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Home / Equine Research Bank / J Biosci / Modulation of chaperone-like and membranolytic activities of...
Journal of biosciences2018; 42(3); 469-479; doi: 10.1007/s12038-017-9693-6

Modulation of chaperone-like and membranolytic activities of major horse seminal plasma protein HSP-1/2 by L-carnitine.

Abstract: The major protein of horse seminal plasma, HSP-1/2, exhibits membranolytic and chaperone-like activities and plays a crucial role in regulating sperm capacitation. L-Carnitine is a small polar molecule present in high concentrations in mammalian seminal plasma. The present results demonstrate that L-carnitine binds to HSP-1/2 and increases its thermal stability, enhances cooperativity of its chemical unfolding and decreases both chaperone-like and membranolytic activities of this protein. The HSP-1/2-L-carnitine complex exhibits anti-oxidative behaviour by inhibiting the production of hydroxyl radicals, suggesting that it can protect other constituents of seminal plasma from damage by hydroxyl radicals. As HSP-1/2 and L-carnitine share the same spatiotemporal location in the horse reproductive tract, this interaction is physiologically significant and may prevent premature interaction of HSP-1/2 with sperm, which in turn regulates the sperm capacitation.
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Publication Date: 2018-01-24 PubMed ID: 29358560DOI: 10.1007/s12038-017-9693-6Google Scholar: Lookup
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Summary

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The research paper explores the effects of L-carnitine, a molecule present in mammalian seminal plasma, on the major protein of horse seminal plasma, HSP-1/2, showing that L-carnitine increases its stability and reduces its membrane disruption and internal stress protection activities. This interaction also prevents damage to other contents of the seminal plasma by hydroxyl radicals, and as a result, regulates sperm capacitation.

Role of HSP-1/2 and L-Carnitine in Horse Seminal Plasma

  • The horse seminal plasma protein, HSP-1/2, has both membranolytic (disrupting cell membranes) and chaperone-like (protecting proteins from stress damage) activities.
  • Vital for regulating sperm capacitation (the process which makes sperm capable of fertilizing an egg), the HSP-1/2 protein is significantly influenced by the presence of L-carnitine, a molecule with a high concentration in seminal plasma.

Effects of L-Carnitine on HSP-1/2

  • The research findings suggest that when L-Carnitine binds to HSP-1/2, it increases the protein’s thermal stability and enhances the cooperativity of its chemical unfolding, which is the process in which a protein loses its structure under chemical stress.
  • This binding with L-carnitine also decreases the membranolytic and chaperone-like activities of HSP-1/2. By reducing these activities, the protein contributes less to cell membrane disruption and internal stress protection.

Anti-Oxidative Behaviour of HSP-1/2-L-Carnitine Complex

  • While the decreased activities of HSP-1/2 may seem harmful, the study ultimately reveals that the HSP-1/2-L-carnitine complex exhibits anti-oxidative behaviour. This quality allows it to inhibit the production of harmful hydroxyl radicals, thereby preventing other components of seminal plasma from damage.

Physiological Significance

  • HSP-1/2 and L-carnitine both share the same location in the horse reproductive tract, suggesting this interaction is physiologically significant.
  • Through the regulation of HSP-1/2, L-carnitine contributes to preventing premature interaction of the protein with sperm, thus effectively regulating sperm capacitation. Without premature interaction, the sperm are more likely to successfully complete capacitation, increasing fertility potential.

Cite This Article

APA
Sudheer Kumar C, Swamy MJ. (2018). Modulation of chaperone-like and membranolytic activities of major horse seminal plasma protein HSP-1/2 by L-carnitine. J Biosci, 42(3), 469-479. https://doi.org/10.1007/s12038-017-9693-6

Publication

Journal of biosciences
ISSN: 0973-7138
NlmUniqueID: 8100809
Country: India
Language: English
Volume: 42
Issue: 3
Pages: 469-479

Researcher Affiliations

Sudheer Kumar, C
  • School of Chemistry, University of Hyderabad, Hyderabad 500 046, India.
Swamy, Musti J

    MeSH Terms

    • Animals
    • Antioxidants / metabolism
    • Antioxidants / pharmacology
    • Carnitine / metabolism
    • Carnitine / pharmacology
    • Carrier Proteins / genetics
    • Carrier Proteins / metabolism
    • Carrier Proteins / pharmacology
    • Gene Expression
    • Glycoproteins / genetics
    • Glycoproteins / metabolism
    • Glycoproteins / pharmacology
    • Horses
    • Hydroxyl Radical / antagonists & inhibitors
    • Hydroxyl Radical / metabolism
    • Male
    • Molecular Chaperones / genetics
    • Molecular Chaperones / metabolism
    • Molecular Chaperones / pharmacology
    • Protein Binding
    • Protein Folding
    • Protein Stability
    • Semen / chemistry
    • Semen / metabolism
    • Seminal Plasma Proteins / genetics
    • Seminal Plasma Proteins / metabolism
    • Seminal Plasma Proteins / pharmacology
    • Sperm Capacitation / drug effects
    • Sperm Capacitation / physiology
    • Spermatozoa / drug effects
    • Spermatozoa / physiology

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    Citations

    This article has been cited 1 times.
    1. Eronina TB, Mikhaylova VV, Chebotareva NA, Tugaeva KV, Kurganov BI. Effect of Betaine and Arginine on Interaction of αB-Crystallin with Glycogen Phosphorylase b.. Int J Mol Sci 2022 Mar 30;23(7).
      doi: 10.3390/ijms23073816pubmed: 35409175google scholar: lookup
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