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Abstract
Most of the proteins secreted in the epididymis are
produced by the proximal region, and several of them are
secreted in abundance. Many of these major proteins have
now been identified, including a new epididymis-specific
RNase A-like Train A protein, which has been recently
described in several mammals. This protein is expressed
and secreted exclusively in the initial part of the
epididymis. RNase A activity was analyzed in the fluids
from the testis and from different epididymal regions, but
in no case was this protein found to have RNase A
activity. The protein was present only in the luminal
fluid of the epididymal region which secreted it. Using an
in vitro/in vivo microperfusion technique and immunogold
electron microscopy labeling, we demonstrated that the
epithelium which secreted it specifically reabsorbed the
protein present in the lumen of the tubule. Thus, the
presence of Train A protein in the epididymal fluid was
the result of a steady state between secretion and
absorption. The transcription and translation of Train A
mRNA were simultaneous and actively regulated by
testicular factors. The function of this protein is
unknown but it does not seem to interact directly with
sperm. As for other members of the RNase family (e.g.
angiogenin), its biological activity might be expressed
after its cellular reabsorption. This new compound might
therefore participate in an unknown function in the
epithelial cells of this first part of the epididymis by
an autocrine pathway.
Key words:
Male Reproductive Tract
Epididymis
Sperm maturation
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