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Query: UNIPROT:P01185 (vasopressin)
 23,126 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In a preliminary report we described the effects of rat prolactin on the incorporation of [14C]acetate into lipids by a cell line from a dimethylbenz(a)anthracene-induced rat mammary tumor. The characteristics of the response to prolactin were very similar to those described for the normal rat mammary gland; namely, insulin was required for full expression of the response, maximal activity was not seen until 36 hr after the addition of the hormones, and growth hormone was able to elicit the same response. However, we were unable to detect binding of 125I-labeled prolactin to these cells, and furthermore, other more purified prolactin preparations were inactive. Upon further investigation we discovered that the activity resided in a low-molecular-weight fraction of the rat prolactin B-1 preparation and was probably either vasopressin or oxytocin or both. These data suggest the possibility that vasopressin may play a role in rodent mammary tumorigenesis.
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PMID:Vasopressin stimulation of acetate incorporation into lipids in a dimethylbenz(a)anthracene-induced rat mammary tumor cell line. 10 Feb 17

WRK1 cells (a rat mammary tumor cell line) exhibit a vasopressinergic receptor of V1a subtype tightly coupled to phospholipase C. Addition of dexamethasone to the culture medium principally potentiated the vasopressin-sensitive accumulation of inositol phosphates and to a lesser extent the NaF-sensitive phospholipase C activity. On the opposite, such treatment was without effect on the basal level of intracellular inositol phosphates or on bradykinin- or serotonin-sensitive phosphoinositide metabolisms. Glucocorticoid receptors were probably involved in these actions since dexamethasone was found to be more potent than aldosterone or corticosterone. Dexamethasone treatment also increased the number of vasopressin binding sites without affecting its affinity for vasopressin or other specific vasopressin analogues. These results strongly suggest that dexamethasone principally acts at the vasopressin receptor level by affecting its synthesis and/or the translation of its mRNA and also affects the G protein that couples the V1a receptor to the phospholipase C. These results explain how glucocorticoids may regulate the transduction mechanisms involved in vasopressin actions on WRK1 cells. They provide explanations for understanding the cross talk between adrenal steroids and hormones, which mobilize intracellular calcium.
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PMID:Upregulation of V1a vasopressin receptors by glucocorticoids. 147 77

We have investigated the metabolic interrelationships of the major inositol phosphates in vasopressin-stimulated WRK 1 mammary tumor cells which were labeled to equilibrium with [14C]inositol and briefly, just prior to stimulation, with [3H]inositol. A comparison of the 3H/14C ratios of these compounds with those of the cellular inositol lipids suggests that most of the known inositol mono-, bis-, tris-, and tetrakis-phosphates are derived from precursors with turnover rates similar to those of these lipids. However, Ins(3,4,5,6)P4 (which is the major inositol tetrakisphosphate to accumulate in stimulated WRK 1 cells), Ins(1,3,4,5,6)P5, and InsP6 had 3H/14C ratios of 0 in this experiment, indicating that they must have a different metabolic origin.
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PMID:Inositol phosphates in receptor-mediated cell signaling: metabolic origins and interrelationships. 228 2

WRK1 cells, an established cell line derived from a chemically induced mammary tumor in the rat, are sensitive to vasopressin. Binding studies with intact WRK1 cells indicated the presence of a single population of [3H]vasopressin binding sites (dissociation constant, Kd = 12.7 +/- 0.2 nM, maximal binding capacity = 75 +/- 6 fmole/10(6) cells). Competition experiments using a series of vasopressin analogs with enhanced selectivity for the three subtypes of receptors already characterized--that is, renal V2 receptors, V1 receptors of the vascular or hepatic subtype (V1a), and V1 receptors from rat adenohypophysis (V1b)--indicated that vasopressin receptors from WRK1 cells have a ligand specificity very similar, if not identical, to that of V1a receptors. Vasopressin induced a marked (up to tenfold) increase in the production of labeled inositol phosphate (Ins 1,4,5 P3, Ins 1,4 P2, and Ins P) by WRK1 cells prelabeled with [3H]inositol. Antagonists of the vasopressor effect of vasopressin inhibited vasopressin-induced inositol lipid breakdown in WRK1 cells. For the entire series of vasopressin analogs tested, there was a close correlation between the respective Kd values for binding of these peptides to WRK1 cells and the corresponding Ka or Ki values derived from the determination of dose-dependent stimulation of inositol phosphate production, or inhibition of vasopressin-induced stimulation.
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PMID:WRK1 cells: a model system for studying properties of V1a vasopressin receptors. 243 65

Specific vasopressin binding to WRK-1 rat mammary tumor cells was assessed and compared with vasopressin-induced alterations in phosphatidylinositol metabolism. Scatchard analysis revealed the presence of two binding sites: a saturable, high affinity site with a dissociation constant of 1 X 10(-9) M and an n of 2700 sites per cell, and a nonsaturable, apparent lower affinity site. The higher affinity site appeared to have V1a specificity and to correlate with vasopressin's ability to stimulate phosphatidylinositol turnover in the cells.
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PMID:Characterization of the vasopressin receptor on WRK-1 cells. 296 14

We have previously characterized two distinct pools of phosphatidylinositol (PI) in the WRK-1 rat mammary tumor cell, one whose metabolism is enhanced in response to vasopressin and another which is insensitive to hormonal manipulation. The purpose of the present study was to examine the relationship between cellular phosphatidylinositol 4,5-bisphosphate (PIP2) and each of the two PI pools. We have found that in WRK-1 cells, vasopressin induces the rapid loss of PIP2 and the accumulation of inositol phosphates. By making use of kinetic differences in 32Pi uptake into the two pools of PI and assessing radioactivity levels in the 1-phosphate of PIP2, we have determined that hormone-sensitive PI is the precursor of approximately 60% of the cellular PIP2; the remainder is synthesized from the hormone-insensitive pool. Additional data indicate that PIP2 derived from hormone-sensitive PI is likewise hormone-sensitive, while that synthesized from hormone-insensitive PI remains stable over a long period of time and is not affected by the presence of vasopressin.
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PMID:The relationship of hormone-sensitive and hormone-insensitive phosphatidylinositol to phosphatidylinositol 4,5-bisphosphate in the WRK-1 cell. 300 Oct 64

WRK-1 rat mammary tumor cells respond to vasopressin with an increase in the rate of phosphatidylinositol turnover. Evidence derived from a series of experiments performed under various prelabeling conditions suggests that the hormone-sensitive phosphatidylinositol resides in a distinct pool within the cell, accounting for approximately 17% (8-37%) of the total cellular phosphatidylinositol. The possibility that two distinct cell types might explain this finding is unlikely since neither newly cloned nor thymidine-blocked cells exhibit any alteration in the nature of their response. This hormone-sensitive phosphatidylinositol moiety has the following characteristics. 1) Under equilibrium labeling conditions, it is completely turned over within 5 min of hormone addition. 2) It is both synthesized and degraded even in the absence of hormone, although at a much slower rate. 3) Under the conditions employed, there does not appear to be transfer of phosphatidylinositol from the insensitive to the sensitive pool. A model of these events is outlined.
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PMID:Characterization of the hormone-sensitive phosphatidylinositol pool in WRK-1 cells. 665 10

WRK-1, a cell line in long-term culture derived from a 7, 12-dimethylbenz[a]anthracene-induced rat mammary tumor, responds to physiologic concentrations of vasopressin with increased precursor incorporation into phospholipids and with increased protein accumulation. Because vasopressin has been reported to be a potent mitogen for Hela cells and 3T3 cells, a study was conducted to determine whether it could act as a mitogen for WRK-1 cells. Under no conditions was a clear-cut mitogen response to vasopressin demonstrated.
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PMID:Vasopressin: action on WRK-1 rat mammary tumor cells. 680 67

Using the vasopressin-sensitive rat mammary tumor cell line, WRK-1, we examined conditions under which vasopressin was able to stimulate turnover of prelabeled, radioactive phosphatidylinositol. Only cells which had been preincubated with 32Pi in the presence of hormone were able to subsequently respond to the hormone by increased loss of radioactivity from phosphatidylinositol. In addition, in experiments performed with uniformly labeled cells, we estimated that the hormone-sensitive phosphatidylinositol accounted for 17% of the total cellular phosphatidylinositol. Implications of these findings are discussed.
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PMID:The phosphatidylinositol cycle in WRK-1 cells. Evidence for a separate, hormone-sensitive phosphatidylinositol pool. 703 62

An early manifestation of the response of WRK-1 rat mammary tumor cells to vasopressin is an increase in incorporation of (32P)Pi into phospholipids. Incorporation into all classes of phospholipids is stimulated; however, incorporation into phosphatidylinositol (PI) is increased to the greatest degree (3- to 10-fold as compared with 1.3- to 2-fold for the other phospholipids). Furthermore, increased incorporation into PI is accompanied by an increased rate of PI turnover; turnover rates of the other phospholipids are unaffected by vasopressin.
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PMID:A new model system for studying the phosphatidylinositol cycle. 705 Jan 32


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