation ◽  
Progressive Motility ◽  
Direct Addition ◽  
Sperm Sample ◽  
Sperm Survival ◽  
Better Than

It is universally recognized that cryopreservation impairs sperm quality. In order to improve postthawing sperm survival and motility, media of different composition and different protocols have been proposed. However, no clear evidence is available to understand which are the most efficient protocol and medium for sperm cryopreservation. The present study evaluates the efficiency of two different cryopreservation protocols and two common freezing media (FM) containing different cryoprotectants (CPs), TEST Yolk Buffer (TYB) and Sperm Freeze (SF), to preserve human sperm quality. Our data suggest that TYB is better than SF both in terms of postthaw viability and in terms of progressive motility, while the direct addition of FM to the sperm sample resulted in the most efficient protocol in terms of postthaw viability but not in terms of progressive motility.

Regulation of human sperm motility by opioid receptors

Andrologia ◽  
2011 ◽  
Vol 44 ◽  
pp. 578-585 ◽  
Author(s):  
E. Agirregoitia ◽  
N. Subiran ◽  
A. Valdivia ◽  
J. Gil ◽  
J. Zubero ◽  
...  
Keyword(s):  
Sperm Motility ◽  
Opioid Receptors ◽  
Human Sperm

Low physiological levels of prostaglandins E2 and F2α improve human sperm functions

2016 ◽  
Vol 28 (4) ◽  
pp. 434 ◽  
Author(s):  
Mariana Rios ◽  
Daniela V. Carreño ◽  
Carolina Oses ◽  
Nelson Barrera ◽  
Bredford Kerr ◽  
...  
Keyword(s):  
Intracellular Calcium ◽  
Sperm Motility ◽  
Acrosome Reaction ◽  
Seminal Fluid ◽  
Human Sperm ◽  
Human Spermatozoa ◽  
Control Solution ◽  
Prostaglandins E2 And F2α ◽  
Motility Parameters ◽  
Sperm Functions

Prostaglandins (PGs) have been reported to be present in the seminal fluid and cervical mucus, affecting different stages of sperm maturation from spermatogenesis to the acrosome reaction. This study assessed the effects of low physiological PGE2 and PGF2α concentrations on human sperm motility and on the ability of the spermatozoa to bind to the zona pellucida (ZP). Human spermatozoa were isolated from seminal samples with normal concentration and motility parameters and incubated with 1 μM PGE2, 1 μM PGF2α or control solution to determine sperm motility and the ability to bind to human ZP. The effects of both PGs on intracellular calcium levels were determined. Incubation for 2 or 18 h with PGE2 or PGF2α resulted in a significant (P < 0.05) increase in the percentage of spermatozoa with progressive motility. In contrast with PGF2α, PGE2 alone induced an increase in sperm intracellular calcium levels; however, the percentage of sperm bound to the human ZP was doubled for both PGs. These results indicate that incubation of human spermatozoa with low physiological levels of PGE2 or PGF2α increases sperm functions and could improve conditions for assisted reproduction protocols.

Sign in / Sign up

Export Citation Format

Share Document