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

    • Fulltext


        Click here to view fulltext PDF

      Permanent link:

    • Keywords


      Capacitation; membranolytic activity; molecular chaperone; oxidative stress

    • Abstract


      The major protein of horse seminal plasma, HSP-1/2, exhibits membranolytic and chaperone-like activities and plays acrucial role in regulating sperm capacitation. L-Carnitine is a small polar molecule present in high concentrations inmammalian seminal plasma. The present results demonstrate that L-carnitine binds to HSP-1/2 and increases its thermalstability, enhances cooperativity of its chemical unfolding and decreases both chaperone-like and membranolytic activitiesof this protein. The HSP-1/2–L-carnitine complex exhibits anti-oxidative behaviour by inhibiting the production ofhydroxyl radicals, suggesting that it can protect other constituents of seminal plasma from damage by hydroxyl radicals. AsHSP-1/2 and L-carnitine share the same spatiotemporal location in the horse reproductive tract, this interaction is physiologicallysignificant and may prevent premature interaction of HSP-1/2 with sperm, which in turn regulates the spermcapacitation.

    • Author Affiliations



      1. School of Chemistry, University of Hyderabad, Hyderabad 500 046, India
    • Dates

  • Journal of Biosciences | News

    • Editorial Note on Continuous Article Publication

      Posted on July 25, 2019

      Click here for Editorial Note on CAP Mode

© 2017-2019 Indian Academy of Sciences, Bengaluru.