Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UNIPROT:P56851 (
epididymal
)
11,273
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Oviductins are high-molecular-weight glycoproteins synthesized and secreted by nonciliated oviductal epithelial cells and have been shown to play a role in fertilization and early embryo development. The present study was carried out to examine the in vitro binding capacity of hamster
oviductin
to homologous sperm and to determine the sites of its localization in untreated, capacitated, and acrosome-reacted spermatozoa. Freshly prepared
epididymal
and capacitated sperm as well as acrosome-reacted sperm were incubated with oviductal fluid prepared from isolated hamster oviducts, fixed and then probed with a monoclonal antibody against hamster
oviductin
. Results obtained with pre-embedding immunolabeling experiments revealed binding of
oviductin
to the acrosomal cap and the apical aspect of the postacrosomal region. Immunolabeling of both regions appeared to be more intense in capacitated spermatozoa. Acrosome-reacted sperm showed an immunoreaction of moderate intensity over the postacrosomal region. The plasma membrane overlying the equatorial segment also exhibited a weak labeling. Quantitative analysis obtained with the surface replica technique indicated that
oviductin
had a higher binding affinity for the acrosomal cap than the postacrosomal region and that the binding of
oviductin
to the latter plasma membrane domain was enhanced during capacitation. Binding of
oviductin
to the postacrosomal region, however, was attenuated after acrosome reaction. Immunolabeling for
oviductin
was found to be the weakest over the equatorial segment regardless of the experimental conditions. The binding of hamster
oviductin
to specific membrane domains of the homologous sperm and the changes in its distribution during capacitation and acrosome reaction may be important for the function of hamster
oviductin
preceding and during fertilization.
...
PMID:Surface mapping of binding of oviductin to the plasma membrane of golden hamster spermatozoa during in vitro capacitation and acrosome reaction. 1649 83
Oviductal glycoprotein 1 (OVGP1), also called
oviductin
, is an oviduct-specific protein and is suggested to play a role in fertilization. Traditionally, Ovgp1 has been shown to be exclusively expressed by the oviduct; however, recent studies have demonstrated its expression in some cancers. This observation led us to hypothesize that Ovgp1 might have some extra-oviductal expression. In the current study, we evaluated the mRNA and protein expression of Ovgp1 in normal reproductive tissues of male and female mice. For the first time, we demonstrate that beyond the oviduct, Ovgp1 mRNA is expressed in the testis, epididymis and ovary, but not in the uterus, cervix, vagina, breast, seminal vesicles and prostate gland. In the testis, Ovgp1 mRNA was localized in the cells at the base of seminiferous tubules (most likely, Sertoli cells), while the protein was detected in the round and elongating spermatids. In the epididymis, Ovgp1 transcripts were localized in
epididymal
epithelium of the caput but not the corpus and cauda; OVGP1 protein was, however, not detected in any of the segments but was present in the
epididymal
sperm. In the ovary, Ovgp1 transcripts and protein were detected in the surface epithelium, granulosa cells of the preantral and the antral follicles and corpus luteum. In both, the ovary and oviduct, the expression of Ovgp1 was found to be higher at estrus stage than at diestrus stage. To the best of our knowledge, this is the first study demonstrating the extra-oviductal expression of Ovgp1. Our data suggests that, beyond fertilization, Ovgp1 might have specific roles in gonadal physiology. [Laheri S, Modi D and Bhatt P 2017 Extra-oviductal expression of oviductal.
...
PMID:Extra-oviductal expression of oviductal glycoprotein 1 in mouse: Detection in testis, epididymis and ovary. 2822 66