CD26 and adenosine deaminase interaction: its role in the fusion between horse membrane vesicles and spermatozoa.
Abstract: Membrane vesicles of horse seminal plasma present at their surface a highly specific serine-type protease, dipeptidyl peptidase IV/CD26, a surface antigen known to characterize human prostasomes. Horse sperm cells expressed at their surface A(1) adenosine receptors (A(1)AR) and ecto-adenosine deaminase (ecto-ADA), both detected by immunoblot analysis, whereas CD26 was visualized at the equatorial segment by immunofluorescence microscopy. In addition to CD26, horse membrane vesicles showed ecto-ADA. The fusion process between horse sperm cells and vesicles was evidenced by confocal microscopy, which showed the localization of CD26 at the postacrosomal region and at the midpiece of the spermatozoa after incubation with vesicles. Moreover, a similar localization of CD26 and ecto-ADA on the spermatozoa was evidenced after fusion. Our results suggest that the interaction CD26/ecto-ADA might be responsible for fusion. Since A(1)ARs are said to be second receptors for ecto-ADA to form ecto-ADA/A(1)AR complexes, and since horse spermatozoa have A(1)ARs at their surface, the interaction CD26/ecto-ADA/A(1)AR during the fusion process cannot be ruled out.
Publication Date: 1999-08-24 PubMed ID: 10456860DOI: 10.1095/biolreprod61.3.802Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research article discusses the potential role of CD26 and adenosine deaminase (ecto-ADA) interaction in the fusion between horse membrane vesicles and spermatozoa. It suggests that this interaction may ultimately be responsible for facilitating this fusion process.
Background Information
- Horse seminal plasma contains membrane vesicles which have a specific serine-type protease known as dipeptidyl peptidase IV or CD26 at their surface. This antigen is known to characterize human prostasomes as well.
- Like these vesicles, horse sperm cells also express CD26, along with A(1) adenosine receptors (A(1)ARs) and ecto-adenosine deaminase (ecto-ADA), both of which are confirmed through immunoblot analysis.
- Through immunofluorescence microscopy, the scientists were able to visualize CD26 specifically at the equatorial segment of the horse sperm cells.
Fusion Process
- The fusion process of horse sperm cells and vesicles was observed using confocal microscopy, showing that CD26 localizes at the postacrosomal region and midpiece of the spermatozoa after interaction with the vesicles.
- The study also observed a similar location of CD26 and ecto-ADA on the sperm cells following fusion, hinting towards a potential interaction.
Significance of CD26/Ecto-ADA Interaction
- The study’s results propose that the interaction between CD26 and ecto-ADA might be responsible for the fusion of horse sperm and vesicles. This could potentially shed light on a novel mechanism in sperm-egg fusion, although more validation is needed for this hypothesis.
- Furthermore, considering that A(1)ARs are suggested to be secondary receptors for ecto-ADA, forming ecto-ADA/A(1)AR complexes, and since horse sperm cells have A(1)ARs at their surface, the research puts forth that the interaction of CD26/ecto-ADA/A(1)AR during the fusion process cannot be discounted.
Without a more thorough investigation, the exact role of CD26 and ecto-ADA interaction in the sperm-vesicle fusion process cannot be definitively determined. However, this study provides important groundwork for further exploration into the subject.
Cite This Article
APA
Minelli A, Allegrucci C, Mezzasoma I, Ronquist G, Lluis C, Franco R.
(1999).
CD26 and adenosine deaminase interaction: its role in the fusion between horse membrane vesicles and spermatozoa.
Biol Reprod, 61(3), 802-808.
https://doi.org/10.1095/biolreprod61.3.802 Publication
Researcher Affiliations
- Dipartimento di Biologia Cellulare e Molecolare, Università di Perugia, 06123 Perugia, Italia. albami@tin.it
MeSH Terms
- Adenosine Deaminase / analysis
- Animals
- Cell Membrane / chemistry
- Cell Membrane / physiology
- Dipeptidyl Peptidase 4 / analysis
- Fluorescent Antibody Technique
- Horses
- Immunoblotting
- Male
- Membrane Fusion
- Microscopy, Confocal
- Microscopy, Fluorescence
- Receptors, Purinergic P1 / analysis
- Semen
- Spermatozoa / physiology
- Spermatozoa / ultrastructure
Citations
This article has been cited 5 times.- Dubois L, Ronquist KK, Ek B, Ronquist G, Larsson A. Proteomic Profiling of Detergent Resistant Membranes (Lipid Rafts) of Prostasomes. Mol Cell Proteomics 2015 Nov;14(11):3015-22.
- Ronquist G. Prostasomes: Their Characterisation: Implications for Human Reproduction: Prostasomes and Human Reproduction. Adv Exp Med Biol 2015;868:191-209.
- Waldenström A, Gennebäck N, Hellman U, Ronquist G. Cardiomyocyte microvesicles contain DNA/RNA and convey biological messages to target cells. PLoS One 2012;7(4):e34653.
- Arienti G, Carlini E, Saccardi C, Palmerini CA. Role of human prostasomes in the activation of spermatozoa. J Cell Mol Med 2004 Jan-Mar;8(1):77-84.
- Troisi A, Schrank M, Bellezza I, Fallarino F, Pastore S, Verstegen JP, Pieramati C, Di Michele A, Talesa VN, Martìnez Barbitta M, Orlandi R, Polisca A. Expression of CD13 and CD26 on extracellular vesicles in canine seminal plasma: preliminary results. Vet Res Commun 2024 Feb;48(1):357-366.
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