UNIPROT:P01185 - FACTA Search

Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01185 (vasopressin)
23,126 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In this report, we have reviewed recent information gathered by probing with a push-pull cannula (PPC) the in vivo activity of the suprachiasmatic nucleus (SCN), hypothalamus, and anterior pituitary gland of freely moving animals. In male and female rats, probing of the SCN with the PPC revealed distinct oscillatory patterns of 5-hydroxy indole-acetic acid (5-HIAA) output very much dependent on the position of the cannula. In males, it was also possible to demonstrate, for the first time, in vivo output of immunoreactive vasopressin (VP) most likely from the SCN. Interestingly, the output of VP was stimulated by local activation of probable 5-hydroxytryptamine (5-HT) terminals with 5-hydroxytryptophan (5-HTP), a precursor of 5-HT synthesis. Probing the hypothalamus of rats and rabbits revealed that the in vivo release of luteinizing hormone-releasing hormone (LHRH) (frequency and amplitude of the LHRH signal) can be altered by administration of estrogen to ovariectomized rats; in both species, progesterone stimulated the amplitude of the LHRH signal, but only when this steroid was infused in pulses--the physiological mode of circulating progesterone in the rat. Further, in male rabbits, pulses of progesterone did not stimulate LHRH release. Last, probing the anterior pituitary with the PPC revealed that a series of push-pull perfusions could be performed in the same animal under different experimental conditions for nearly 60 days of experimentation. It also resolved the apparent paradox that after castration, decreased instead of increased activity of the neural LHRH apparatus was noticed when the PPC was positioned in the hypothalamus. Moving the PPC to the anterior pituitary revealed that castration was accompanied by an increase in the amplitude and frequency of the LHRH signals arriving in the anterior pituitary of castrated male rats. This mode of operation of the LHRH pulse generator is clearly compatible with the mode of luteinizing hormone (LH) release in gonadectomized animals. Finally, based on these results, a hypothetical model of the operation of the LHRH pulse generator has been proposed.
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PMID:Release of luteinizing hormone-releasing hormone (LHRH) and neuroactive substances in unanesthetized animals as estimated with push-pull cannulae (PPC). 288 90

Arginine vasotocin (AVT) content was determined in the telencephalon, the hypothalamus, and the pituitary gland of sham-operated and pinealectomized goldfish subjected to 20 degrees and 12/12LD or 24DD photoperiods in winter or spring. The tissues collected at 1000 or 2200 hr were homogenized and extracted in acetic acid. Hypothalamic and telencephalic AVT content, determined by radioimmunoassay, fluctuated throughout the light-dark cycle; AVT content was higher at 2200 than at 1000 hr under the 12/12LD photoperiod. No fluctuations were detected in pituitary AVT content. Telencephalic AVT did not fluctuate under constant darkness, and hypothalamic AVT increased and pituitary AVT decreased compared to the AVT content detected in the 12/12LD groups. No significant effects of pinealectomy or season on AVT levels in the telencephalon, hypothalamus, and the pituitary were evident. The results indicate that AVT content within the preoptico-neurohypophyseal system of the goldfish fluctuate within 24-hr periods and that photoperiod has an effect on the pattern of these fluctuations. The photoperiodic influences do not seem to be mediated by the pineal organ.
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PMID:Diel variations in arginine vasotocin content of goldfish brain and pituitary: effects of photoperiod and pinealectomy. 403 78

Trichloroacetic acid extracts of plasma were fractionated on a CG-50 resin column and the 50% acetic acid eluents chromatographed on silicic acid-impregnated glass paper in butanol-acetic acid-water. The specific arginine vasopressin (AVP) zone was eluted and assayed for antidiuretic activity in the diuretic rat. Thioglycolate inactivation was used to confirm AVP activity. Recovery of as little as 4 muU AVP per ml plasma ranged between 80 and 90%. In normal subjects after an overnight fast, plasma AVP ranged between 2.5 and 10.0 muU per ml. AVP secretion was inhibited by hemodilution and stimulated with nicotine and hypertonic saline. Plasma AVP was absent in patients with diabetes insipidus even after neurohypophyseal stimulation. Plasma AVP was abnormally elevated during mild dehydration and remained above the normal range despite hemodilution in patients with untreated adrenocortical insufficiency demonstrating a delayed water diuresis. Glucosteroid therapy lowered plasma AVP to normal in dehydrated patients. A normal diuretic response to hydration was accompanied by a fall in plasma AVP to zero in steroid-treated patients. These findings suggest that hypersecretion of AVP may play an important role in the abnormal water metabolism of adrenocortical insufficiency and that the glucosteroids promote normal water diuresis by inhibiting the secretion of AVP from the neurohypophysis.
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PMID:Increased plasma arginine vasopressin in clinical adrenocortical insufficeincy and its inhibition by glucosteroids. 601 44

To determine whether propressophysin (vasopressin-neurophysin precursor) is present in human plasma, the nature of the immunoreactive neurophysin was characterized by gel filtration. When plasma samples obtained from six patients with the syndrome of inappropriate antidiuretic hormone secretion due to central nervous system disease were fractionated on a column of Sephadex G-50 in 0.2 N acetic acid, virtually all of the nicotine-stimulated neurophysin (NSN) immunoreactivity coeluted with 125I-labeled NSN. In contrast, gel filtration of plasma from six patients with oat cell carcinoma of the lung with ectopic vasopressin production consistently demonstrated, in addition, a peak of a higher molecular weight (HMW) form of neurophysin. This HMW neurophysin represented 8.7-29.4% of the total NSN immunoreactivity in plasma and its elution profile was not changed when chromatographed after incubation in 6 M urea. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the HMW neurophysin ran in the 20,000-dalton area of the gel. A substantial portion of the HMW neurophysin appeared to be a glycoprotein judging from its binding to Concanavalin A. When the HMW neurophysin was incubated with trypsin, most of the immunoreactivity was converted into a smaller neurophysin which bound to a vasopressin-agarose column in a pH-dependent manner. Moreover, a definite peak of immunoreactive vasopressin appeared after the trypsin treatment. This peak coeluted with synthetic arginine vasopressin on gel filtration and had the characteristic affinity of vasopressin for neurophysin-agarose. These results indicate that propressophysin circulates in patients with oat cell carcinoma of the lung with ectopic vasopressin production and suggest that plasma propressophysin may be a marker for ectopic vasopressin production.
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PMID:Propressophysin in human blood: a possible marker of ectopic vasopressin production. 608 1

The calcium-complexing abilities of acetate, bicarbonate, lactate, succinate, and citrate were quantified, and were found to differ substantially. Acetate was a more potent vasodilator than lactate, and the vasorelaxant potencies of acetate and lactate failed to correlate with their calcium-complexing ability. The vasodilator action of acetate was not abolished after correction for complexing of ionized calcium. Strips constricted with vasopressin were especially sensitive to the vasodilator effects of acetate.
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PMID:Calcium-complexing versus vasorelaxant effect of acetate, lactate, and other bases. 609 30

L[35S]Cys-arginine vasopressin, -oxytocin, and -somatostatin were purified from hypothalami and neurohypophyses 4 h after rats received L[35S]Cys via the third ventricle. After acetic acid extraction, Sephadex G-25 filtration, and chemoadsorption to C18-silica (Sep-Pak cartridges), the labeled peptides were rapidly separated by gradient elution, reversed phase, high pressure liquid chromatography (HPLC). The identity and isotopic purity of the labeled peptides were determined by several reversed phase HPLC procedures in conjunction with chemical modification. The labeled peptide fractions were at least 50% radiochemically pure. Using this HPLC isolation procedure, incorporation of L-[35S]Cys into each peptide was determined n hydrated and dehydrated rats. Label incorporation into arginine vasopressin and oxytocin in the hypothalamus and the neurohypophysis of dehydrated rats was 2-3 times greater than that in hydrated rats. Incorporation of label into hypothalamic and neurohypophyseal somatostatin was unaffected by the hydration state of the animal. This procedure thus provides a very rapid, but sensitive, set of techniques for studying the control of small peptide biosynthesis in the brain.
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PMID:In vivo biosynthesis of L-[35S]Cys-arginine vasopressin, -oxytocin, and -somatostatin: rapid estimation using reversed phase high pressure liquid chromatography. 611 94

In an attempt to delineate the nature of the immunoreactive neurophysins in oat cell carcinomas of the lung with ectopic vasopressin production, tumor neurophysins were characterized by gel filtration and by electrophoresis. In all of the five tumor tissues, activities of both vasopressin and nicotine-stimulated neurophysin (NSN) determined by radioimmunoassay were demonstrated. A small amount of oxytocin as well as estrogen-stimulated neurophysin was detected in three of the tissues. When tissue extract was subjected to Sephadex G-50 gel filtration in 0.2 N acetic acid, the major portion of immunoreactive NSN emerged in the fractions corresponding to the molecular size of 10,000. The migration pattern of NSN in these fractions on electrophoresis was qualitatively the same as that of NSN extracted from human posterior pituitary glands. In addition to this major neurophysin, immunoreactive NSN with the molecular size of 20,000 was consistently demonstrated in three tumor extracts. This high molecular weight form of neurophysin represented 6.5--8.7% of total NSN immunoactivities in each tumor extract and its elution profile was not changed when analyzed under denaturating conditions in 6 M guanidine hydrochloride. On electrophoresis, it migrated near the gamma globulin region; however, the peak was broad suggesting that it consists of more than two different molecular populations. A substantial portion of the high molecular weight NSN appears to be a glycoprotein judging from its binding to concanavalin A. When the high molecular weight from of neurophysin was incubated with trypsin, essentially all of the activities were converted into NSN with the molecular size of 10,000. Moreover, an equimolar amount of vasopressin was liberated after the treatment, the elution pattern of which closely resembled that of synthetic arginine vasopressin. When a lower concentration of trypsin was used, some of the 20,000-dalton neurophysin exhibited activities of both NSN and vasopressin. Since the antivasopressin serum used in this study appeared to be directed toward the ring portion side of vasopressin, these results suggest that this 20,000-dalton neurophysin is, in all probability, a common precursor to vasopressin and neurophysin, and that vasopressin may be located in the middle of the precursor molecule.
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PMID:Nature of the immunoreactive neurophysins in ectopic vasopressin-producing oat cell carcinomas of the lung. Demonstration of a putative common precursor to vasopressin and neurophysin. 626 3

A sensitive and specific radioimmunoassay (RIA) for arginine vasopressin (AVP) has been developed and validated. Synthetic AVP was coupled to bovine serum albumin (BSA) with glutaraldehyde. Antisera against AVP were raised in three rabbits immunized with AVP-BSA complex. After 6 months, at the 16th injection, one of the antisera had a titer high enough to be utilizable for RIA at a final dilution of 1:400,000. The labeling of AVP with 125I Na was performed with the modified chloramine T method, and the purification of iodinated AVP was done with gel filtration chromatography on a Sephadex G-25 fine column (1 X 20 cm) with an elution buffer of 0.01 M acetic acid containing 0.1% BSA. Radioactivities from the Sephadex G-25 were eluted in three peaks. 125I-AVP, which was reactive to the antiserum, was contained in the third peak, and 125I-AVP in the fractions on the down slope of the peak was used for the radioligand in the amount of 1000 cpm. The specific activity of purified 125I-AVP was about 400 muCi/microgram. Diluted antiserum and samples, unlabeled AVP or related peptides were preincubated at 4 degrees C for 24 hr, and then 125I-AVP was added to the mixture and incubated for a further 72 hr. Separation of B and F was done with polyethyleneglycol. The minimal detection limit of AVP, which was 95% of the confidence limit of the mean value of B0, was 0.4 pg/tube. The cross-reactivities with lysine vasopressin, arginine vasotocin, DDAVP and oxytocin were 0.1%, 30%, 1% and 0%, respectively. AVP in plasma was extracted with cold acetone and petroleum ether. The recoveries of synthetic AVP from plasma which was added (2-16 pg) were more than 94%. The intra and inter-assay coefficients of variation determined by plasma of AVP concentration of about 4.8 pg/ml were 8.7% and 11.3%, respectively. The RIA detected AVP of concentration as low as 1 pg/ml following the extraction procedure. AVP immunoreactivity was detected without extraction in urine, and the lyophilized cerebrospinal fluid and acid extract of tissues of the central nervous system, and the reactivities in these samples were demonstrated to be immunologically identical to that of synthetic AVP when diluted serially. The changes of plasma and urinary AVP concentration on water intake, water deprivation and smoking in humans were clearly demonstrated.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:[A sensitive and specific radioimmunoassay for arginine vasopressin and its validation]. 647 76

Hypothalamic median eminence extracts (MEE) were subjected to gel filtration on Sephadex G-25 and G-75 columns to characterize the corticotropin releasing factor (CRF) in relation to arginine vasopressin (AVP). CRF activity was measured using monolayer cultured anterior pituitary cells, and AVP was measured by radioimmunoassay. Sephadex G-25 chromatography of AVP immunoreactivity of MEE (NIAMDD-Rat HE-RP-1) showed three peaks on elution with 0.1 N HCI and four peaks on elution with 0.2M acetic acid. But freshly prepared MEE showed only one peak on elution with 0.1 N HCI. These results suggest that AVP in NIAMDD-Rat HE-RP-1 is polymerized or aggregated on the Sephadex G-25 column, especially when eluted in 0.2M acetic acid. Two main peaks of CRF activity appeared consistently on both Sephadex G-25 and G-75 chromatography. One was near the void volume and the other was retarded. The small molecular CRF (small-CRF) peak was coeluted with immunoreactive AVP and 125I-AVP, on both chromatographies on elution with 0.1 N HCI. The large molecular CRF (big-CRF) appeared between the void volume and I-39 ACTH on Sephadex G-75 chromatography. Big-CRF from freshly prepared MEE had no AVP immunoreactivity. AVP showed CRF activity in pituitary cell cultures, but its CRF activity accounted for no more than 20% of the CRF activity of NIAMDD-Rat HE-RP-1. The log dose-response characteristics of the CRF activities of small-CRF and AVP differed. These results suggest that the median eminence has at least two substances with CRF activity: one is large molecular CRF, and the other is small molecular CRF which may have a vasopressin-like molecular weight. AVP may account for a part of the CRF activity of small molecular CRF but is not identical with genuine CRF.
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PMID:Characterization of corticotropin releasing factor (CRF) and arginine vasopressin in median eminence extracts on sephadex gel-filtration. 697 67

Synthetic arginine-vasopressin (AVP), oxytocin (OXY) and arginine-vasotocin (AVT) were labelled with radioiodine at a moderate specific activity. The purity of the labelled octapeptides was checked by descendent paper chromatography in butanol-acetic acid-water (4 : 1 : 5 v/v) after a double filtration on a Sephadex G-25 column of the labelling mixtures. The rabbit anti-AVP serum bound 125I--AVP, the highest binding belling observed on the descendent eluates from the Sephadex column. The antiserum is specific to AVP, no binding being observed will AVT or oxytocin. The sensitivity of a RIA system using 125I--AVP, commercial anti-AVP serum and polyethyleneglycol separation technique, was of 5 pg/ml in terms of AVP with a biological activity of 385 IU/mg. The validity of the assay was tested on five patients (two with diabetes inspidus (DI) and three with other endocrine diseases) submitted to dehydration of hydration tests.
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PMID:Labelling of octapeptide neurohormones for in vitro studies. Radioimmunologic assay for arginine-vasopressin. 729 46

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