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|Title:||Spermatozoa from a marsupial, the brushtail possum, contain beta 1,4-galactosyltransferase|
|Citation:||Reproduction Fertility and Development, 2008; 20(3):402-407|
|Publisher:||C S I R O Publishing|
|A. G. Braundmeier, William G. Breed and D. J. Miller|
|Abstract:||Beta1,4-galactosyltransferase-I (GalTase-I) is one of the key molecules on the sperm surface of eutherian mammals that is likely to be involved in binding to the egg coat, the zona pellucida, to mediate sperm-egg interaction. In laboratory mice, the species for which most data are available, this protein functions as a receptor for the zona pellucida protein ZP3 of the oocyte and, upon binding, triggers the sperm acrosome reaction. In the present study, we investigated the presence and abundance of GalTase-I in epididymal sperm extracts of a marsupial, the brushtail possum, Trichosurus vulpecula. For this, spermatozoa were collected from cauda epididymides and the amount of beta1,4-galactosyltransferase activity in washed sperm extracts was compared with that of porcine spermatozoa. Overall beta1,4-galactosyltransferase enzyme activity was found to be more abundant in possum sperm extracts than those from porcine spermatozoa (P<0.05). Immunoblots with an antibody to mouse GalTase-I revealed that the molecular weight of possum spermatozoa GalTase-I was 66 kDa, which is similar to the molecular weight of GalTase-I in spermatozoa from eutherian mammals. The molecular weight of GalTase-I was the same in sperm extracts collected from the caput and cauda epididymides. These results demonstrate that GalTase-I is indeed present in possum spermatozoa and thus it may be a gamete receptor molecule on the sperm surface of marsupials as well as those of eutherian mammals.|
|Description:||Copyright © CSIRO 2008|
|Appears in Collections:||Anatomical Sciences publications|
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