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Science 27 August 1999:
Vol. 285. no. 5432, pp. 1393 - 1396
DOI: 10.1126/science.285.5432.1393
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Reports

Dual Function of the Selenoprotein PHGPx During Sperm Maturation

Fulvio Ursini, 1 Sabina Heim, 2 Michael Kiess, 2 Matilde Maiorino, 1 Antonella Roveri, 1 Josef Wissing, 2 Leopold Flohé 3*

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.

1 Dipartmento di Chimica Biologica, Università di Padova, Viale G. Colombo 3, I-35121 Padova, Italy.
2 National Research Centre for Biotechnology (GBF), Mascheroder Weg 1, D-38124 Braunschweig, Germany.
3 Department of Biochemistry, Technical University of Braunschweig, Mascheroder Weg 1, D-38124 Braunschweig, Germany.
*   To whom correspondence should be addressed. E-mail: lfl{at}gbf.de

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   Abstract »    Full Text »    PDF »
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   Abstract »    Full Text »    PDF »


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