Abstract

Mouse vas deferens protein (AKR1B7), a member of the aldo-keto reductase family, was purified to homogeneity. Antibodies raised to AKR1B7 revealed an aldo-keto reductase on the human sperm surface, while confocal microscopy experiments demonstrated that this enzyme covered the entire human sperm surface and was concentrated on the mid-piece. Further functional characterisation of a recombinant form of AKR1B7 showed that the likely role of AKR1B7 is the reduction of the reactive aldehyde, acrolein, a by-product of spermine catabolism in the reproductive tract. A similar acrolein detoxification activity was displayed by human sperm membrane extracts but was not present in seminal plasma. These results indicate that human sperm possess an aldo-keto reductase on their membrane surface and are thus enzymatically protected against reactive aldehyde species both in the male and female reproductive tract.

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