Dual function of the selenoprotein PHGPx during sperm maturation

被引：638

作者：

Ursini, F

Heim, S

Kiess, M

Maiorino, M

Roveri, A

Wissing, J

Flohé, L

机构：

[1] Tech Univ Braunschweig, Dept Biochem, D-38124 Braunschweig, Germany

[2] Univ Padua, Dipartimento Chim Biol, I-35121 Padua, Italy

[3] Natl Res Ctr Biotechnol, D-38124 Braunschweig, Germany

来源：

SCIENCE | 1999年 / 285卷 / 5432期

关键词：

D O I：

10.1126/science.285.5432.1393

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：1393 / 1396

页数：4

共 45 条

[1] Cloning, expression, and chromosomal localization of the rat mitochondrial capsule selenoprotein gene (MCS), the reading frame does not contain potential UGA selenocysteine codons [J].