Effects of scrotal heating on sperm surface protein PH-20 expression in sheep

2004 ◽  
Vol 68 (1) ◽  
pp. 103-114 ◽  
Author(s):  
Jean S. Fleming ◽  
Fu Yu ◽  
Robin M. McDonald ◽  
Stuart A. Meyers ◽  
Grant W. Montgomery ◽  
...  
Keyword(s):  
Surface Protein ◽  
Sperm Surface ◽  
Scrotal Heating

scholarly journals The Ubiquitin-Proteasome System Does Not Regulate the Degradation of Porcine β-Microseminoprotein during Sperm Capacitation

2020 ◽  
Vol 21 (11) ◽  
pp. 4151
Author(s):  
Lucie Tumova ◽  
Michal Zigo ◽  
Peter Sutovsky ◽  
Marketa Sedmikova ◽  
Pavla Postlerova
Keyword(s):  
Seminal Plasma ◽  
Plasma Proteins ◽  
Protein Composition ◽  
Surface Protein ◽  
Ubiquitin Proteasome System ◽  
Sperm Capacitation ◽  
Sperm Surface ◽  
Ubiquitin Proteasome ◽  
Seminal Plasma Proteins

Sperm capacitation, one of the key events during successful fertilization, is associated with extensive structural and functional sperm remodeling, beginning with the modification of protein composition within the sperm plasma membrane. The ubiquitin-proteasome system (UPS), a multiprotein complex responsible for protein degradation and turnover, participates in capacitation events. Previous studies showed that capacitation-induced shedding of the seminal plasma proteins such as SPINK2, AQN1, and DQH from the sperm surface is regulated by UPS. Alterations in the sperm surface protein composition also relate to the porcine β-microseminoprotein (MSMB/PSP94), seminal plasma protein known as immunoglobulin-binding factor, and motility inhibitor. MSMB was detected in the acrosomal region as well as the flagellum of ejaculated boar spermatozoa, while the signal disappeared from the acrosomal region after in vitro capacitation (IVC). The involvement of UPS in the MSMB degradation during sperm IVC was studied using proteasomal interference and ubiquitin-activating enzyme (E1) inhibiting conditions by image-based flow cytometry and Western blot detection. Our results showed no accumulation of porcine MSMB either under proteasomal inhibition or under E1 inhibiting conditions. In addition, the immunoprecipitation study did not detect any ubiquitination of sperm MSMB nor was MSMB detected in the affinity-purified fraction containing ubiquitinated sperm proteins. Based on our results, we conclude that UPS does not appear to be the regulatory mechanism in the case of MSMB and opening new questions for further studies. Thus, the capacitation-induced processing of seminal plasma proteins on the sperm surface may be more complex than previously thought, employing multiple proteolytic systems in a non-redundant manner.

Monoclonal antibody against a 52 K sperm surface protein inhibits sperm-zona pellucida interactions in the rat

1995 ◽  
Vol 272 (2) ◽  
pp. 123-133 ◽  
Author(s):  
Marlene S. Dias Alves ◽  
Maria Sonia Martins ◽  
Sérgio D. J. Pena
Keyword(s):  
Monoclonal Antibody ◽  
Zona Pellucida ◽  
Surface Protein ◽  
Sperm Surface

scholarly journals The gene for the human tMDC I sperm surface protein is non-functional: implications for its proposed role in mammalian sperm–egg recognition

1998 ◽  
Vol 334 (1) ◽  
pp. 171-176 ◽  
Author(s):  
Jan FRAYNE ◽  
Len HALL
Keyword(s):  
Plasma Membrane ◽  
Macaca Fascicularis ◽  
Surface Protein ◽  
Human Testis ◽  
Egg Recognition ◽  
Integrin Receptor ◽  
Western Blots ◽  
Sperm Surface ◽  
Mammalian Sperm ◽  
Functional Implications

The sperm surface antigen tMDC I (also known as cyritestin) has been proposed to play a role in sperm–egg binding in the mouse via an interaction between its disintegrin-like domain and an integrin receptor on the oolemma plasma membrane. Here we report the cloning and sequence of human tMDC I transcripts and show that they are non-functional, owing to the presence of a variety of deletions, insertions and in-frame termination codons. The absence of a tMDC I protein is further supported by the lack of immunoreactivity on Western blots of human testis and sperm extracts probed with macaque (Macaca fascicularis) and human anti-tMDC I antisera.

scholarly journals Redox control of surface protein sulphhydryls in bovine spermatozoa reversibly modulates sperm adhesion to the oviductal epithelium and capacitation

Reproduction ◽  
2009 ◽  
Vol 138 (1) ◽  
pp. 33-43 ◽  
Author(s):  
Roberto Gualtieri ◽  
Valentina Mollo ◽  
Gennaro Duma ◽  
Riccardo Talevi
Keyword(s):  
Surface Protein ◽  
Surface Proteins ◽  
Sperm Surface ◽  
Sperm Suspension ◽  
Oviductal Epithelium ◽  
Bovine Spermatozoa ◽  
Sulphated Glycosaminoglycans ◽  
Oviductal Fluid ◽  
Adhesion Assays

Oviductal fluid molecules, such as sulphated glycosaminoglycans and disulphide-reductants, may represent periovulatory signals for the release of spermatozoa from the oviductal reservoir in the bovine species. Disulphide-reductants release spermatozoa through the reduction of sperm-surface disulphides to sulphhydryls (SH). Herein, we studied sperm-surface protein SH through labelling with maleimidylpropionyl biocytin in the initial sperm suspension, in the subpopulations able and unable to adhere to the in vitro cultured oviductal epithelium, and in spermatozoa released either through the disulphide-reductant penicillamine (PEN) or the sulphated glycosaminoglycan heparin (HEP). Adhesion assays were performed to study the ability of released spermatozoa to readhere to the oviductal epithelium. Results showed that the level of SH in sperm-surface proteins was: 1) low in adhering spermatozoa; 2) high in spermatozoa unable to adhere; and 3) markedly increased in released spermatozoa. Adhesion assays showed that: 1) PEN-released spermatozoa promptly recovered adhesion after removal of the disulphide-reductant and could be released again in response to PEN; 2) conversely, a limited number of HEP-released spermatozoa was able to readhere to the oviductal epithelium and this ability was not affected by HEP removal. Recovery of adhesion was associated to reoxidation of sperm-surface protein SH and to the reversal of capacitation. In conclusion, redox modulation of sperm-surface protein SH is involved in the release of spermatozoa adhering to the oviduct in vitro; the reversible action of disulphide-reductants might be responsible for intermittent phases of adhesions and releases; and the irreversible action of HEP indicates that it may represent a terminal releasing signal.

scholarly journals Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion.

1987 ◽  
Vol 104 (1) ◽  
pp. 141-149 ◽  
Author(s):  
P Primakoff ◽  
H Hyatt ◽  
J Tredick-Kline
Keyword(s):  
Membrane Fusion ◽  
Disulfide Bonds ◽  
Surface Protein ◽  
Equatorial Region ◽  
Proteolytic Fragment ◽  
Sperm Surface ◽  
Antigenic Activity ◽  
Head Surface ◽  
Sds Page ◽  
Egg Membrane

Sperm-egg plasma membrane fusion during fertilization was studied using guinea pig gametes and mAbs to sperm surface antigens. The mAb, PH-30, strongly inhibited sperm-egg fusion in a concentration-dependent fashion. When zona-free eggs were inseminated with acrosome-reacted sperm preincubated in saturating (140 micrograms/ml) PH-30 mAb, the percent of eggs showing fusion was reduced 75%. The average number of sperm fused per egg was also reduced by 75%. In contrast a control mAb, PH-1, preincubated with sperm at 400 micrograms/ml, caused no inhibition. The PH-30 and PH-1 mAbs apparently recognize the same antigen but bind to two different determinants. Both mAbs immunoprecipitated the same two 125I-labeled polypeptides with Mr 60,000 (60 kD) and Mr 44,000 (44 kD). Boiling a detergent extract of sperm severely reduced the binding of PH-30 but had essentially no effect on the binding of PH-1, indicating that the two mAbs recognize different epitopes. Immunoelectron microscopy revealed that PH-30 mAb binding was restricted to the sperm posterior head surface and was absent from the equatorial region. The PH-30 and PH-1 mAbs did not bind to sperm from the testis, the caput, or the corpus epididymis. PH-30 mAb binding was first detectable on sperm from the proximal cauda epididymis, i.e., sperm at the developmental stage where fertilization competence appears. After purification by mAb affinity chromatography, the PH-30 protein retained antigenic activity, binding both the PH-30 and PH-1 mAbs. The purified protein showed two polypeptide bands of 60 and 44 kD on reducing SDS PAGE. The two polypeptides migrated further (to approximately 49 kD and approximately 33 kD) on nonreducing SDS PAGE, showing that they do not contain interchain disulfide bonds, but probably have intrachain disulfides. 44 kD appears not to be a proteolytic fragment of 60 kD because V8 protease digestion patterns did not reveal related peptide patterns from the 44- and 60-kD bands. In the absence of detergent, the purified protein precipitates, suggesting that either 60 or 44 kD could be an integral membrane polypeptide.

Origin, localization and binding abilities of boar DQH sperm surface protein tested by specific monoclonal antibodies

2007 ◽  
Vol 74 (1-2) ◽  
pp. 103-113 ◽  
Author(s):  
P. Maňásková ◽  
J. Pěknicová ◽  
F. Elzeinová ◽  
M. Tichá ◽  
V. Jonáková
Keyword(s):  
Monoclonal Antibodies ◽  
Surface Protein ◽  
Sperm Surface

scholarly journals Transcripts encoding the sperm surface protein tMDC II are non-functional in the human

1999 ◽  
Vol 341 (3) ◽  
pp. 771 ◽  
Author(s):  
Jan FRAYNE ◽  
Elizabeth A.C. DIMSEY ◽  
Jenny A. JURY ◽  
Len HALL
Keyword(s):  
Surface Protein ◽  
Sperm Surface
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