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Results for “OVIDUCTS”

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At least 73 records · Page 4Linked to original sources
PubMed2006

Human oviductal stromal fibroblasts, but not oviductal epithelial cells, express Toll-like receptor 4: the site-specific mucosal immunity of the human fallopian tube against bacterial infection.

PROBLEM: To evaluate the site-specific immunoregulatory mechanisms against bacterial infection in the human fallopian tubes. METHOD OF STUDY: We investigated the effects of lipopolysaccharide (LPS) on the production of CXC chemokines by cultured oviductal epithelial cells (OEC) and oviductal stromal fibroblasts (OSF). The expression of Toll-like receptor (TLR) 4 and CD14 protein in OEC and OSF were evaluated. The phosphorylation of the inhibitor kappaB-alpha (IkappaB-alpha) protein after LPS stimulation was also examined. RESULTS: Lipopolysaccharide stimulated the secretion of granulocyte chemotactic protein-2, growth-regulated oncogene-alpha, and epithelial neutrophil activating peptide-78 by OSF, but not by OEC. The phosphorylation of the IkappaB-alpha protein was not detected in OEC after stimulation by LPS, whereas IkappaB-alpha phosphorylation was observed in OSF after stimulation by LPS. The expression of the TLR4 protein and mRNA was detected only in OSF but not in OEC. The expression of CD14 was not detected in either OEC or OSF. CONCLUSION: These results suggest that epithelial cells and fibroblasts in the human fallopian tube have evolved a unique, site-specific mechanism for recognizing Gram-negative pathogens. The lack of TLR4 in OEC may be important for avoiding a state of unnecessary inflammation that could disrupt the epithelial barrier and cause irreversible tubal scarring.

Cells, Cultured↗
PubMed1995

Comparison of the effects of oviductal cell co-culture and oviductal cell-conditioned medium on the development and metabolic activity of cattle embryos.

The objective of this study was to compare the development and metabolic activity of cattle embryos co-cultured with bovine oviductal cells or cultured in serum-free medium previously conditioned by bovine oviductal cells. Zygotes were produced by in vitro fertilization of oocytes from bovine ovaries obtained from an abattoir. Development to the four-cell stage occurred by 48 h after fertilization in both culture systems, but co-cultured embryos reached the 16-cell stage by 96 h, whereas those cultured in conditioned medium did not do so until 24 h later. Similarly, the morula and blastocyst stages were reached 24 h earlier in co-culture than in conditioned medium. There were significantly more cells in the blastocysts from co-culture (96.8 +/- 6.1 versus 56.7 +/- 3.3; P < or = 0.0001). The metabolism of glutamine did not differ between embryos cultured in the two systems, but the metabolism of glucose was significantly greater in embryos cultured in conditioned medium. The first significant increase in glucose metabolism occurred between the four-cell and the 16-cell stages in embryos cultured in conditioned medium, but occurred between the 16-cell and morula stages in the co-cultured embryos, such that the glucose metabolism was significantly greater at the 16-cell stage in embryos cultured in conditioned medium compared with co-cultured embryos (6.5 +/- 1.0 versus 1.5 +/- 0.4 pmol per embryo per 3 h, P < or = 0.0001). The concentration of glucose was significantly less, and that of lactate significantly greater, in co-culture medium than in conditioned medium.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed2004

Fertilization, embryonic development and oviductal environment: role of estrogen induced oviductal glycoprotein.

Mammalian oviduct is the physiological site for sperm capacitation, gamete fertilization and early embryonic development. The secretory cells lining the lumen of the mammalian oviduct synthesize and secrete high molecular weight glycoprotein (OGP) in response to estrogen. The protein has been shown to interact with gametes and early embryo. Several key functions have been postulated particularly its role in pre-implantation events which would have far reaching implications in assisted reproductive technology and in the development of non-hormonal contraceptive vaccine. The intention of this article is to discuss the current status of the protein and analyze how far the postulated function of OGP has been borne out by the available data.

Animals↗
PubMed1977

Progesterone-binding components of chick oviduct. Receptor B subunit protein purified to apparent homogeneity from laying hen oviducts.

The progesterone receptor B subunit has been purified to apparent homogeneity from hen oviduct cytosol using ammonium sulfate precipitation and chromatography on DEAE-cellulose, phosphocellulose, hydroxylapatite, and gel filtration on Agarose A-1.5m. The material is obtained (1 mug of purified protein/g of tissue) in about 17% yield. The protein is highly purified; a single band is seen on gel electrophoresis in acid-urea and sodium dodecyl sulfate gels as well as gel electrophoresis under nondenaturing conditions. In the latter system, labeled progesterone co-migrates with the protein band, demonstrating that the isolated protein is a progesterone-binding species. Labeled progesterone bound to the protein is displaced by progestational steroids but not by estradiol or hydrocortisone. The protein has a molecular weight of 116,000 g/mol as determined by gel electrophoresis and has a single polypeptide chain. The isolated protein contains 98% endogenous nonradioactive progesterone and is 2% labeled by incubation in vitro with radiolabeled progesterone. It behaves identically on all of the chromatographic steps to chick receptor B subunits described in earlier publications.

Animals↗
PubMed1977

Progesterone-binding components of chick oviduct. Biochemical characterization of purified oviduct progesterone receptor B subunit.

A number of physical and chemical properties of pure hen oviduct progesterone receptor B subunit have been determined. The molecule consists of a single polypeptide chain with a molecular weight of 115,000 g/mol as determined by gel filtration in the presence of 6 M guanidine hydrochloride and by gel electrophoresis in sodium dodecyl sulfate. The labeled subunit has retained the biologically important properties which it displayed in cruder preparations: it binds to nuclei (Kd = 1 X 10(-9) M) and chromatin (Kd = 1.5 X 10(-9) M) but does not bind to DNA. Reaction of the purified subunit with dansyl (5-dimethylaminonaphthalene-1-sulfonyl) chloride revealed a single NH2-terminal lysine. The amino acid composition has been determined and has been shown to be distinct from that of other steroid-binding proteins and consistent with the known properties of the molecule. In addition, no evidence for carbohydrate or phosphorylated amino acids was observed. The protein contains about 12% alpha helix as determined by circular dichroism. The ultraviolet spectrum of intact steroid receptor complexes revealed that the purified subunit had no pyridine nucleotide cofactor or nucleic acid, and that each receptor molecule contains a single hormone binding site. Electron microscopic analysis confirms the prolate-ellipsoid shape of the protein, with a long axis of 114 A. The purified protein isolated as described in a companion paper is shown here to have the characteristics of the crude receptor subunit B. Due to the apparent role in the hormone response, this protein has been named progestophilin B.

Amino Acids↗
PubMed1996

Local regulation of oviductal blood flow.

1. Blood flow to the oviduct is implicated in the genesis and maintenance of oviductal fluid, in this way contributing to the creation of an adequate medium for ovum/embryo physiology. Therefore, factors controlling the tone of the vessels supplying the oviduct would be expected to affect its luminal environment. In addition, cyclic changes in oviductal blood flow have been suggested to have mechanical functions in the transport of the ovum/embryo. 2. The vascular supply to the oviduct has a prominent adrenergic vasomotor control. A dense adrenergic innervation, together with the presence of a predominant population of alpha(1)-adrenoceptors, provides a contractile regulatory mechanism of oviductal blood flow. No evidence is available on the presence of beta-adrenoceptors. The scanty cholinergic innervation of mammalian oviduct is mainly confined to the vessels, where acetylcholine (ACh) has a vasodilatory effect by releasing endothelium-derived relaxing factors. 3. The presence of nerves containing neuropeptides has been shown in the oviduct. Specifically, a high density of neuropeptide Y- and vasointestinal peptide-containing nerve fibers has been found in relation to blood vessels, but their role in the neutral control of the oviduct blood flow remains to be established. To date, it is not known whether or not oviductal blood vessels receive perivascular nitrergic nerves. 4. Relaxing and contracting factors derived from endothelium also seem to have a modulatory role on oviductal vascular tone. Neurotransmitters or autacoids, such as ACh and histamine, acting on endothelial receptors, release nitric oxide (NO), which relaxes oviductal arteries through guanylyl cyclase activation and accumulation of cyclic GMP. In addition, the release of an endothelium-derived hyperpolarizing factor (EDHF), distinct from NO, by ACh has been shown in oviductal arteries. It acts through the opening of low-conductance Ca(2+)-activated K+ channels leading to hyperpolarization and relaxation. Furthermore, potent and long-lasting contractions induced by the endothelium-derived contractile factor, endothelin (ET), points to its role in the long-term regulation of oviductal vascular tone. 5. A particularly high density of 5-hydroxytryptamine (5-HT) and histamine, present in mast cells clustered in the vicinity of blood vessels, has been described in the oviduct. It is known that histamine elicits a relaxation of oviductal arteries that is partially endothelium-dependent and mediated by the activation of H1-receptors. The implication of histamine in both the increase in blood flow and edema around ovulation, as well as the existence of a functional antagonism between histamine and 5-HT in the regulation of oviductal blood flow, await further investigation. 6. Other factors, such as relaxing and contracting cyclooxygenase-derived products, may also participate in the modulation of blood flow to the oviduct. 7. An overall endocrine regulation of the oviductal vascular supply exists, acting by both direct effects on smooth muscle and modulation of neural and autocrine factors. This control enables cyclic changes in blood flow to the oviduct that are tightly coupled to the reproductive functions of the tube.

Adrenergic Fibers↗