Dual Function of the Selenoprotein PHGPx During Sperm Maturation

  • Fulvio Ursini
    Dipartmento di Chimica Biologica, Università di Padova, Viale G. Colombo 3, I-35121 Padova, Italy.
  • Sabina Heim
    National Research Centre for Biotechnology (GBF), Mascheroder Weg 1, D-38124 Braunschweig, Germany.
  • Michael Kiess
    National Research Centre for Biotechnology (GBF), Mascheroder Weg 1, D-38124 Braunschweig, Germany.
  • Matilde Maiorino
    Dipartmento di Chimica Biologica, Università di Padova, Viale G. Colombo 3, I-35121 Padova, Italy.
  • Antonella Roveri
    Dipartmento di Chimica Biologica, Università di Padova, Viale G. Colombo 3, I-35121 Padova, Italy.
  • Josef Wissing
    National Research Centre for Biotechnology (GBF), Mascheroder Weg 1, D-38124 Braunschweig, Germany.
  • Leopold Flohé
    Department of Biochemistry, Technical University of Braunschweig, Mascheroder Weg 1, D-38124 Braunschweig, Germany.

抄録

<jats:p>The selenoprotein phospholipid hydroperoxide glutathione peroxidase (PHGPx) changes its physical characteristics and biological functions during sperm maturation. PHGPx exists as a soluble peroxidase in spermatids but persists in mature spermatozoa as an enzymatically inactive, oxidatively cross-linked, insoluble protein. In the midpiece of mature spermatozoa, PHGPx protein represents at least 50 percent of the capsule material that embeds the helix of mitochondria. The role of PHGPx as a structural protein may explain the mechanical instability of the mitochondrial midpiece that is observed in selenium deficiency.</jats:p>

収録刊行物

  • Science

    Science 285 (5432), 1393-1396, 1999-08-27

    American Association for the Advancement of Science (AAAS)

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