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Abstract
A widely conserved sperm antigen, the Sperm Adhesion
Molecule 1 (SPAM1 or PH-20) is a glycosylphosphatidyl
inositol- (GPI)-linked protein with multiple roles in
mammalian fertilization. It has been shown to be
dually-expressed in testis and epididymis and this is
conserved in the four species (mouse, rat, macaques,
humans) that have been studied to date. Here we report
Spam1 RNA and protein expression in the murine vas
deferens and efferent ducts. In situ hybridization and
immunohistochemistry indicate that transcript and protein
are distributed in the non-ciliated epithelial cells, and
that the efferent ducts have the most intense staining of
all three regions of the excurrent ducts. Spam1
products
were also present in the accessory organs, the prostate
and seminal vesicles and its fluid. Using hyaluronic acid
substrate gel electrophoresis, hyaluronidase activity at
pH 7.0 was detected in the vas deferens; but was absent
from the efferent ducts, the prostate, and the seminal
vesicles/fluid. This suggests that Spam1 may play a
non-enzymatic role in these organs. The expression of
Spam1 without hyaluronidase activity in the efferent ducts
parallels that in the proximal tubules in the kidneys
where it is proposed to play a role in concentration of
the urine. The parallelism in embryological origin,
ultrastructure and physiology of the proximal tubules and
the efferent ducts allow us to propose that in the latter
Spam1 may play a role in sperm fluid concentration.
Key words:
Male Reproductive Tract
Epididymis
Prostate
Sperm
Vas deferens
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