Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01178 (oxytocin)
 15,767 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Homogenates of human luteal tissue bound radioiodinated luteinizing hormone releasing hormone agonist. Specific binding was both time- and temperature-dependent. Native LHRH and two LHRH agonists competed for binding, whereas TRH, somatostatin and oxytocin did not, indicating that the binding sites were specific. The apparent Ka values were 2 X 10(7)M-1 for both LHRH agonists and 10(6)M-1 for native LHRH. This is the first demonstration of specific binding of LHRH to human ovarian tissue. No binding could be detected to ovarian tissue from postmenopausal women.
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PMID:Specific binding of luteinizing hormone releasing hormone to human luteal tissue. 630 78

Partially purified cell membranes were prepared from midterm and term placentas after sedimentation on a sucrose density gradient. Biochemical characterization showed that the sucrose density pellet was enriched 8-fold in alkaline phosphatase activity and also contained the majority of [125I]LHRH binding sites. This enrichment was also confirmed by electron microscopy. Specific binding of LHRH was then determined by incubating iodinated LHRH or two of its superanalogs with increasing doses of the corresponding radioinert ligand. Scatchard representation of the data showed curvilinear plots whose first component revealed, for both stages of pregnancy, saturable binding of [125I]LHRH and its agonists with similar association constants (Ka) that ranged between 5.5 X 10(5) M-1 and 1.1 X 10(7) M-1. When standardized per milligram of DNA content, the number of binding sites ranged between 225 and 310 X 10(-12) M. Specificity was evidenced by the inability of a biologically active LHRH antagonist, oxytocin, and TRH to inhibit [125I]LHRH binding. Short term placental cultures incubated with 1.5 X 10(-6)M LHRH had increased production rates of both immunoassayable and bioassayable hCG, and this effect was 4-fold higher in midterm placental cultures. Placental incubations with either buffer or equimolar concentrations of oxytocin or TRH had no effect on hCG production. These observations expand information on extrapituitary binding sites of LHRH and suggest a role for this peptide in the physiology of the human placenta.
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PMID:Luteinizing hormone-releasing hormone binds to enriched human placental membranes and stimulates in vitro the synthesis of bioactive human chorionic gonadotropin. 632 54

The distribution of vasopressin-, oxytocin- and LHRH-containing nerve fibers in the pineal organ of the dog was demonstrated by use of the peroxidase-antiperoxidase immunohistochemical technique. These neuropeptide-containing fibers penetrated through the pineal stalk from the brain, mainly from the posterior commissural region, into the pineal organ. The vasopressin fibers were the most prominent in number, oxytocin fibers and LHRH fibers were the least. Most of these fibers were found in the proximal part of the pineal organ, but some of them were also observed in the distal part. These peptidergic fibers were distributed not only in the perivascular spaces but among the parenchymal cells.
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PMID:Immunohistochemical studies on the peptidergic nerve fibers in the pineal organ of the dog. 635 38

The axonal projections of cell groups containing the most dense collections of steroid hormone concentrating cells have been demonstrated with retrograde neuroanatomical tracing methods. Horseradish peroxidase revealed large numbers of neurons in ventrolateral ventromedial nucleus (VL-VM) which project to dorsal midbrain. Wheat germ agglutinin (immunocytochemical recognition method) revealed large numbers of neurons in medial basal hypothalamus (MBH) and particular subdivisions of paraventricular nucleus (PVN) that project to dorsal caudal medulla or spinal cord. Fluorescent dyes revealed that many preoptic area (POA), anterior hypothalamic (AHA), and bed nucleus of the stria terminalis (BNST) neurons project to ventral tegmental area of Tsai (VTA). Also many neurons in POA and BNST project to amygdala. A method which enabled simultaneous demonstration of the steroid binding capacity and axonal projections of neurons in the same tissue section revealed that 26-36% estradiol (E2) concentrating cells in VL-VM project to dorsal midbrain. E2 concentrating neurons in POA and BNST project to amygdala and E2 concentrating POA neurons project to VTA. These neurons, which send their axons to cell groups located in different brain regions, are probably under the genomic-regulatory influence of E2. Using a method which allows simultaneous demonstration of peptide content and steroid hormone concentrating capacity of cells, many oxytocin-neurophysin and vasopressin-neurophysin containing magnocellular neurons in the caudal PVN were found to concentrate E2. About 4% of the beta-endorphin and about 6% of the dynorphin containing neurons in the MBH concentrate E2. In contrast, virtually none (less than 0.2%) of the LHRH containing hypothalamic neurons concentrate E2.
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PMID:Axonal projections and peptide content of steroid hormone concentrating neurons. 638 52

We have compared the effectiveness of TRH and a rat hypothalamic PRL-releasing factor (PRF; previously incubated with rat serum to destroy TRH) in stimulating the release of PRL into the plasma of conscious lactating rats when injected before and after pituitary PRL had been depleted and transformed into releasable PRL by 10 min of suckling. TRH (1.25 microgramsss) and PRF [equivalent to 2.5 stalk median eminence (SME) fragments] each caused a small increase (38 and 30 ng, respectively) in the plasma PRL concentration within 10 min when injected into nondepleted mothers. The levels then fell quickly. Suckling, by comparison, caused a sustained 175 ng/ml increase above basal levels. Though PRL depletion occurred, as expected, as a result of suckling, there was no measurable depletion within the pituitaries of TRH- or PRF-injected rats. By contrast, the iv administration of TRH (doses ranging from 2-250 ng) and hypothalamic PRF (doses ranging from 0.2-1.0 SME equivalent) after depletion-transformation had been effected by 10 min of suckling resulted in a rapid and, in most instances, a sustained elevation in the plasma PRL concentration comparable to that seen after suckling. Dose-response relationships, though, were not clearly evident with either PRF or TRH. Neither saline, 1.25 microgram TRH previously incubated in serum, 50 mU oxytocin, 1 microgram dopamine, 25 microgram LHRH, nor an extract of cerebral cortex prepared in the same manner as hypothalamic TRH caused plasma PRL to rise after PRL depletion. We conclude that TRH and possibly a separate hypothalamic PRF have a stimulatory action upon the releasable, but not upon the depletion-transformation, phase of PRL secretion in the lactating rat.
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PMID:Evidence that thyrotropin-releasing hormone and a hypothalamic prolactin-releasing factor may function in the release of prolactin in the lactating rat. 677 47

Hypothalmic tissue from 16 to 18-day fetal rats was transplanted onto the choridal pia overlying the superior colliculus in adult female rats. After survival periods of 2 weeks to 19 months, brains containing transplants were processed for monoamine fluorescence histochemistry, immunohistochemistry for three neuropeptides (LHRH, somatostatin, neurophysin), or for autoradiography in ovariectomized hosts that received [3 H] estradiol. Most of the transplants survived and retained or increased in size; 14 of 25 transplants examined by fluorescence histochemistry were found to contain median eminence-like structures. In almost all of the transplants that were stained for neuropeptides, beaded processes and occasional cell bodies were observed. Although immunoreactive fibers were found near blood vessels, no palisade arrangement typical of the normal median eminence was evident. Each of the hypothalamic transplants on which steroid autoradiography was performed contained clusters of estrophilic neurons, the intensity of labeling of which was comparable to that seen in the host hypothalamus. These results indicate that many characteristic morphological and chemical features of the hypothalamus, which are not evident in the 16 to 18-day fetus, are elaborated in transplants during the survival period in the host. Transplantation of fetal hypothalamus to adult choridal pia thus appears to be a valuable approach for studying the factors, humoral or neural, that regulate the differentiation of this brain region.
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PMID:Differentiation of embryonic hypothalamic transplants cultured on the choroidal pia in brains of adult rats. 698 85

In summary, highly vascularized CVOs of the mammalian brain are the site of increased vascular permeability for peptides and other molecules which generally do not cross the blood-brain barrier. In the CVOs the blood-brain barrier is shifted from the level of the capillaries to the tight junctions of the oligociliated ependymal cells. The neurohypophysis is the well known target of various peptidergic neuroendocrine neurons. In the neural lobe, peptide hormones from magnocellular neurons are stored and released into the general circulation in the median eminence, releasing and inhibiting hormones enter the hypothalamo-adenohypophyseal portal circulation. The OVLT appears to be an additional vascular outlet for LHRH and somatostatin. In the pineal, no pinealocytes stain positively for arginine-vasotocin; however, occasionally a single neurophysin (vasopressin or oxytocin) fiber has been observed. In the subfornical organ and area postrema which do not appear to have a primary neuroendocrine function, hemo-neural interactions may be important for effects of circulating peptides and other molecules on specific receptors. In the subcommissural organ, which does not have a special vascular permeability, ependymal cells secrete Reissner's fiber, a mucopolysaccharide, whose function in unclear.
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PMID:Relation of neuropeptides to mammalian circumventricular organs. 701 Sep 39

The distribution of gonadotropin-releasing hormone (GnRH) was studied in the brain and infundibulum (INF) or median eminence of sheep utilizing a peroxidase-antiperoxidase immunohistochemical method. This procedure utilized a specific antiserum generated against GnRH conjugated to bovine serum albumin. In the rostral INF, the greatest concentration of GnRH positive axons was found in the medial region, mostly in the external layer dorsal to the hypophysial portal plexus. In the intermediate portion of the INF, the hormone was mainly observed in the external layer at the more dorsolateral areas ventral to the tuberoinfundibular sulcus. GnRH was generally located medially in the caudal portion of the INF and dorsomedially in the rostral infundibular stalk. Substantial amounts of reaction product were also noted in the internal layer throughout the entire rostrocaudal extent of the INF. The hormone was localized in axons throughout the brain from the septal and medial preoptic areas to the mammillary bodies. GnRH-positive perikarya were scattered in various regions of the infundibular (arcuate) and for the first time in the ventromedial nuclei of sheep hypothalamus. Preabsorption of the specific antiserum with synthetic GnRH abolished staining in both axons and perikarya, whereas preabsorption with thyrotropin-releasing hormone, oxytocin, arginine-vasopressin, and adrenocorticotrophic hormone did not affect staining intensity.
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PMID:Immunohistochemical localization of gonadotropin-releasing hormone (GnRH) in the brain and infundibulum of the sheep. 701 81

Reabsorption and/or degradation of proteins or peptides are functions of the proximal tubule. Large polypeptides or proteins are reabsorbed by luminal endocytosis and hydrolyzed by lysosomal enzymes. Our recent studies indicate that small linear peptides are hydrolyzed at the luminal membrane, with reabsorption of metabolites. The renal transport and hydrolysis of radiolabeled Al, All, BKN, oxytocin, glucagon, insulin, and LHRH were studied. Techniques for in vivo microinfusion of surface tubules in rats, arterial infusion in filtering and nonfiltering rat kidneys in vivo, and in vitro microperfusion of isolated rabbit nephron segments were used. Reabsorption of radiolabeled material was measured and the intact peptide or its metabolites were identified and quantified in urine, renal venous blood, bathing medium, and/or collection fluid. In addition, peptides were incubated in the presence of isolated renal membrane preparations to identify a probably cellular site of hydrolysis. The findings indicate that in proximal, but not distal tubules, radiolabeled Al, All, BKN, glucagon, and LHRH are hydrolyzed by brush border enzymes at the luminal membrane, followed by reabsorption of metabolites. In addition, it was found that, similar to the small intestine, the proximal tubule reabsorbed small peptide fragments, which were further degraded intracellurarly, In vivo inhibition studies with excess peptides revealed that hydrolysis is a more specific process than studies with excess peptides revealed that hydrolysis is a more specific process than reabsorption of metabolites. Large or small, complex peptides like insulin, oxytocin, or vasopressin that contain disulfide bridges are not hydrolyzed at the luminal brush border of the proximal tubule. In vivo sequestration and slow degradation of insulin by rat tubules suggest that this peptide is reabsorbed by endocytosis and degraded in lysosomes. Thus, as the molecular complexity or weight of a peptide increases, the mechanism for renal tubular degradation, instead of depending on luminal membrane hydrolysis, may primarily involve endocytosis and lysosomal digestion. This recently described mechanism for hydrolysis and transport of small linear peptides in the proximal nephron is characterized by having a high capacity and is analogous to membrane hydrolysis described for intestinal microvilli. The process may be biologically important to (1) conserve amino acids, (2) inactivate toxic peptides, and (3) help regulate circulating levels of peptide hormones.
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PMID:Renal tubular processing of small peptide hormones. 704 58

Sixteen peptides were injected intracerebroventricularly to test their effects on rectal temperature of rabbits in a thermoneutral environment. In initial tests 5 micrograms alpha-MSH, ACTH(1--24), oxytocin, vasopressin and glucagon altered body temperature while ACTH(1--10), cholecystokinin, contraceptive tetrapeptide, gastrin, insulin, interferon, leupeptin, LHRH, panhibin (somatostatin), and proctolin did not. Bombesin also altered body temperature but in no consistent direction. In further tests on the effective peptides 1.25--5.0 micrograms alpha-MSH and ACTH(1--24) produced dose-related decreases in rectal temperature as great as 1.0 degrees C. The same doses of oxytocin and glucagon produced small, prolonged hyperthermias which did not exceed 0.4 degrees C. Vasopressin caused rapid development of small increases in rectal temperature; temperature returned to normal in 2--3 hr. The results suggest that five of the peptides tested may have roles in central mediation of normal body temperature, hypothermia, hyperthermia and fever.
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PMID:Central administration of peptides alters thermoregulation in the rabbit. 724 7


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