Alpha-mannosidase activity in stallion epididymal fluid and spermatozoa

Theriogenology
C A RetamalM L López

Abstract

The expression of α-D-mannosidase activity was fluorometrically and electrophoretically assessed in spermatozoa, epididymal fluid and homogenates of stallion epididymal tissue. Enzyme activity had regional differences; it was higher (P<0.05) in samples from the cauda epididymal region than in samples from the proximal caput region (largely composed of efferent ducts). Based on enzyme activity, as a function of pH of the assay substrate, electrophoretic analysis in native and native/SDS-PAGE conditions, and the effect of inhibitors or activators, we inferred the presence of at least two catalytically active forms of α-D-mannosidase. The neutral form of the enzyme (α-mannosidase II) was activated by Co2+, whereas the acid form (optimum pH 3.5 to 4.0) was sensitive to swainsonine (an inhibitor of α-mannosidase I), stabilized or stimulated by Zn2+, and not activated by Co2+ (activator of the neutral form). The activity of the acid form of the enzyme was highest in the epididymal fluid, where it seemed to be mainly in a secretory form. This form of the enzyme may have a role in plasma membrane remodeling associated with sperm maturation. In contrast, the activity of α-mannosidase II was higher in mature spermatozoa. It has been post...Continue Reading

References

Jan 1, 1992·Biology of Reproduction·D R TulsianiM C Orgebin-Crist
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Jun 26, 2007·Asian Journal of Andrology·R John AitkenMark A Baker
Jan 13, 2009·Human Reproduction Update·Gail A Cornwall

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Citations

Jan 15, 2014·Animal Reproduction Science·G M DiasC A Retamal
Jun 16, 2015·Molecular Reproduction and Development·Lara C Meneguelli De SouzaMaria Luisa Lopez
Apr 14, 2015·Biotechnology Progress·David BrühlmannHervé Broly

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