FREE SHIPPING over $40
OVER 10000 FIVE-STAR REVIEWS
5% OFF ALL SUBSCRIPTIONS
100% HAPPINESS GUARANTEE
Analyze Diet
0
FEBS letters1997; 407(2); 201-206; doi: 10.1016/s0014-5793(97)00344-x

Isolation and characterization of heparin- and phosphorylcholine-binding proteins of boar and stallion seminal plasma. Primary structure of porcine pB1.

Abstract: In the bovine, seminal plasma heparin-binding proteins bind to sperm lipids containing the phosphorylcholine group and mediate the capacitating effects of heparin-like glycosaminoglycans during sperm residence in the female genital tract. We report the characterization of heparin- and phosphorylcholine-binding proteins of stallion and boar seminal plasma. Horse seminal plasma proteins HSP-1 and HSP-2, and boar protein pB1, belong to the same family as the bull heparin- and phosphorylcholine-binding proteins BSP-A1/2, BSP-A3, and BSP-30K. We have determined the amino acid sequence and posttranslational modifications of boar glycoprotein pB1. It contains 105 amino acids arranged into a mosaic structure consisting of a N-terminal 18-residue O-glycosylated polypeptide followed by two tandemly organized 40-45-residue fibronectin type II domains. pB1 displays 60-65% amino acid sequence similarity with its equine and bovine homologues. However, in their respective seminal plasmas, the BSP and the HSP proteins associate into 90-150-kDa oligomeric complexes, whereas pB1 forms a 35-40-kDa complex with spermadhesin AQN-1. In addition, pB1 appears to be identical to the recently described leukocyte adhesion regulator of porcine seminal fluid pAIF-1. Our results tie in with the hypothesis that homologous proteins from different mammalian species may display distinct biological activities, which may be related to species-specific aspects of sperm physiology.
Get Full Text
Publication Date: 1997-04-28 PubMed ID: 9166899DOI: 10.1016/s0014-5793(97)00344-xGoogle Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
LinkedInCopy
  • Comparative Study
  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The study focuses on the characterization and comparative study of proteins found in horse and pig seminal fluid, particularly those that bind to heparin and phosphorylcholine. These proteins play a crucial role in the fertilization process. Specifically, the researchers isolated and analyzed the structure of pB1, a protein in boar seminal plasma.

Characterization of Seminal Proteins

  • The researchers conducted a comparative study of heparin- and phosphorylcholine-binding proteins (proteins that bind to sperm lipids) in stallion and boar seminal fluid.
  • They identified that the proteins in horse seminal plasma called HSP-1 and HSP-2, and a protein in boar seminal fluid called pB1, are part of the same protein family as the bull proteins BSP-A1/2, BSP-A3, and BSP-30K.

Primary Structure of pB1

  • The researchers decoded the structure of a specific protein in boar seminal plasma, referred to as pB1.
  • pB1 is composed of 105 amino acids and is organized into a mosaic structure consisting of an 18-residue O-glycosylated polypeptide, followed by two 40-45-residue domains that resemble the structure of fibronectin, a high-molecular-weight glycoprotein of the extracellular matrix.
  • pB1 shows a significant sequence similarity (60-65%) with related proteins found in stallion and bull seminal fluid. However, the way these proteins associate in the seminal fluid is species-specific.
  • In boar seminal plasma, pB1 appears to assist in forming a 35-40-kDa complex with another protein spermadhesin AQN-1. The protein interaction does not resemble how homologous proteins act in other species’ seminal plasmas, demonstrating species-specific involvement.

Implications of the findings

  • The findings suggest that despite structural and sequence similarities, homologous proteins from different species may exhibit different biological activities.
  • These differences could be related to how different species’ sperm interact with these proteins, potentially influencing their fertilization capabilities, representing a significant area for reproductive biology research.

These findings help to understand the specific molecular interactions that take place during mammalian fertilization and the differences in these interactions across species. Such understanding is crucial for developing improved fertility treatments or contraceptives.

Cite This Article

APA
Calvete JJ, Raida M, Gentzel M, Urbanke C, Sanz L, Töpfer-Petersen E. (1997). Isolation and characterization of heparin- and phosphorylcholine-binding proteins of boar and stallion seminal plasma. Primary structure of porcine pB1. FEBS Lett, 407(2), 201-206. https://doi.org/10.1016/s0014-5793(97)00344-x

Publication

FEBS letters
ISSN: 0014-5793
NlmUniqueID: 0155157
Country: England
Language: English
Volume: 407
Issue: 2
Pages: 201-206

Researcher Affiliations

Calvete, J J
  • Institut für Reproduktionsmedizin, Tierärztliche Hochschule Hannover,Hannover-Kirchrode, Germany. jcalvete@repro.tiho-hannover.de
Raida, M
    Gentzel, M
      Urbanke, C
        Sanz, L
          Töpfer-Petersen, E

            MeSH Terms

            • Amino Acid Sequence
            • Animals
            • Carrier Proteins / chemistry
            • Glycoproteins / chemistry
            • Glycosylation
            • Heparin / metabolism
            • Horses
            • Male
            • Molecular Sequence Data
            • Peptide Mapping
            • Phosphorylcholine / metabolism
            • Semen / chemistry
            • Seminal Plasma Proteins
            • Sequence Analysis
            • Sequence Homology, Amino Acid
            • Species Specificity
            • Swine

            Citations

            This article has been cited 12 times.
            1. Rajabi-Toustani R, Mehr MR, Motamedi-Mojdehi R. Reduction of seminal plasma concentration can decrease detrimental effects of seminal plasma on chilled ram spermatozoa. Anim Reprod 2021 May 28;18(1):e20200211.
              doi: 10.1590/1984-3143-AR2020-0211pubmed: 34122651google scholar: lookup
            2. Tumova L, Zigo M, Sutovsky P, Sedmikova M, Postlerova P. Ligands and Receptors Involved in the Sperm-Zona Pellucida Interactions in Mammals. Cells 2021 Jan 12;10(1).
              doi: 10.3390/cells10010133pubmed: 33445482google scholar: lookup
            3. Johannisson A, Al-Essawe EM, Al-Saffar AK, Karkehabadi S, Lima-Verde I, Wulf M, Aurich C, Morrell JM. Season does not have a deleterious effect on proportions of stallion seminal plasma proteins. J Reprod Dev 2020 Jun 12;66(3):215-221.
              doi: 10.1262/jrd.2019-072pubmed: 32051351google scholar: lookup
            4. Pérez-Patiño C, Parrilla I, Li J, Barranco I, Martínez EA, Rodriguez-Martínez H, Roca J. The Proteome of Pig Spermatozoa Is Remodeled During Ejaculation. Mol Cell Proteomics 2019 Jan;18(1):41-50.
              doi: 10.1074/mcp.RA118.000840pubmed: 30257877google scholar: lookup
            5. Defaus S, Avilés M, Andreu D, Gutiérrez-Gallego R. Lectin-Binding Specificity of the Fertilization-Relevant Protein PDC-109 by Means of Surface Plasmon Resonance and Carbohydrate REcognition Domain EXcision-Mass Spectrometry. Int J Mol Sci 2018 Apr 4;19(4).
              doi: 10.3390/ijms19041076pubmed: 29617298google scholar: lookup
            6. Plante G, Lusignan MF, Lafleur M, Manjunath P. Interaction of milk proteins and Binder of Sperm (BSP) proteins from boar, stallion and ram semen. Reprod Biol Endocrinol 2015 Aug 15;13:92.
              doi: 10.1186/s12958-015-0093-1pubmed: 26272219google scholar: lookup
            7. Jois PS, Plante G, Thérien I, Manjunath P. Functional characterization of the domains of the bovine binder of SPerm 5 (BSP5) protein. Reprod Biol Endocrinol 2015 Jun 19;13:64.
              doi: 10.1186/s12958-015-0058-4pubmed: 26084664google scholar: lookup
            8. Anbazhagan V, Sankhala RS, Singh BP, Swamy MJ. Isothermal titration calorimetric studies on the interaction of the major bovine seminal plasma protein, PDC-109 with phospholipid membranes. PLoS One 2011;6(10):e25993.
              doi: 10.1371/journal.pone.0025993pubmed: 22022488google scholar: lookup
            9. Kumar V, Hassan MI, Tomar AK, Kashav T, Nautiyal J, Singh S, Singh TP, Yadav S. Proteomic analysis of heparin-binding proteins from human seminal plasma: a step towards identification of molecular markers of male fertility. J Biosci 2009 Dec;34(6):899-908.
              doi: 10.1007/s12038-009-0104-5pubmed: 20093743google scholar: lookup
            10. Manjunath P, Lefebvre J, Jois PS, Fan J, Wright MW. New nomenclature for mammalian BSP genes. Biol Reprod 2009 Mar;80(3):394-7.
              doi: 10.1095/biolreprod.108.074088pubmed: 18923155google scholar: lookup
            11. Villemure M, Lazure C, Manjunath P. Isolation and characterization of gelatin-binding proteins from goat seminal plasma. Reprod Biol Endocrinol 2003 Apr 28;1:39.
              doi: 10.1186/1477-7827-1-39pubmed: 12737634google scholar: lookup
            12. Bezouska K, Sklenár J, Novák P, Halada P, Havlícek V, Kraus M, Tichá M, Jonáková V. Determination of the complete covalent structure of the major glycoform of DQH sperm surface protein, a novel trypsin-resistant boar seminal plasma O-glycoprotein related to pB1 protein. Protein Sci 1999 Jul;8(7):1551-6.
              doi: 10.1110/ps.8.7.1551pubmed: 10422846google scholar: lookup
            Subscribe to our newsletter
            Join 99,727 horse owners like you who receive our email updates on horse health and nutrition.