Ae. Lamont et al., PROTEIN-SYNTHESIS AND SECRETION BY THE EPIDIDYMIS OF THE BRUSHTAIL POSSUM, TRICHOSURUS-VULPECULA, Journal of Reproduction and Fertility, 114(1), 1998, pp. 169-177
In this study of brushtail possums, proteins present in epididymal flu
id and not present in blood plasma and those that become associated wi
th spermatozoa as they pass along the tract were investigated. At leas
t 19 proteins were present in epididymal fluid in the various regions
of the tract that were not detected in serum. Some of these may be pre
sent on the sperm plasmalemma. Six proteins were extracted from caput
spermatozoa (M-r 117 000, 103 000, 87 500, 85 000, 62 000 and 33 000)
that did not appear in the caudal sperm extracts. Eight proteins (M-r
50 000, 49 000, 32 000, 27 000, 26 500, 25 000, 24 500 and 18 000) wer
e localized to caudal sperm extracts. These findings suggest that some
sperm proteins are lost or modified, whereas others are added to the
sperm plasma membrane during epididymal transit. In vitro incorporatio
n of [S-35]methionine by the epididymal tissue showed that the distal
caput and corpus are the most active regions in the synthesis and secr
etion of proteins. Four caudal epididymal proteins (M-r 72 000, 31 000
, 26 500 and 21 000) were partially sequenced. Those of M-r 31 000 and
26 500 had the same N-terminal amino acid sequence suggesting post-tr
anslational modification of the same protein; they showed homology to
a retinoic acid-binding protein. The protein of M-r 72 000 was found t
o be homologous to a-fetoprotein, whereas the protein of M-r 21 000 sh
owed no significant homology to any protein in the database. These res
ults show that the lumen of the epididymis has many proteins that are
not present in the blood, some of which appear to become associated wi
th spermatozoa during epididymal transit.