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Abstract
Small membranous vesicles, between 25 to 75 nm-diameter
were collected by high-speed centrifugation from the ram
cauda epididymal fluid and were found to be normal
constituents of this fluid and of the seminal plasma. The
SDS-PAGE protein pattern of these vesicles was specific
and very different from that of the caudal fluid, seminal
plasma, sperm extract and cytoplasmic droplets. After
two-dimensional electrophoresis separation and mass
spectrometry analysis, several proteins were identified
and grouped into: i) membrane-linked enzymes such as
dipeptidyl peptidase IV (DPP-IV), neprilysin (NEP),
phosphodiesterase-I (E-NPP3) and protein G-beta, ii)
vesicle-associated proteins such as lactadherin
(MFEG8-PAS6/7) and vacuolar ATPase, iii) several
cytoskeleton-associated proteins such as actin, ezrin and
annexin, and iv) metabolic enzymes. The presence of some
of these proteins as well as several different hydrophobic
proteins secreted by the epididymis was further confirmed
by immunoblotting. These markers showed that the majority
of the vesicles originated from the cauda epididymal
region. The physical and biochemical characteristics of
these vesicles suggest they are the equivalent to the
exosomes secreted by several cell types and epithelium.
The main membrane-linked proteins of the vesicles were not
retrieved in the extract from cauda or ejaculated sperm
suggesting that these vesicles did not fuse with sperm in
vivo.
Key words:
Gamete Biology •
Male Reproductive Tract •
Epididymis •
Sperm •
Sperm maturation
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