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PubMed1997

Toxocara canis (Nematoda:Ascaridae): the fine structure of the oviduct, oviduct-uterine junction and uterus.

The fine structure of the oviduct, oviduct-uterine junction and uterus of the nematode Toxocara canis (Werner, 1782) is described. Columnar-type epithelioid cells with numerous microvilli at the apical membrane border the oviduct lumen. Many electron dense secretory products are present in these cells. The cells lining the oviduct-uterine junction have no microvilli. They are coated with an electron-dense layer and contain numerous membrane-bound dense material containing bodies. Externally, the cells are surrounded by a basal lamina and muscle cells. The epithelial cells lining the greater part of the paired uteri appear to be rather flat. The oocytes inside the oviduct are covered with a dense thick plasma membrane and contain lipid droplets, dense granules and glycogen. The morphology of the oocytes before the fertilization inside the oviduct-uterine junction resembles that of the oocyte in the oviduct. After the fertilization the egg shell formation takes place. The egg shell of T.canis is composed of four layers: uterine, vitelline, middle chitinous and inner layer. The differences between the fine structure of the egg shell of T. canis and other related nematodes are discussed.

Animals↗
PubMed1993

Immunogold localization of porcine oviductal secretory proteins within the zona pellucida, perivitelline space, and plasma membrane of oviductal and uterine oocytes and early embryos.

The objectives of the present study were to develop an antibody probe to the porcine estrogen-dependent oviductal glycoproteins and to determine, by use of immunogold electron microscopy, whether these glycoproteins become associated with oviductal and uterine oocytes and early embryos. Polyclonal antibody, prepared using the M(r) 75,000-85,000 glycoprotein, separated from other proteins by two-dimensional SDS-PAGE, specifically recognized all three estrogen-dependent glycoproteins (acidic 75,000-85,000 M(r); acidic 100,000 M(r); basic 100,000 M(r)). In ampullary tissue collected from ovariectomized and estrogen-treated gilts and from gilts at Day 1 of estrus, gold particles were clustered over putative secretory granules restricted to the apical region of secretory epithelial cells. While follicular oocytes did not react with immunoreactive colloidal gold, oviductal and uterine unfertilized oocytes were found to be densely and uniformly labeled by colloidal gold throughout the zona pellucida, associated with flocculent material in the perivitelline space, and associated with microvilli and vitelline membrane. Similarly, in oviductal (1-4-cell) and unhatched uterine (4-cell/blastocyst) embryos, colloidal gold particles were distributed throughout the zona pellucida, heavily associated with flocculent material in the perivitelline space, and associated with the plasma membrane of the blastomeres. Immunoreactive colloidal gold remained detectable within Day 7 hatched uterine embryos, but not with embryos from later days. These results further support the proposal that porcine estrogen-dependent oviductal glycoproteins are released into the oviductal lumen, become associated with oviductal and uterine oocytes and early embryos, and are retained by oocytes and early embryos in the uterus.

Animals↗
PubMed2000

Effect of nitric oxide synthase inhibitors on ovum transport and oviductal smooth muscle activity in the rat oviduct.

The effect of the inhibition of nitric oxide synthase (NOS) on ovum transport and oviductal motility in rats was investigated. Three different NOS inhibitors were injected into the ovarian bursa at oestrus or day 3 of pregnancy. Oviducts and uteri were flushed 24 h later and the presence of ova was recorded. In oestrous and pregnant rats, treatment resulted in accelerated egg transport, as shown by a decrease in the number of ova present in the oviducts. In cyclic rats, intrabursal injection of 1 mg kg-1 of either N-monomethyl-L-arginine (L-NMMA) or N omega nitro-L-arginine methyl ester (L-NAME) elicited a 30% reduction in the number of ova present in the oviducts, whereas in pregnant animals, the same dose of L-NMMA produced a reduction of 40%. Simultaneous administration of the NO donor spermine NONOate (5 mg kg-1) completely reversed the effect of L-NMMA. Tubal motility was assessed by microsphere displacement analysis within the oviduct. Surrogate ova were transferred to the oviductal lumen at oestrus and 24 h later the effect of intraoviductal injection of 1 microgram L-NMMA or vehicle was assessed. The microspheres in the isthmus showed an oscillating motion, and periods in which movement was not detectable. However, L-NMMA treatment produced a 3.6-fold increase in the maximum instant velocities and a significant reduction in the resting periods of the microspheres compared with the control group (P < 0.001). These results provide evidence that NO inhibition increases tubal motility that results in accelerated ovum transport, and indicate that NO could act as a paracrine signal between different layers of the oviductal wall, providing a role for endogenous NO in regulation of tubal function.

Analysis of Variance↗
PubMed1984

The chick oviduct in tissue culture. I. Initial characterization of growing primary oviduct tissue cultures.

A simple three-enzyme treatment of collagenase, dispase and hyaluronidase on finely minced chick oviduct yields clumps of 50-150 cells. These cells attach to collagen-treated dishes and survive in culture for at least 2 weeks without subculturing. Oviduct cell cultures can also be induced to grow. Estradiol or epidermal growth factor (EGF) induce a 40% increase in cells in 4 days when cultures are grown in serum levels that do not support growth. Serum from estrogen-stimulated chicks promotes rapid cellular proliferation (doubling times of 1-2 days). Sera from estrogen withdrawn chicks, laying hen or horse do not support as rapid proliferation. The oviduct growth-promoting factors in serum from estrogen-stimulated chicks are not steroids or fibroblast growth factors (FGF). Removal of steroids from these sera by charcoal treatment or delipidization does not decrease the rate of growth. The addition of 1-100 nM estradiol does not increase a serum's ability to promote growth. Purified FGF or platelet-derived growth factor (PDGF) do not induce oviduct proliferation. These results were reproduced in oviduct cell cultures started from estrogen-stimulated and withdrawn chicks as well as laying hens. Thus the factors in serum from estrogen-stimulated chicks that promote rapid oviduct growth are induced by estrogen treatments in vivo, but do not seem to be only steroids.

Animals↗
PubMed1990

Oviductal epithelium of the baboon: hormonal control and the immuno-gold localization of oviduct-specific glycoproteins.

Oviducts were obtained from a series of cycling and ovariectomized steroid-treated baboons. The lining epithelium of the ampulla and isthmus was analyzed by light and electron microscopy. Both morphological and cytomorphometric analyses revealed that the morphological and functional state of the oviductal epithelium in the baboon is controlled by the ovarian steroids. Additionally, a clear cephalocaudal steroid-responsive gradient was observed when the data from the ampulla and isthmus of the same animal were compared. Within the ampulla, estradiol induced hypertrophy, hyperplasia, ciliogenesis, and secretory activity, whereas adding progesterone to the treatment regimen (+/- estradiol) resulted in atrophy, deciliation, apoptosis, and loss of the secretory activity. These cyclic processes were less evident in the isthmus. We also used an indirect electron microscopic immunogold technique and a previously characterized polyclonal antibody to determine the localization of oviduct-specific glycoproteins. These glycoproteins were present in every secretory granule observed, regardless of oviduct region, electron density, or size of the secretory granule. In summary, our data show that 1) estradiol induces and maintains the mature epithelium of the baboon oviduct, 2) steroid withdrawal or the administration of progesterone causes regression of the epithelium, and 3) the previously identified estradiol-dependent oviduct-specific glycoproteins are synthesized within and released from the secretory epithelial cells.

Animals↗
PubMed1995

Bovine oviductal epithelial cells (BOEC) and oviducts: I. For embryo culture. II. Using SEM for studying interactions with spermatozoa.

The oviduct (uterine tube) plays a major role in reproduction. It is a dynamic organ which selectively permits a few sperm to undergo capacitation and reach the oocyte which has continued to undergo maturation following ovulation. Then following fertilization the embryo undergoes cleavage before arriving in the uterus. Extensive information has become available from in vitro studies on oocytes as well as spermatozoal interactions with oviductal cells. Bovine oviduct epithelial cell (BOEC) monolayers with simple media provide an environment in which zygotes can be cultured to blastocysts in 6 days with cell numbers essentially equivalent to blastocysts grown totally in the donor animal. These yield normal pregnancy rates upon transfer. The simple protein-free media currently under test hold promise for elucidating specific requirements of the preimplantation embryo and these defined conditions facilitate many related studies on in vitro fertilization and genetic engineering of embryos. The second part of this paper is an extensive study on the interaction of fresh and frozen-thawed bull spermatozoa with BOEC and segments of intact oviducts as viewed by SEM. Both types of oviductal cells were incubated at 39 degrees C for 0, 3, 6, and 9 hours, using material obtained from periovulatory cows. Sperm attached immediately to both types of epithelium and reached a peak at 3 hours. They were found primarily in the furrows of the intact oviducts. Secretory droplets appeared rapidly on the anterior portion of the sperm head and acrosomal changes were evident in 3 hours, similar to those reported in vivo. Changes were more rapid with frozen-thawed sperm.

Animals↗
PubMed2004

Kinetics of protein tyrosine phosphorylation in sperm selected by binding to homologous and heterologous oviductal explants: how specific is the regulation by the oviduct?

Essential steps of the capacitation process take place in the oviductal isthmus. A crucial step in the process of capacitation is the phosphorylation of membrane proteins. The aims of this work were (1) to study the effect of dog sperm binding to oviductal epithelium on tyrosine phosphorylation and (2) to investigate the specificity of regulation of molecular changes by the oviduct of different species by comparing the numbers of canine sperm bound to heterologous (porcine) and homologous epithelium, and the kinetics of tyrosine phosphorylation. Semen was collected from four healthy dogs and washed through a Percoll gradient. Explants, small pieces of epithelium, were cut from porcine and estrous bitch oviducts. During 6 h of coincubation in Tyrode medium, the numbers of bound sperm were counted by microvideographic observation, and the state of tyrosine phosphorylation was determined immunocytochemically after 3, 30, 90, 180 and 360 min. Canine sperm bound in similar numbers to homologous and heterologous explants. Increasing tyrosine phosphorylation of tail proteins and subsequent phosphorylation of sperm head proteins were observed. Binding occurred mainly in sperm with non-phosphorylated heads (approximately 2% phosphorylated), while higher proportions of head-phosphorylated cells were found in unbound populations (approximately 40-60%;P<0.05). The head phosphorylation progressed significantly during incubation in unbound spermatozoa (P<0.05), while it was suppressed in bound suspensions. The rate of tyrosine phosphorylation of sperm tail proteins was higher in cells bound to explants than in unbound cells or in those incubated in control medium. There were no significant differences with respect to the kinetics of tyrosine phosphorylation between the two coincubation systems. These observations support the hypothesis that spermatozoa with non-phosphorylated heads preferentially attach to epithelial cells. Tyrosine phosphorylation of sperm head proteins and capacitation are delayed in spermatozoa in close contact with oviductal epithelium. This mechanism appears to be species-independent, as sperm bound similarly to pig and dog oviduct explants, and similar phosphorylation kinetics were observed in both types of tissue.

Animals↗
PubMed1999

Synthetic oviductal fluid and oviductal cell coculture for canine oocyte maturation in vitro.

The perfection of in vitro maturation in the bitch has yet to be achieved, and is an essential prerequisite for gamete salvage programmes in endangered canine species. In contrast to most mammals, the bitch ovulates an immature oocyte which undergoes meiotic maturation within the oviduct. A model of the oviductal environment may therefore be useful for performing in vitro maturation. This study was performed to investigate the effect of introducing an oviductal element to the culture environment, first with the use of a synthetic oviductal fluid (SOF), and secondly, using coculture with isolated canine oviductal epithelial cells, upon the rate of oocyte maturation in vitro. It was found that there was no difference in the proportion of oocytes undergoing germinal vesicle breakdown (GVBD) after 48 h in culture between SOF containing 0.3% bovine serum albumin (BSA, 45%), containing 4% BSA (36%) and control medium 199 (27%). There was also no difference in oocyte nuclear maturation to metaphase I/anaphase I/metaphase II (MI/AI/MII) after 48 h in culture between SOF containing 0.3% BSA (5%), containing 4% BSA (7%) and control medium 199 (6%). In addition, there was no difference in oocyte nuclear maturation to MI/AI/MII after 96 h between SOF containing 0.3% BSA (0), containing 4% BSA (7%) and control medium 199 (11%). In contrast, the proportion of oocytes undergoing GVBD after 96 h in culture was affected by the treatment used, with 27% in SOF + 0.3% BSA, 62% in SOF + 4% BSA and 63% in medium 199. It was found that there was no difference in the proportion of oocytes undergoing GVBD between the coculture treatments 199 (33%), 199 + cells (37%), coculture medium (30%) and coculture medium + cells (49%), and for oocyte nuclear maturation to MI/AI/MII, between medium 199 (2%), 199 + cells (0), coculture medium (6%) and coculture medium + cells (2%) after 48 h in culture. In addition, there was no difference in oocyte nuclear maturation to GVBD after 96 h between 199 (61%), 199 + cells (59%), coculture medium (65%) and coculture medium + cells (53%). In contrast, the proportion of oocytes maturing to MI/AI/MII after 96 h in culture was affected by the treatment used, with a significant difference between 199 (0), 199 + cells (9%), coculture medium (0) and coculture medium + cells (0). It was shown, therefore, that the culture of oocytes in the SOF improved oocyte nuclear maturation when supplemented with a high concentration of protein and that culture in the presence of oviductal epithelial cells improved oocyte maturation, but only after a prolonged period of time.

Animals↗
PubMed1996

Development of ovine embryos in synthetic oviductal fluid containing amino acids at oviductal fluid concentrations.

The effects of supplementing synthetic oviductal fluid (SOF) with amino acids, at oviductal fluid concentrations, on the development of ovine in vitro-matured/in vitro-fertilized embryos was examined in three experiments. In the first, embryo development in SOF, SOF + 2% human serum (HS), SOF + 20% HS, and SOF + BSA, with and without amino acid supplementation, was examined. Development of zygotes to the blastocyst and hatching blastocyst stages was highest in medium containing 20% HS (64.8% and 54.4%, respectively) irrespective of amino acid supplementation. However, supplementation was significantly beneficial in all other media, with up to 42.1% of zygotes developing into hatching blastocysts. In these media, supplementation also significantly increased the mean number of nuclei per newly formed blastocyst (up to a mean of 70.8) and reduced the time during which blastocysts formed. Experiment 2 was an examination of the effect on embryo development of three amino acid preparations (oviduct amino acid concentrations vs. Eagle's Basal Medium (BME) essential + Minimum Essential Medium (MEM) nonessential vs. MEM essential + MEM nonessential concentrations) and the presence or absence of BSA. Both the amino acid and BSA treatments significantly influenced the percentage of zygotes that developed to the hatching blastocyst stage but not to the blastocyst stage. The preferred medium contained amino acids at oviductal fluid concentrations and BSA (54.5% hatching rate). The amino acid treatments did not significantly influence the mean number of nuclei per newly formed blastocyst, but the addition of BSA had a significant effect (70.7 +/- 1.14 vs. 75.7 +/- 1.13). In experiment 3, embryo development to Day 13 was examined after culture in SOF containing amino acids at oviductal fluid concentrations. Embryos were cultured in the presence of either BSA, polyvinyl alcohol (PVA), or no additional supplement and were transferred to recipient ewes on either Day 0 (after in vitro fertilization), 3, or 5. The addition of BSA or PVA had no significant effect, but significantly more embryos developed to Day 13 following transfer on Day 0 (60.0%) than on either Day 3 or 5 (overall 45.4%). It is concluded that SOF containing oviductal fluid concentrations of amino acids 1) facilitates the development of a high percentage (57.5%) of blastocysts, 2) improves embryo morphology compared with that observed in medium containing HS, 3) significantly improves hatching rates compared with those obtained in SOF containing commercially available preparations of amino acids, and 4) produces embryos with relatively high levels of viability to Day 13 of pregnancy.

Amino Acids↗
PubMed1996

Immunocytochemical evidence that a specialised region of the rat oviduct secretes an oviductal glycoprotein.

The immunocytochemical localisation in the rat oviduct of an oviductal glycoprotein was investigated by light and electron microscopy. Using a monoclonal antibody (MAb) that cross-reacted with the rat oviductal glycoprotein ( > 330 kDa), we examined the epithelium of 4 regions (fimbriae, ampulla, isthmus and uterotubal junction) of the rat oviduct during the oestrous cycle. The MAb reacted specifically with the epithelial cells of the rat oviduct and not with the stromal cells. Intense labelling was observed in the isthmic epithelium throughout the oestrous cycle. Immunohistochemical staining was observed in the ampullary epithelium but the reaction was very weak. In the fimbriae and at the uterotubal junction, the immunoreaction was barely apparent in the epithelial cells. At the ultrastructural level, the MAb bound selectively to the putative secretory granules of nonciliated secretory cells in the isthmus, but no labelling was observed in most of the secretory granules in the ampullary segment. These results demonstrate that certain glycoproteins are secreted mainly by the isthmic secretory cells, suggesting regional specificity of the production of the glycoprotein in the rat oviduct.

Animals↗
PubMed1999

Involvement of gicerin, a cell adhesion molecule, in development and regeneration of oviduct and metastasis of oviductal adenocarcinomas of the chicken.

Gicerin is a novel cell adhesion molecule in the immunoglobulin superfamily and has both homophilic adhesion and heterophilic adhesive activity to neurite outgrowth factor (NOF), an extracellular matrix protein in the laminin family. We investigated the possible involvement of gicerin in oviductal development, regeneration, and metastasis of oviductal adenocarcinomas of the chicken. In the oviductal epithelium, gicerin was expressed strongly during development, disappeared after maturation, and reappeared during regeneration. NOF was constitutively expressed in the basement membrane of the epithelium. These molecules were expressed strongly in oviductal adenocarcinomas in both primary and metastatic lesions in the mesentery. An anti-gicerin antibody inhibited the attachment of adenocarcinoma cells to the mesentery in vitro. Many cells migrated from adenocarcinoma tissues on NOF, which were inhibited by an anti-gicerin antibody. These results suggest that gicerin might play a role in oviductal development and regeneration and also in the metastasis of adenocarcinomas.

Adenocarcinoma↗
PubMed1991

Immunocytochemical localization of an oviductal zona pellucida glycoprotein in the oviductal epithelium of the golden hamster.

The immunocytochemical localization of an oviductal glycoprotein associated with ovulated eggs was investigated. Using a monoclonal antibody, we studied three regions of epithelium in the golden hamster oviduct. The monoclonal antibody reacted with the oviductal epithelium throughout the fimbriae and isthmus. Intense binding was observed in the ampulla and isthmus, especially in the caudal isthmus. In addition, reactive materials were present in the ovarian bursal sac and lumen of the ampulla. At the ultrastructural level, the monoclonal antibody reacted specifically with putative secretory granules and Golgi apparatus of nonciliated cells in the oviductal epithelium. Other cellular organelles did not react. Quantitative data indicated that the immunolabelings were intense in the ampullar and isthmic cells but weak in the fimbrial cells. Lipid droplet-like granules of the fimbriae and lysosome-like vesicles of the isthmus did not react with the monoclonal antibody. In all cases, ciliated cells did not react with the monoclonal antibody. These results suggest that the glycoprotein is primarily produced and secreted by ampullar and isthmic secretory cells and is then accumulated in the ovarian bursal sac. These findings may provide insight into regional and cellular differences in secretion of the golden hamster oviduct.

Animals↗
PubMed1993

Immunocytochemical localization of oviduct-specific glycoproteins in the oviductal epithelium from cows at follicular and luteal phases.

The immunocytochemical localization of bovine oviduct-specific glycoproteins was investigated by light and electron microscopy. Using monoclonal antibodies (MAbs) specific for bovine oviductal glycoproteins, 3 regions (fimbriae, ampulla, and isthmus) of the epithelium in the bovine oviduct we studied during the follicular and luteal phases. The MAbs reacted specifically with the oviductal epithelial cells. Intense labeling was observed in the ampullar and fimbrial epithelia of cows at the follicular phase, but the reactions were weaker at the luteal phase. In the isthmus, the immunohistochemical reaction was faint during both follicular and luteal phases. At the ultrastructural level, the MAbs bound selectively to putative secretory granules of nonciliated cells in the ampulla and fimbriae, but not in the isthmus. These results suggest that there are cyclic changes and regional differences in the production of glycoproteins in the bovine oviduct.

Animals↗
PubMed1998

Effect of prostaglandin F2 alpha (PGF2 alpha) on oviductal nitric oxide synthase (NOS) activity: possible role of endogenous NO on PGF2 alpha-induced contractions in rat oviduct.

In this paper, we evaluated the hypothesis that prostaglandin F2 alpha (PGF2 alpha) regulates NOS activity and we also investigated, by means of nitric oxide inhibitors (N-monomethyl-L-arginine monoacetate, L-NMMA) the role of endogenous NO on PGF2 alpha-induced contractions in rat oviduct. NOS activity was determined by measuring the conversion of 14[C]-L-arginine to 14[C]-L-citrulline on oviductal homogenates from estrogenized rats (1 microgram/rat). The presence of PGF2 alpha (10(-8) M) in the incubation medium produced an increase in NOS activity (p < or = 0.05). The effect of the prostanoid was blocked completely by the presence of two NOS inhibitors: N-nitro-L-arginine methyl ester (L-NAME, 0.6 mM) and aminoguanidine (Ag, 0.5 mM). These results suggested that PGF2 alpha could be modulating the Ca(2+)-independent NOS activity. We determined NOS activity using 1 mM EGTA, a chelator of Ca2+, in a free Ca2+ medium. These results indicated that PGF2 alpha produces an increase in Ca(2+)-independent NOS activity (p < or = 0.05). PGF2 alpha induces contraction of the oviductal smooth muscle in a concentration dependent manner. L-NMMA enhanced PGF2 alpha induced contraction of the oviduct, providing indirect evidence that there is a basal release of NO in the oviduct, which may reduce and/or modulate the contractile effects of PGF2 alpha.

Animals↗
PubMed2003

Comparison of proteins synthesized by polarized caprine oviductal epithelial cells and oviductal explants in vitro.

Our objectives were to compare proteins secreted by caprine oviductal explants and oviductal epithelial (OE) cells in vitro. Oviducts were collected from goats on Days 1 (n=5) and 5 (n=5) of the estrous cycle. Radiolabeled secretory proteins from tissue segments and cell cultures were visualized using SDS-PAGE and fluorography. After culture, media from ampulla oviduct segments collected on Days 1 and 5 of the estrous cycle contained an acidic 97 kDa protein, which was greatly reduced in culture medium obtained from infundibulum and isthmus oviduct segments. A complex of low molecular weight proteins (14-26 kDa) could be modulated by estradiol when OE cells were cultured on plastic. This complex was constitutively expressed when OE cells were cultured on Matrigel-coated filters. Polarized OE cells were also capable of compartment-specific secretion of [L-(35)S]-methionine-labeled proteins. A 45 kDa acidic protein was predominantly secreted into the apical compartment while a 66 kDa acidic protein was preferentially localized in the basal compartment. Proteins secreted by OE cells were similar to proteins secreted by tissue segments in vitro. Therefore, under well-defined culture conditions OE cells may be useful in enhancing in vitro fertilization or early embryonic development.

Animals↗
PubMed2005

Effects of human oviductal in vitro secretion on spermatozoa and search of sperm-oviductal proteins interactions.

It has been suggested that oviductal proteins could be involved in modulating sperm function and fertilizing ability through as yet not well-known mechanisms. The objective of the study was to investigate the pattern of proteins secreted by human oviductal tissue cultures and the effects of their conditioned media (CM) on sperm function under capacitating conditions and in phosphate buffered saline (PBS). In addition, interactions between spermatozoa and oviductal proteins were examined. The oviductal tissue was obtained from pre-menopausal patients scheduled for hysterectomies because of uterine fibromyoma. Normozoospermic semen samples were obtained from healthy donors. Cultures of human fallopian tissue were carried out and CM were collected for analysis of the de novo production of [35S]-methionine-labelled proteins by SDS-PAGE. Motile spermatozoa were incubated under capacitating conditions and in PBS, with or without CM, and sperm fertilizing ability was assessed by ionophore-induced acrosome reaction (AR) and the acrosome reaction to ionophore challenge (ARIC) score. The ionophore-induced AR was evaluated by the Pisum sativum technique. Sixteen de novo produced proteins were detected in CM. One of these proteins (molecular weight 79 kDa) was detected in extracts from spermatozoa pre-incubated with CM. Sperm survival and motility were maintained in the presence of CM, although results showed a significant decrease in ARIC score (p < 0.05), with respect to controls. The presence of CM significantly decreased sperm fertilizing ability, without affecting sperm survival. These results suggest that the oviductal secretion could contribute to preserve sperm viability and motility, and to prevent a premature response of spermatozoa to AR inducers.

Cell Survival↗
PubMedDate not supplied

Investigation of ovum transport in the oviduct: the dynamics of oviductal fluids in domestic rabbits.

Ova are captured by the oviductal fimbria and rapidly transported to the ampullary-isthmic junction of the fallopian tube. Fertilized ova and oviductal fluids are then carried medially in the fallopian tube, while undergoing maturation in preparation for entering the uterine cavity, where nidation and further development take place. This movement of oviductal fluids was visualized in a rabbit model with human chorionic gonadotropin-induced ovulation, by injection of a contrast medium into the ampulla region of the oviduct. In the ampulla, the opaque medium was observed to oscillate at 0-85.4 mm/s. This medial transport of the fluid towards the uterus decreased to 0-9.6 mm/s in the isthmic portion of the tube. This decrease substantiates previous findings that the transport of material in the isthmic portion of the oviduct is more strongly under the control of ciliary action than under peristaltic activity.

Animals↗
PubMed1988

FOSP-1 (frog oviduct-specific protein-1) gene: cloning of cDNA and induction by estrogen in primary cultures of Xenopus oviduct cells.

We describe the isolation of a cloned cDNA from a cDNA library of oviduct of estrogen-treated adult Xenopus. Although the protein encoded by this cDNA is not known, it is designated as FOSP-1 (frog oviduct-specific protein-1). A partial restriction map of FOSP-1 cDNA, which is 1.5 kb in size, is presented. Northern hybridization analysis showed that FOSP-1 cDNA codes for a single species of mRNA of 2.6 kb which is exclusively expressed in Xenopus oviduct. Southern blot analysis showed that the gene was present in only one or two copies. Sequencing of partial FOSP-1 cDNA did not reveal homology with any protein in the sequence data bank. Measurement of steady-state levels of FOSP-1 mRNA in primary cultures of Xenopus oviduct cells by a technique of quantitative slot-blot analysis showed that both 17 beta and 17 alpha stereoisomers of estradiol caused a rapid 5-fold enhancement of accumulation of the mRNA with maximum values obtained at 5 X 10(-8) M estrogen. Progesterone caused only a small increase in FOSP-1 mRNA concentration. This hormone-specific induction of mRNA makes FOSP-1 a valuable candidate for exploring tissue specificity of regulation by estrogen of gene expression.

Amino Acid Sequence↗