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Biology of Reproduction 67, 967-971 (2002)
© 2002 Society for the Study of Reproduction, Inc.


Regular Article

Male Fertility Is Linked to the Selenoprotein Phospholipid Hydroperoxide Glutathione Peroxidase1

Carlo Forestaa, Leopold Flohéb, Andrea Garollaa, Antonella Roveric, Fulvio Ursinic, and Matilde Maiorino2,,a

a Department of Medical and Surgical Sciences, Clinica Medica 3, University of Padova, I-35128 Padova, Italy b Department of Biochemistry, Technical University of Braunschweig, D-38124 Braunschweig, Germany c Department of Biological Chemistry, University of Padova, I-35121 Padova, Italy

The selenoprotein phospholipid hydroperoxide glutathione peroxidase (PHGPx) accounts for almost the entire selenium content of mammalian testis. PHGPx is abundantly expressed in spermatids as active peroxidase but is transformed to an oxidatively inactivated protein in mature sperm, where it is a major constituent of the mitochondrial capsule in the midpiece. Male infertility in selenium-deficient animals, which is characterized by impaired sperm motility and morphological midpiece alterations, is considered to result from insufficient PHGPx content. We studied the relationship between sperm PHGPx, measured as rescued activity, and human fertility. Sperm specimens from 75 infertile men and 37 controls were analyzed for fertility-related parameters according to World Health Organization criteria. The PHGPx protein content was estimated after reductive solubilization of the spermatozoa by measuring the rescued PHGPx activity. Rescued PHGPx activity of infertile men ranged significantly below that of controls (93.2 ± 60.1 units/mg sperm protein vs. 187.5 ± 55.3 units/mg) and was particularly low in oligoasthenozoospermic specimens (61.93 ± 45.42 units/mg; P < 0.001 compared with controls and asthenozoospermic samples). Rescued PHGPx activity was correlated positively with viability, morphological integrity, and most profoundly forward motility (r = 0.35, 0.44, and 0.45, respectively). In isolated motile samples, motility decreased faster with decreasing PHGPx content. In humans, PHGPx appears to be indispensable for structural integrity of spermatozoa and to codetermine sperm motility and viability. Because the content of PHGPx, irrespective of the cause of alteration, is correlated with fertility-related parameters, PHGPx can be considered a predictive measure for fertilization capacity.

First decision: 20 February 2002.

1 This work was supported by the Deutsche Forschungsgemeinschaft (grant Fl 61/12-1) and by the Italian Ministry of Education.

2 Correspondence: Matilde Maiorino, Department of Biological Chemistry, University of Padova, Viale G. Colombo, 3, I-35121 Padova, Italy. FAX: 39 049 8073310; mmaior{at}mail.bio.unipd.it




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