Prostaglandin F in the fallopian tube secretion of the ewe

Oviducal secretions were obtained from conscious unrestrained ewes throughout the oestrous cycle via indwelling cannulae and the content of prostaglandin F (PGF) was determined by radioimmunoassay. Levels of PGF of up to 230 ng/ml were found in oviducal fluids obtained from ewes showing regular patterns of secretion and normal cyclical ovarian function as indicated by plasma progesterone measurement. Relatively large day to day fluctuations in content were evident, but there was no consistent relationship between concentration and stage of the oestrous cycle. Concentrations of PGF in excess of 100 ng/ml were common in preparations where autopsy later revealed infection or tissue irritation, and the concentration of PGF invariably exceeded 75 ng/ml when the concentration of protein in the oviducal fluid was abnormally high.     

New assay for steroid sulfatase (EC 3.1.6.2) and its application for studies of human placental and skin sulfatase

A new, simple, fast and highly practicable sulfatase assay and its application is described. Sterol sulfatase sulfohydrolase (EC 3.1.6.2) activity is determined by a two-phase scintillation technique separating the unreacted [4-14C]dehydroepiandrosterone sulfate from carbon-14-labeled products. The principle of the separation relies on the limited emulsifying capacity of the dioxane-based scintillation solution for water and the different partition of dehydroepiandrosterone sulfate and sulfate-free steroid products between the scintillation fluid and the aqueous phase as recently applied for determination of aromatase activity [1]. [7-3H]Dehydroepiandrosterone sulfate can also be used as a substrate for this assay. This test was applied to studies of microsomal sulfatase prepared from human term placenta and to the detection of sulfatase activity in human skin biopsies. Using placental microsomes, the Km of dehydroepiandrosterone sulfate was determined to be 5.0 X 10(7)M. Sulfatase activity in frozen scrotal skin was found to be 2-3 fold than with vaginal skin. Using an incubation time of 24h/skin sulfatase can be detected in biopsies as small as 2.5 mm2. The sulfatase assay can be applied for routine detection of human placental sulfatase deficiency and, furthermore, the application of this assay has to be demonstrated for the analysis of sulfatase activity in patients with congenital ichthyosis (X-chromosomal, recessive type).     

Identification of an oestrus-associated glycoprotein in oviducal fluid of the sheep

Samples of oviducal fluid were collected daily from sheep with indwelling catheters. Fluid samples taken from both oviducts of 2 sheep for 2 cycles during the middle of the breeding season (April/May) (8 sets of data) were compared with 9 sets of data generated from 2 cycles in 3 sheep later in the breeding season (June/July). Around the period of oestrus, the output of oviducal fluid increased to a peak volume of 1.56 +/- 0.35 ml per day (mean +/- s.d.) compared with a mid-cycle volume of 0.49 +/- 0.29 ml. Later in the breeding season, the flow rates were lower, but showed the same trend (0.91 +/- 0.24 ml at the peak and 0.25 +/- 0.18 ml 7 days later). The total amount of protein secreted by the oviduct each day increased 2-4-fold around the time of oestrus, with higher levels in mid-season ewes. When oviducal fluids were fractionated by SDS electrophoresis, a novel glycoprotein, subunit size of Mr 80-90 000 was identified in samples for 3-6 days of each cycle, coinciding with the period of high fluid flow rate. This protein first appeared in the oviducal fluid on the day of oestrus or the following day and it represented 1 of the 2 major glycoproteins in oviducal fluid as assessed by periodic acid-Schiff (PAS) staining. A PAS-positive protein (Mr 80-90 000) was also detected in fluid taken after oestrus on native highly cross-linked gradient gels after electrophoresis at pH 3.1 but not at pH 8.3. Both gradient gel systems showed an increase in high molecular weight material (Mr greater than 10(6] in fluid taken soon after oestrus.     

Oestrogen and seasonal effects on the production of an oestrus-associated glycoprotein in oviducal fluid of sheep

In 14 cyclic ewes, the oestrus-associated glycoprotein in the oviducal fluid was never detected between Days 7 and -2 of the oestrous cycle and it was present in 5% of fluid samples collected on Day -1, 59% on Day 0, 96% on Day 1, 100% on Day 2, 79% on Day 3, 31% on Day 4, 16% on Day 5, and 4% on Day 6. Its presence generally coincided with the period of high flow rate of oviducal fluid which occurs around oestrus. The duration of detectable levels of the oestrus-associated glycoprotein did not vary significantly during the breeding season from a mean (+/- s.d.) of 3.9 +/- 1.0 days. However, the peak flow rate of oviducal fluid dropped from 1.63 +/- 0.50 (early) to 1.38 +/- 0.40 (mid-) and to 0.85 +/- 0.21 ml/day late in the season. Anoestrous ewes (3) induced to ovulate by treatment with progesterone implants and gonadotrophin showed low peak fluid flow rates (0.92 +/- 0.30 ml/day) and the presence of the oestrus-associated glycoprotein for a shorter period (2.7 +/- 0.7 days). Pregnancy (N = 3) did not appear to prolong the production of the protein. The injection of 25 micrograms oestradiol benzoate into 3 anoestrous, 2 mid-cycle and 9 ovariectomized ewes caused an increase in fluid flow rate and appearance of the glycoprotein 1-2 days later. The glycoprotein was present for a longer period in response to the exogenous oestrogen--6.8 +/- 1.6 days in the ovariectomized ewes, 7.9 +/- 1.3 days in anoestrous ewes, and 8.4 +/- 0.8 days in the dioestrous ewes.(ABSTRACT TRUNCATED AT 250 WORDS)     

Sterol sulfates in the epididymis; synthesis and possible function in the reproductive process

Sterol sulfates are present in relatively high concentrations in the male reproductive tract. Cholesteryl sulfate is the major sterol sulfate in the human epididymis while desmosteryl sulfate is the major sterol sulfate in the hamster epididymis. While the testis is the major source of sterol sulfate in the human, the epididymis of the hamster is the source of demosteryl sulfate. This conjugate accumulates along the length of the epididymis and is taken up by the plasma membrane in the acrosomal region of the spermatozoa. Sulfotransferase activity increases along the epididymis and this is due to the actual synthesis of the enzyme. Sterol sulfates are potent and specific inhibitors of the proteolytic enzyme, acrosin. This property could provide protection against the premature release of proteolytic activity within the male reproductive tract. It is proposed that the removal of this inhibition occurs within the female tract via sulfatase activity in order to enable the acrosome reaction and ovum penetration to occur.     

Preliminary observations on the collection of baboon oviducal fluid

Five sexually mature and regularly ovulating baboons (Papio cyanocephalus) were subjected to bilateral oviducal cannulation. Prior to failure of the primary cannulation, peri-ovulatory fluids were collected during three menstrual cycles from one animal, during two cycles from a second animal, and during a single cycle from each of two additional animals. These four animals were subsequently recannulated and oviducal fluids obtained during six additional cycles, but tubal fluid collection after the second procedure was generally less satisfactory than following the initial manipulation. Two attempted cannulations in the fifth animal did not result in oviducal fluid collection. Of the 13 menstrual cycles during which tubal fluid was collected, four were apparently anovulatory. Collections from two of these as well as from three ovulatory cycles were characterized by erratic flow and mucous-blood contamination. Tubal fluids were collected without apparent technical interference or serum contamination from six ovulatory and two anovulatory cycles. Maximum volumes (1.77±.34 ml/oviduct/24 hours) of tubal fluids were collected during the 48 hours following the midcycle LH peak. Thereafter, the rate of oviducal fluid collection declined rapidly.     

Regulation of the estrous cycle in ewes with progestin containing implants: Influence of dose and day of cycle at treatment

Implants containing Norgestomet (G. D. Searle and Co., Chicago) were inserted subcutaneously in ewes on selected days of the estrous cycle. When ewes were treated for 13 days with 2 or 3 mg Norgestomet, implantation 13 days post-estrus reduced the number of ewes in estrus within 5 days of implant removal and reduced the number of estrous ewes that lambed compared with ewes implanted 4 days post-estrus. When ewes were implanted with 3 or 6 mg Norgestomet 4 or 13 days post-estrus, no difference in estrus response was found. Conception rate was not influenced by day of treatment, but was higher in those ewes treated with 6 mg than ewes treated with 3 mg. Compared to no treatment, treatment with 3 or 6 mg Norgestomet reduced the number of uterine and oviducal sperm recovered 12 or 24 hr after insemination from ewes implanted for 12 days 2 or 12 days post-estrus. However, more sperm were recovered from ewes treated 2 days than 12 days post-estrus with the principal increase occurring in ewes treated with 6 mg of Norgestomet.     

alpha-Glucosidase activity in the reproductive tract of the ewe.

alpha-Glucosidase activity has been estimated in the tissues and rinsings of the reproductive tract of the ewe. There were peaks of activity in the oviducal mucosa at pH 4.0 and 5.7. In the endometrium, caruncles and cervical mucosa and pH optimum occurred from pH 4.0 to pH 5.7. A sharp peak in the activity in the vaginal mucosa occurred at pH 5.7. The only tissue in which changes in enzyme activity were consistently related to one endocrinological state of the ewe was the cervical mucosa. Cervical alpha-glucosidase activity was greater at oestrus than during the rest of the oestrous cycle, declined during early pregnancy, and increased in ovariectomized ewes following the injection of oestradiol-17 beta.     

Neural inhibition of egg-laying in the locust, Locusta migratoria

The role of the oviducal nerves during egg-laying in Locusta migratoria has been examined. Section of the oviducal nerves did not inhibit egg-laying in any observable way. Electrical stimulation of the oviducal nerves resulted in a contraction of the common and lower lateral oviducts which propelled ovulated eggs up towards the ovaries. Recordings from oviducal nerves using chronically implanted electrodes showed that electrical activity was low during actual egg-laying, but high at times when egg-laying was not occurring (i.e. during digging behaviour, or following interruption of egg-laying). During these periods of high activity recurrent bursts of action potentials occurred. Similar patterns of electrical activity were recorded in semi-intact preparations using suction electrodes applied to exposed oviducal nerves of locusts which had been interrupted during the process of egg-laying. High frequency bursts of activity were recorded simultaneously from both left and right oviducal nerves.It is concluded that one function of the oviducal nerves is to inhibit egg-laying at inappropriate times, by inducing contractions of the oviducts which propel eggs back towards the ovaries. These nerves therefore provide a physiological basis for part of the adaptive ovipositional activities of locusts.     

Uterine estrogen sulfatase activity at the time of blastocyst implantation in the rat

The conversion of estrone sulfate (E1S) to estrone (E1) was measured during the in vitro incubation of the labeled sulfoconjugate with implantation sites (IS) and nonimplanted regions (NIS) of uterine horns from 6-day pregnant rats. Extensive metabolism of E1S occurred in both tissues, being noticeably less (29.31%) in IS than in NIS. Estrogen sulfatase activity present in the uterus of ovariectomized virgin rats was found to be higher than in both uterine regions of the pregnant rats. We suggest that E1S present in uterine fluids may be accessible to be metabolized into unconjugated estrogens by both intrauterine tissues of 6-day pregnant rats. This metabolism could be locally modulated in IS through the participation of the estrogen sulfatase, the activity of which is in turn controlled by the presence of free estrogens, possibly synthesized and/or secreted by the embryo, which has been shown to inhibit the sulfohydrolase activity.     

Lack of effect of insulin or insulin-like growth factor I on the steroid sulfatase activity of human placental cytotrophoblasts

Hyperinsulinemia is known to reduce serum dehydroepiandrosterone sulfate (DHEA-S) levels in normal females. A possible mechanism for this phenomenon would be an insulin-mediated increase in steroid sulfatase activity, with insulin acting either via activation of the insulin receptor or via cross-reaction with the insulin-like growth factor I (IGF-I) receptor. Using a well characterized human cytotrophoblast system, the presence of steroid sulfatase activity in isolated cytotrophoblasts was documented. Half maximal cellular hydrolysis of DHEA-S was observed at a substrate concentration of 9.6-14.5 microM, and maximal hydrolysis at a concentration of 75-100 microM. The hypothesis that insulin increases steroid sulfatase activity was examined by exposing cytotrophoblasts to supraphysiological concentrations of either insulin (2 micrograms/ml) or IGF-I (20 ng/ml) for 24 h and then measuring the rate of DHEA-S hydrolysis. Insulin failed to affect cytotrophoblastic steroid sulfatase activity, irrespective of whether the substrate concentration was 20 microM or 100 microM. IGF-I also exerted no effect on steroid sulfatase activity. These data indicate that neither insulin nor IGF-I affect the steroid sulfatase activity of human cytotrophoblasts. An effect of insulin or IGF-I on the steroid-sulfatase activity of other tissues has not been excluded. These observations suggest that the decline in serum DHEA-S levels during hyperinsulinemia is not mediated via an insulin-induced increase in steroid sulfatase activity.     

Retinoid-mediated stimulation of steroid sulfatase activity in myeloid leukemic cell lines requires RARalpha and RXR and involves the phosphoinositide 3-kinase and ERK-MAP kinase pathways

All-trans retinoic acid and 9-cis-retinoic acid stimulate the activity of steroid sulfatase in HL60 acute myeloid leukemia cells in a concentration- and time-dependent manner. Neither of these 'natural retinoids' augmented steroid sulfatase activity in a HL60 sub-line that expresses a dominant-negative retinoic acid receptor alpha (RARalpha). Experiments with synthetic RAR and RXR agonists and antagonists suggest that RARalpha/RXR heterodimers play a role in the retinoid-stimulated increase in steroid sulfatase activity. The retinoid-driven increase in steroid sulfatase activity was attenuated by inhibition of phospholipase D (PLD), but not by inhibitors of phospholipase C. Experiments with inhibitors of protein kinase C (PKC) show that PKCalpha and PKCdelta play an important role in modulating the retinoid-stimulation of steroid sulfatase activity in HL60 cells. Furthermore, we show that pharmacological inhibition of the RAF-1 and ERK MAP kinases blocked the retinoid-stimulated increase in steroid sulfatase activity in HL60 cells and, by contrast, inhibition of the p38-MAP kinase or JNK-MAP kinase had no effect. Pharmacological inhibitors of the phosphatidylinositol 3-kinase, Akt, and PDK-1 also abrogated the retinoid-stimulated increase in steroid sulfatase activity in HL60 cells. These results show that crosstalk between the retinoid-stimulated genomic and non-genomic pathways is necessary to increase steroid sulfatase activity in HL60 cells.     

Estrone sulfatase activity in rat brain and pituitary: effects of gonadectomy and the estrous cycle

Estrone sulfatase activity was characterized in microsomal preparations from rat brain and anterior pituitary. No differences in apparent Km were found in hypothalamic-preoptic area between male (7.5 microM) and female (7.4 microM) rats. Apparent Km's of anterior pituitaries from males (14.5 microM) and females (22.5 microM) were higher than those found in brain. Estrone sulfatase activity was equally inhibited by estradiol-17 beta-3-sulfate, dehydroepiandrosterone-3-sulfate and estrone-3-sulfate indicating a broad range of substrate specificity for this enzyme. Sulfatase activity in female anterior pituitary was found to be twice that of male. Sulfatase activity was distributed similarly in brain tissues between sexes with cerebellum greater than or equal to medial basal hypothalamus greater than preoptic area = cortex. Following gonadectomy, sulfatase activity in anterior pituitary of males was significantly greater than activity found in intact animals (P less than 0.05). This increase in activity, however, was unaffected by treatment with testosterone, dihydrotestosterone or estradiol-17 beta. Gonadectomy did not change sulfatase activity in brains of males or females or in pituitaries of females. However, sulfatase activity in pituitary glands of females changed significantly (P less than 0.05) with stages of the estrous cycle (metestrus less than diestrus less than proestrus less than estrus). These data indicate sulfatase activity in rat anterior pituitary gland may be controlled by gonadal factors while sulfatase activity in brain is regulated differently.     

Estrogen sulfatase and steroid sulfatase activities in intrauterine tissues of the pregnant guinea pig

The possible role of intrauterine estrogen sulfatase and steroid sulfatase around the time of parturition in the guinea pig was investigated. [3H]Estrone sulfate or [3H]pregnenolone sulfate was incubated with intrauterine tissues. Estrogen sulfatase was found in placenta, endometrium, decidua basalis, amnion and chorion. The presence of steroid sulfatase was established in endometrium and decidua basalis but not in placenta or the fetal membranes. Examination of activities in early (days 32-35), mid (days 44-46) and late (within 5 days of parturition) gestation revealed no significant change in estrogen sulfatase specific activity in decidua basalis. However, in chorion and endometrium this activity was seen to increase approx. 12-fold (P less than 0.001) and 2.8-fold (P less than 0.001), respectively, from early to late gestation. In placenta, estrogen sulfatase activity appeared to increase 2.4-fold (P less than 0.001) and in amnion it decreased 2.8-fold (P less than 0.002). Steroid sulfatase activity in decidua basalis did not change during gestation, while activity in endometrium was found to increase by a factor of 5.3 (P less than 0.001), from early to late gestation. The increases, both in estrogen sulfatase activity in chorion, endometrium and placenta and in steroid sulfatase activity in endometrium, occurred primarily within the final 3 weeks of gestation. In contrast, the decrease in estrogen sulfatase activity in amnion occurred principally between the fifth and sixth weeks of gestation. Analysis of radiolabelled metabolites indicated that estradiol and progesterone could be produced via estrogen sulfatase and steroid sulfatase activities in certain tissues. Subcellular fractionation of tissues revealed that the greatest specific activity and total activity, in all cases, was associated with the 105,000 g pellet. Significant activity was also detected in the 750 and 10,000 g pellets but not in the 105,000 g supernatant. Radioimmunoassay of endogenous estradiol-17 beta (estradiol) in chorion extracts revealed a 6.3-fold increase in the hormone from mid to late gestation. Estradiol levels in endometrium and myometrium did not appear to change during this time. It was concluded that increased estrogen sulfatase activity in guinea pig chorion in late gestation occurs along with elevated levels of the hormone estradiol which may be important for parturition in this species.     

Inhibition of steryl sulfatase activity in LNCaP human prostate cancer cells

The enzyme steryl sulfatase may help support the growth of hormone-dependent tumors, including prostate cancers, by facilitating the conversion of circulating precursor steroids to active hormones. We sought to determine the presence of steryl sulfatase activity in the androgen-dependent human prostate cancer cell line LNCaP, and to determine if this activity was inhibited by known steryl sulfatase inhibitors. Intact LNCaP cultures had steryl sulfatase activity, as determined by conversion of [3H]estrone sulfate (E(1)S) to unconjugated steroids. The level of steryl sulfatase activity was relatively low (4.6 pmol/18 h/million cells) compared to MDA-MB-231 breast cancer cells (284.0 pmol/18 h/million cells). The observed activity in both cell lines was blocked by addition of 1 microM estrone sulfamate (EMATE), an active-site-directed, steroidal inhibitor of steryl sulfatase. Steryl sulfatase activity was also inhibited by Danazol, and by (p-O-sulfamoyl)-tetradecanoyl tyramine (C2-14), a non-steroidal inhibitor. Microsomes prepared from LNCaP cultures also showed steryl sulfatase activity, as determined by hydrolysis of [3H]E(1)S and [3H]dehydroepiandrosterone sulfate (DHEAS) to unconjugated forms. LNCaP and MDA-MB-231 microsomes both hydrolyzed E(1)S about two times faster than DHEAS. Hydrolysis of E(1)S in LNCaP and MDA-MB-231 microsomes was blocked by steryl sulfatase inhibitors with the following relative potencies: EMATE>C2-14>Danazol. These data demonstrate that LNCaP prostate cancer cells contain a steryl sulfatase with properties similar to that found in human breast cancer cells, and that the activity of this enzyme can be blocked by known steryl sulfatase inhibitors. Steryl sulfatase inhibitors may be useful as an adjuvant to androgen deprivation therapy for prostate cancer.     

Steroid sulfatase activities in human leukocytes: biochemical and clinical aspects.

Steroid sulfatase is a membrane-bound microsomal enzyme, present in various tissues. In this report, data on sulfatase activity in peripheral blood leukocytes isolated from normal women and the characterization of its enzyme are studied. In addition, sulfatase activities in placental sulfatase deficiency (PSD) and ichthyosis patients including ichthyosis vulgaris (IV) and recessive X-linked ichthyosis (RXLI) were analysed and were compared with normal subjects. Steroid sulfatase activity was measured by using tritium labeled steroid sulfate as the reaction substrate. It is demonstrated that human leukocytes contain a sulfatase activity for pregnenolone sulfate (P5-S), dehydroepiandrosterone sulfate (DHA-S) and estrone sulfate (E1-S) respectively. This enzyme has a greatest affinity for P5-S, but the activity for E1-S was the highest among the three substrates. The steroid sulfatase activity in female leukocytes is significantly stronger than that in normal males (p less than 0.001) as determined by the cleavage of DHA-S. Sulfatase in leukocytes obtained from the PSD babies and RXLI patients had lower sensitivity. In the case of the mother affected with PSD, the activity was less than half of that in normal men (p less than 0.001) and the levels did not overlap with that in normal women. In patients with IV, the activities were in the normal ranges for both males and females. The measurement of leukocyte sulfatase activity would be a clinically useful tool for the diagnosis of PSD carriers and pedigree analysis.     

The importance of amniotic fluids for the establishment of maternal behaviour in experienced and inexperienced ewes

Maternal behaviour at parturition was studied in multiparous and primiparous ewes whose lambs had been washed to remove amniotic fluids from their coats. In multiparous ewes, washing of the newborn with soap or water decreased licking of the neonate but did not significantly affect other parameters of maternal behaviour (aggressive behaviour, maternal bleats, or acceptance at udder). By contrast, in primiparous ewes, washing of the neonate with only water dramatically reduced licking behaviour and acceptance at udder, while the incidence of aggressive behaviour towards the neonate was increased (P<0·05 in all cases). It is concluded that for inexperienced ewes amniotic fluid on the lamb's coat is necessary for the normal development of maternal behaviour at parturition. For experienced ewes amniotic fluids also play a facilitatory role, but other sensory information can substitute for this cue.     

The iron sulfur protein AtsB is required for posttranslational formation of formylglycine in the Klebsiella sulfatase.

The catalytic residue of eukaryotic and prokaryotic sulfatases is a alpha-formylglycine. In the sulfatase of Klebsiella pneumoniae the formylglycine is generated by posttranslational oxidation of serine 72. We cloned the atsBA operon of K. pneumoniae and found that the sulfatase was expressed in inactive form in Escherichia coli transformed with the structural gene (atsA). Coexpression of the atsB gene, however, led to production of high sulfatase activity, indicating that the atsB gene product plays a posttranslational role that is essential for the sulfatase to gain its catalytic activity. This was verified after purification of the sulfatase from the periplasm of the cells. Peptide analysis of the protein expressed in the presence of AtsB revealed that half of the polypeptides carried the formylglycine at position 72, while the remaining polypeptides carried the encoded serine. The inactive sulfatase expressed in the absence of AtsB carried exclusively serine 72, demonstrating that the atsB gene is required for formylglycine modification. This gene encodes a 395-amino acid residue iron sulfur protein that has a cytosolic localization and is supposed to directly or indirectly catalyze the oxidation of the serine to formylglycine.     

Cloning of a mucin-desulfating sulfatase gene from Prevotella strain RS2 and its expression using a Bacteroides recombinant system

A gene encoding the mucin-desulfating sulfatase in Prevotella strain RS2 has been cloned, sequenced, and expressed in an active form. A 600-bp PCR product generated using primers designed from amino acid sequence data was used to isolate a 5,058-bp genomic DNA fragment containing the mucin-desulfating sulfatase gene. A 1,551-bp open reading frame encoding the sulfatase proprotein was identified, and the deduced 517-amino-acid protein minus its signal sequence corresponded well with the published mass of 58 kDa estimated by denaturing gel electrophoresis. The sulfatase sequence showed homology to aryl- and nonarylsulfatases with different substrate specificities from the sulfatases of other organisms. No sulfatase activity could be detected when the sulfatase gene was cloned into Escherichia coli expression vectors. However, cloning the gene into a Bacteroides expression vector did produce active sulfatase. This is the first mucin-desulfating sulfatase to be sequenced and expressed. A second open reading frame (1,257 bp) was identified immediately upstream from the sulfatase gene, coding in the opposite direction. Its sequence has close homology to iron-sulfur proteins that posttranslationally modify other sulfatases. By analogy, this protein is predicted to catalyze the modification of a serine group to a formylglycine group at the active center of the mucin-desulfating sulfatase, which is necessary for enzymatic activity.     

Neuropeptidergic control of Octopus oviducal gland

The oviducal gland of the female of Octopus vulgaris lies about halfway along the oviduct. Progesterone and 17beta-estradiol receptors have been immunolocalized in the nuclei of the cells of the glandular compartment of previtellogenic glands. We also have evidence of FMRFamide-like and cGnRH-I-like immunoreactivity in the nerve endings that reach the oviducal gland. Moreover, we have recently shown APGWamide immunoreactivity in the glandular cells of the inner part of the oviducal gland. Here we report a review on these findings as well as our latest studies on the effect that neuropeptides may exert on the secretory activity of the oviducal gland. cAMP seems to be a possible second messenger involved in such a process. We discuss the findings of a neuropeptidergic action on the glandular cells of oviducal gland in a more complex frame of molecules, such as steroids, biogenic amines and neuromodulators, controlling the activity of the gland.