Determination of the functional molecular size of vasopressin isoreceptors

Crause, Peter; Boer, Rainer; Fahrenholz, Falk

doi:10.1016/0014-5793(84)80773-5

Cited by 22 publications

(7 citation statements)

References 16 publications

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“…Al though these studies report receptor molecular weights ranging from 60 to 100 kD, most are consistent with those we have found [23,24,[27][28][29]. For instance, Knigge et al [24], using quite similar techniques, reported molecular weights of 55 and 62 kD.…”

Section: Discussionsupporting

confidence: 88%

“…In previous experi ments, Knigge et al [22] have shown that vasopressin competes with a vasopressin anti-idiotype antibody for receptors on the paraventricular and supraoptic nuclei of the hypothalamus. The same investigators [22,29] also have reported that PVA (the 5'-3' complement of AVP) and a vasopressin-binding protein prepared from rat brain membranes were capable of blocking the staining of AVP receptors by vasopressin anti-idiotype an tibody. This evidence suggests that the receptor/vasopressinbinding protein and PVA have similar binding site structures, as they both bind to the anti-idiotypic antibody.…”

Section: Discussionmentioning

confidence: 96%

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An Antibody Directed against a Peptide Encoded by RNA Complementary to mRNA for Vasopressin Recognizes Putative Vasopressin Receptors

Swords

Carr²,

Blalock³

et al. 1990

Neuroendocrinology

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The purpose of this study was to generate an antibody against the binding site of the vasopressin receptor. Recently it has been demonstrated that complementary RNA sequences may encode interacting peptides. We determined whether or not an antibody directed against a peptide (PVA) specified by RNA complementary to the mRNA of rat arginine vasopressin (AVP) would recognize the AVP receptor. The antibody was purified sequentially over a protein A and then a PVA affinity column. A specific anti-PVA antibody affinity column also was made. The specific anti-PVA antibody recognized two proteins with molecular weights of 76 and 70 kD in homogenates from kidney and brain tissue containing the hypothalamus/thalamus/septum. This antibody also blocked binding of ³H-AVP to primary cultured neuronal cells, whereas the nonspecific antibody did not. Furthermore, the blocking efficiency of the antibody increased when more of the specific anti-PVA antibody was present. We also determined whether or not the antiserum contained any biological activity by observing urine volume and urine osmolality in the presence or absence of preimmune or immune serum. Only the immune serum was able to reverse the antidiuretic and urine-concentrating effects of AVP, suggesting that the antibody antagonized the effects of AVP on the kidney. Taken together with the observation that this antibody did not bind to vasopressin, these data strongly indicate that an antibody to the vasopressin receptor binding site has been made and add further support to the molecular recognition theory.

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Section: Discussionsupporting

confidence: 88%

Section: Discussionmentioning

confidence: 96%

An Antibody Directed against a Peptide Encoded by RNA Complementary to mRNA for Vasopressin Recognizes Putative Vasopressin Receptors

Swords

Carr²,

Blalock³

et al. 1990

Neuroendocrinology

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“…Membrane-bound tritiated hormone was separated from free hormone by rapid filtration over cellulose acetate filters (0.22 pm). The filters were washed twice with the filtration medium and counted as described [15]. Specific binding was obtained by the difference between 3H-labelled ligand binding in the absence and presence of a 100-fold excess of unlabelled hormone.…”

Section: Preparation Of Membrane Fractionsmentioning

confidence: 99%

Identification of a myometrial oxytocin‐receptor protein

Fahrenholz

Hackenberg

Muller

1988

European Journal of Biochemistry

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The specific binding of [3H]oxytoxin to uterine membrane peparations derived from different species at late pregnancy was examined. The highest receptor density (b,,, value) was found in membranes derived from the myometria of guinea pigs between day 60 post-conception (b,,, = 3.6 f 0.1 pmol/mg) and day 65 (b,,, = 4.4 f 0.1 pmol/mg). The similarity of & values for oxytocin binding (Kd = 2.6 f 0.2 nM) and for vasopressin binding (& = 2.1 f 0.4 nM) to the same membranes derived from a guinea pig myometrium indicate a homogenous population of high-affinity binding sites which do not discriminate between these two hormones.Competitive binding experiments with specific oxytocin agonists containing either sarcosine or N-methylalanine in the place of Pro' demonstrated that these myometrial receptors have the pharmacological properties of oxytocin receptors.The analogue of 1 -deamino-[8-lysine]vasopressin containing a photoreactive azidophenylamidino group at the sidechain of Lys' retained roughly the same receptor affinity as oxytocin. In photoaffinity labelling experiments with the tritium-labelled analogue a membrane protein from guinea pig myometrium with an apparent relative molecular mass M , of 78000 f 5000 (n = 13) was preferentially labelled. The labelling of this protein was completely suppressed by a 100-fold molar excess of either oxytocin, or [Sar7]oxytocin or [Thr4, Sar7]oxytocin, but not by other peptide hormones. These results provide evidence that the labelled 78000-M, protein is a myometrial oxytocin-receptor protein.The neurohypophysial nonapeptide oxytocin stimulates the contraction of smooth muscle cells in the myometrial layer of the uterus. The existence of specific oxytocin receptors has been demonstrated in the animal and human myometrium [l, 21. The oxytocin sensitivity of the uterus increases during pregnancy and is accompanied by an estrogen-induced increase in the concentration of myometrial oxytocin receptors at late pregnancy and at early-term labor [3 -51.The molecular events which are triggered after binding of oxytocin to its myometrial receptor are not well understood. There is evidence for inositol phosphate production [6] and for Ca2+ influx in the myometrium [7]. Furthermore, oxytocin has been shown to inhibit a (CaZ+ + MgZ+) ATPase [8] and to increase the intercellular communication via gap junctions [9].Little is known about the oxytocin receptor's physical properties. Soloff and Fernstrom were able to solubilize with a relatively low yield (20 -25%) oxytocin binding sites from the pregnant rat myometrium and the rat mammary gland with a zwitterionic detergent [lo]. Gel filtration analysis indicated that the solubilized oxytocin binding components from rat mammary gland were present in multiple molecular mass forms: M, values ranged from 40000 to greater than 200000. The uterine oxytocin-receptor protein, however, has not yet been identified. The present study was performed to identify myometrial oxytocin-receptor proteins. For this purpose, a myometrial membrane from guinea pig c...

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“…Vasopressin induces the pressor and antidiuretic response through activation of two separate receptors, the V1-and V2-receptor respectively (Michell et al, 1979). The receptors are coupled to different intracellular second messengers and differ in their molecular size Crause et al, 1984). For example, Vl-receptor activationinhepatocytesisrelatedtoinositolphospholipid hydrolysis and intracellular Ca2, mobilization, whereas V2-receptor activation in renal tubular cells leads to an increase of cyclic AMP (Kirk et al, 1977(Kirk et al, , 1979(Kirk et al, , 1981Michell et al, 1981;Thomas et al, 1984;Charest et al, 1985;Butlen et al, 1978).…”

Section: Introductionmentioning

confidence: 99%

Activation of V1-receptors by vasopressin stimulates inositol phospholipid hydrolysis and arachidonate metabolism in human platelets

Siess¹,

Stifel²,

Binder³

et al. 1986

Biochemical Journal

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The activation of platelet V1-receptors by vasopressin (0.01-1 microM) induces the rapid formation of inositol phosphates, 1,2-diacylglycerol and phosphatidic acid, indicating inositol phospholipid hydrolysis by phospholipase C. Vasopressin immediately induces the formation of inositol bisphosphate and inositol trisphosphate. Accumulation of inositol 1-monophosphate and inositol 4-monophosphate occurs later after a time lag of 15 s. Low concentrations (10-100 nM) of vasopressin only activate phospholipase C, whereas high concentrations (1 microM) induce activation of phospholipase C and subsequently the production of arachidonate metabolites. Cyclo-oxygenase metabolites are associated with further activation of phospholipase C, release reaction and irreversible platelet aggregation. Vasopressin requires for its action extracellular Mg2+, but not Ca2+. The described platelet changes are not induced by 1-desamino-[8-D-arginine]vasopressin, a V2-receptor agonist, and are blocked by a specific V1-receptor antagonist. The results indicate that platelets possess a V1-receptor that is coupled to polyphosphoinositide hydrolysis by phospholipase C, leading to the formation of 1,2-diacylglycerol and inositol trisphosphate. Those compounds may act as second messengers for platelet responses induced by vasopressin, whereas endoperoxides and thromboxane A2 stimulated by vasopressin may serve as amplifiers for platelet activation.

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Determination of the functional molecular size of vasopressin isoreceptors

Cited by 22 publications

References 16 publications

An Antibody Directed against a Peptide Encoded by RNA Complementary to mRNA for Vasopressin Recognizes Putative Vasopressin Receptors

An Antibody Directed against a Peptide Encoded by RNA Complementary to mRNA for Vasopressin Recognizes Putative Vasopressin Receptors

Identification of a myometrial oxytocin‐receptor protein

Activation of V1-receptors by vasopressin stimulates inositol phospholipid hydrolysis and arachidonate metabolism in human platelets

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