Dopamine stimulation of CAMP production in cultured opossum kidney cells LINDA CHENG, PATRICIA PRECHT, DEBORAH FRANK, AND C. TONY LIANG Laboratory of Biological Chemistry, National Institute on Aging, National Institutes of Health, Gerontology Research Center, Baltimore, Maryland 21224

receptors (16). In rat kidney cortex, a DAl-receptor has been identified by radioligand binding studies with a selective DA1-antagonist (14, 19). In addition, dopamine Electrolyte Physiol. 27): F877-F882, 1990.-Dopamine recep- receptors identified by nonselective dopamine antagonist tors have been identified in many tissues including the kidney. binding studies are found in the proximal tubule of the To establish an in vitro system as a model for dopamine action, we studied the effect of dopamine (DA) receptor agonists and rabbit (12). In renal proximal tubules and renal arteries, antagonists on adenosine 3’,5’-cyclic monophosphate (CAMP) the DA1-receptor is linked to a stimulation of adenylate formation in opossum kidney (OK) cells. The stimulation of cyclase activity (1, 11, 32). Renal arteries and glomeruli CAMP production in these cells by dopamine was dose depend- DAz-receptors, not associated with the adenylate cyclase ent, and markedly higher levels were observed in the presence system, have also been reported (12,21). Recently, it has been reported that DA1- and DAz-receptors are present of dopamine plus a phosphodiesterase inhibitor, 3-isobutyl-lmethylxanthine. Half-maximal stimulation was found with 1.15 in both brush-border and basolateral membranes of renal + - 0.22 PM dopamine. A DAl-receptor agonist, SKF 82526J, proximal tubule (9, 10). DA1- but no DAz-agonists instimulated CAMP production, whereas a DAa-receptor agonist, crease adenylate cyclase and phospholipase C activities Ly 171555, did not. The stimulatory effects of dopamine and in both membranes (9, 10). Primary cultured mesangial SKF 825265 were abolished by a specific DA1-receptor antag- cells and juxtaglomerular cells possess DAl-receptors onist, Sch 23390 with half-maximal inhibition concentrations (24, 34). Cultured mesangial cells respond to dopamine of 1.24 t 0.18 and 4.0 & 0.5 nM, respectively. In contrast, the monophosphate DAz-receptor antagonist, spiperone, had no inhibitory effect on by increasing adenosine 3’,5’-cyclic (34), whereas activation of DA1dopamine- and SKF 82526J-stimulated CAMP production. @- (CAMP) production cells induces renin release Adrenergic antagonists failed to attenuate the stimulatory ef- receptor in juxtaglomerular (24) fects of dopamine and SKF 825265 on CAMP production. In Thus far, dopamine receptors have not been studied addition, the ,&adrenergic receptor agonist, isoproterenol, did not stimulate CAMP production. These results suggest that the in continuously cultured renal cells. The established action of dopamine was not mediated through ,&adrenergic opossum kidney (OK) cell line retains properties of the receptors. Furthermore, our results clearly demonstrated the proximal tubule (23), including a parathyroid hormone existence of DA1-receptors linked to adenylate cyclase in OK (PTH)-inhibitable sodium-dependent phosphate transcells. port system and a PTH-stimulatable adenylate cyclase (4, 8, 28, 35). Recently, az-adrenergic receptors (5, 30) dopaminel receptor; catecholamine and serotoninl receptor (30) were also identified in OK cells. It has also been reported that dopamine can interact with CY-and ,&adrenergic receptors (20). The availaDOPAMINE MODULATES a variety of physiological funcbility of specific agonists and antagonists allows one to tions in the kidney, including increasing renal blood flow, discriminate between the different receptors. In the presglomerular filtration rate, and sodium excretion (26). ent study, we examine the effects of dopamine, as well The natriuretic effect of exogenously administered do- as its agonists and antagonists, on CAMP formation in pamine has been attributed to the change in renal blood OK cells. We also study the effects of P-agonists and flow and glomerular filtration rate (20, 29). However, antagonists on CAMP production in OK cells. A prelimdopamine-induced natriuresis can occur in the absence inary communication of this study has been reported (6). of changes in renal hemodynamics (36). Dopamine alters sodium reabsorption in the renal proximal tubule, but METHODS the results are conflicting. In microperfusion experiments on the rabbit proximal tubule, the addition of Cell culture. Growth and subculture of OK cells were dopamine to the bathing solution decreased sodium reab- performed as previously described (5). Briefly, the cells sorption (3). In other studies, dopamine increased sodium were grown on plastic tissue culture dishes containing uptake into rabbit proximal renal cells (25). low-glucose (1 g/l) bicarbonate-buffered Dulbecco’s modThe action of dopamine may be mediated through ified Eagle’s medium (DMEM) supplemented with 10% interaction with specific dopamine receptors. There are fetal calf serum, penicillin (50 pg/ml), streptomycin (50 two subclasses of dopamine receptors, DA1- and DA2- pg/ml), and neomycin (100 pg/ml). All studies were CHENG, LINDA, PATRICIA PRECHT, DEBORAH FRANK, AND C. TONY LIANG. Dopamine stimulation of CAMP production in cultured opossum kidney cells. Am. J. Physiol. 258 (Renal Fluid

F877 Downloaded from www.physiology.org/journal/ajprenal at Tulane University (129.081.226.078) on February 12, 2019.

F878

DOPAMINEl

RECEPTOR

performed with cells between passages 65 and 82. For experiments, the cells were grown in 35-mm-diameter dishes to confluency (-5-6 days). The medium was changed to DMEM without bicarbonate 30 min before the addition of test compounds. The medium was adjusted to pH 7.4 with 20 mM N-2-hydroxyethylpiperazine-N’-2-ethanesulfonic acid (HEPES)-KOH, and the cells were preincubated at 37°C in air. CAMP measurement. Agonist and antagonist solutions (final volume 10 ~1) were added to cell monolayer in 1 ml DMEM without bicarbonate. After a lo-min incubation at 37”C, the reaction was stopped by the addition of 50 ~1 of 60% perchloric acid. Aliquots were taken for the measurement of total CAMP content. CAMP was determined with a radioimmunoassay kit (Incstar, Stillwater, MN). Adenylate cyclase assay. To assess OK cell adenylate cyclase activity, crude membranes of OK cells were prepared. Cells were washed and harvested with phosphatebuffered saline and pelleted by centrifugation at 2,000 g for 5 min. The pellet was resuspended in 30 vol of icecold 50 mM tris(hydroxymethyl)aminomethane (Tris)HCl (pH 7.6) and 1 mM EDTA and were homogenized in a Polytron homogenizer at setting 6 for 10 s. The homogenate was centrifuged at 25,000 g for 15 min. The membranes were resuspended in the same buffer and then recentrifuged at 25,000 g for 15 min. Membranes were suspended in a small volume of buffer and stored at -65°C until used. Adenylate cyclase activity was assayed as described previously (27). Protein determination. The cell monolayer was solubilized in 0.5 N NaOH. Protein was measured using the Bio-Rad protein assay kit with bovine serum albumin as the reference protein. Materials. Cell culture media were purchased from GIBCO. All catecholamines and other chemicals were obtained from Sigma Chemical. The following drugs were gifts from their respective pharmaceutical companies: SKF 825265 (Smith Kline & French Laboratories, Philadelphia, PA) and Ly 171555 (Lilly Research Laboratories, Indianapolis, IN). (+) -Butaclamol hydrochloride and Sch 23390 were obtained from Research Biochemicals (Natick, MA). RESULTS

Effects of dopamine and other catecholamines. The effects of various concentrations of dopamine on CAMP levels in OK cells in the presence and absence of 50 PM 3-isobutyl-l-methylxanthine (IBMX), a phosphodiesterase inhibitor, are shown in Fig. 1. In the presence of IBMX, CAMP production was slightly but significantly increased at 10B8 M dopamine (P c 0.001). Half-maximal stimulation of CAMP formation (E&o) was found with 1.15 t 0.22 PM dopamine. At 10B5 M dopamine, a >20fold increase was observed from a basal value of 4.0 t 0.6 to 90.3 t 11.7 pmol/mg protein. In the absence of IBMX in the medium, 10m5M dopamine increased CAMP production about fourfold from a basal value of 3.10 t 0.03 to 11.3 t 1.8 pmol/mg protein. To maximize the dopamine effect, all subsequent experiments were done in the presence of IBMX.

AND CAMP PRODUCTION

DOPAMINE

(M)

Dose-response relationship between CAMP production and dopamine concentration. OK cells were incubated at 37°C with DMEM medium for 10 min in presence (filled circles) or absence of IBMX (open circles). Data represent means k SE of 6 experiments. FIG.

1.

In view of the structural similarity between dopamine, norepinephrine, and epinephrine, it is not surprising that dopamine also interacts with cy- and P-adrenergic receptors (15). To determine whether the effect of dopamine on CAMP formation was mediated in part through nondopamine receptors, the dose-dependent effects of isoproterenol, epinephrine, norepinephrine, dopamine, and serotonin on CAMP formation were compared (Fig. 2). With the exception of isoproterenol and serotonin, which had no effect on CAMP production at any concentration, epinephrine, norepinephrine, and dopamine stimulated CAMP formation in OK cells. Maximal stimulations by epinephrine and norepinephrine were less than that observed with dopamine. Epinephrine, norepinephrine, and dopamine stimulated CAMP formation 6-, lo-, and 23fold, respectively, at 10D4 M compared with basal value. These results suggested that dopamine-stimulated CAMP formation was not mediated through P-adrenergic receptors and that norepinephrine and epinephrine might act in part through dopamine receptors. Effect of dopamine and ,&adrenergic antagonists on norepinephrine-stimulated CAMP production. Norepi-

nephrine and epinephrine stimulated CAMP production in OK cells (Fig. 2). To test whether this increase resulted from norepinephrine and epinephrine interacting with dopamine receptors or ,&adrenergic receptors, the effects of Sch 23390 and L-propranolol on norepinephrine-stimulated CAMP formation were studied. As shown in Fig. 3, Sch 23390, a selective DAl-receptor antagonist, inhibited norepinephrine-stimulated CAMP production by ~40-60% at lo-’ M and 90% at lOa M with ICsO (concentration of antagonist that produces half-maximal inhibition) of 1.39 t 0.21 nM. L-Propanolol. a B-adrenereic

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DOPAMINEl

r

I

I

I

I

I

RECEPTOR

pamine as well as ,&adrenergic antagonists were tested (Fig. 4). Sch 23390, a selective DAl-receptor antagonist, and (+) -butaclamol, a nonselective DA-receptor antagonist, completely inhibited dopamine-stimulated CAMP production. Haloperidol, a nonselective DA-receptor antagonist, reduced the DA-stimulated CAMP production by 65%. Spiperone, a selective DAg-receptor antagonist, and propranolol, a ,&adrenergic antagonist, had no inhibitory effect. The attenuation of dopamine-stimulated CAMP production by Sch 23390, (+)-butaclamol, and haloperidol was dose dependent. As shown in Fig. 4, Sch 23390 inhibited dopamine-stimulated CAMP production by 40% at lo-' and 95% at low7M with an I& of 1.24 t 0.18nM. Butaclamol was lo-20 times less potent than Sch 23390 and haloperidol was three orders of magnitude less potent than Sch 23390. Table 1 lists the inhibition constants (Ki) and ICso for each antagonist. Effect of specific DA,-agonist SKF 82526J. To further confirm that the stimulatory effect of dopamine was mediated through DAl-receptors, the specific DAl-ago-

I

T

T

I

1o-8

0

1o-7

1o-6

lo+

CATECHOLAMINE

(M)

F879

AND CAMP PRODUCTION

I

I

I

--

I

80

1o-4

F.a 5 a F \ E

2. Effects of different catecholamines on CAMP formation. OK cells were incubated with increasing concentration of dopamine (filled circles), norepinephrine (open circles), epinephrine (filled triangles), isoproterenol (open squares), and serotonin (open triangles) for 10 min at 37°C. Data represent means t SE of 5 experiments. FIG.

s

60

40

4 o

20

ANTAGONIST(M) FIG. 4. Effects of antagonists on dopamine-stimulated CAMP production. OK cells were incubated with increasing concentration of Sch 23390 (filled circles), butaclamol (open circles), haloperidol (filled triangles), spiperone (open squares), and L-propranolol (open triangles) for 3 min, and then 10B5 M dopamine was added for a further 10 min. Data represent means ~frSE of 5-7 experiments. III’

0

’

’

’

’

TABLE 1. Ki and I&-, of various dopamine antagonists for effects on dopamine-, norepinephrine-, and SKF 82526J-stimulated CAMP formation

‘I

10-g10-810-710-~o-510-4

ANTAGONIST

(M)

FIG. 3. Effects of Sch 23390 and L-propranolol on norepinephrinestimulated CAMP formation. OK cells were incubated with different concentrations of Sch 23390 (filled circles) and L-propranolol (open circles) for 3 min, and then 10m5 M dopamine was added for a further 10 min. Data represent means rt SE of 5 experiments.

antagonist, had no inhibitory effect on norepinephrinestimulated effects at concentrations as high as 10m4 M. These data demonstrated that norepinephrine-stimulated CAMP production was mediated through dopamine receptors. Effect of dopamine and ,&adrenergic dopamine-stimulated CAMP production.

termine whether the stimulatory mediated by specific dopamine

antagonists

on

To further deeffect of dopamine was receptors, different do-

Agonist

Dopamine

Norepinephrine

Antagonist

Sch 23390 (+) -Butaclamol Haloperidol Sch 23390

IGO, nM 1.24tO.

18

23.80k5.69 3,340.0+611.7 1.39t0.21*

Kiy nM 0.12~0.02

2.3620.56 331.02t60.6

ND

SKF 825265 Sch 23390 4.0+0.5t ND Values are means t SE of 5-7 experiment.s. Cells were incubated with various concentrations of antagonists for 3 min and then 10B5 M dopamine, norepinephrine and SKF 825265 were added for a further 10 min, respectively. IC 50, concentration of antagonist that produces half-maximal inhibition; Ki, inhibition constant [calculated according to Cheng and Prusoff (7)]; ND, not determined. * Not significant compared with dopamine + Sch 23390. t P < 0.05 compared with dopamine + Sch 23390.

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F880

DOPAMINEl

RECEPTOR

AND

CAMP

PRODUCTION

nist, SKF 825265was tested in the presence of IBMX (Table 2). SKF 825265 increased CAMP formation but less than dopamine. Ly 171555, a potent DAB-receptor agonist, caused no significant increase in CAMP formation. The dose-dependent effects of antagonists Sch 23390 and spiperone on SKF 82526J-stimulated CAMP production are shown in Fig. 5. Sch 23390 inhibited SKF 82526J-stimulated CAMP production by 30% at lo-' M and >90% at 10m5M with an I& of 4.0 t 0.5 nM. In contrast, spiperone had no inhibitory effect. Propranolol also had no inhibitory effect (data not shown).

I

I

I

I

I

,o-7

,o-6

1o-5

100

Effect of serotonin on dopamine- and SKF 82526Jstimulated CAMP production. Recently, the 5-HT1 class

of serotonin receptors was identified in OK cells and linked to inhibition of PTH-stimulated CAMP production (31). Figure 6 shows the dose-dependent inhibitory effect of serotonin on dopamine-stimulated CAMP formation. Serotonin inhibited dopamine stimulation by -25% at 10m8 M and 60% at low5 M. In addition, Fig. 6 also shows that serotonin inhibited SKF 82526J-stimulated CAMP production. The maximum effect of serotonin was 50% attenuation of SKF 82526J-stimulated CAMP production.

20

P I

0

Effects of dopamine agonists and isoproterenol on adenylate cyhse actuity. In renal cortical membranes, dopa-

CAMP,

pmol/mg

Dopamine SKF 82526 Ly 171555 Basal

protein

I

I

Cells

I

I

-8

10

I

I

SEROTONIN

(M)

3. Effects of dopamine agonists on adenylate cyclase activity

TABLE

67.4t5.6 23.0t2.0 6.7kl.O 4.7kO.8

Values are means t SE of 7 experiments. different agonists (1 X 10B5 M) for 10 min.

I

FIG. 6. Inhibition of dopamineand SKF 82526-stimulated CAMP by serotonin. OK cells were incubated with serotonin for 3 min, and then 10B5 M dopamine (filled circles) or 10B5 M SKF 825265 (open circles) was added to medium for a further 10 min. Data represent means t SE of 4 experiments.

2. Effect of dopamine agonists on CAMP formation

TABLE

Agonist

..

IIII

Agonist

were

I

incubated

I

with

Adenylate Cyclase Activity, nmol mg protein-’ 30 min-l l

Dopamine SKF 82526 Isoproterenol Basal

4

Values determined

l

0.28t0.04 0.17t0.02 0.11t0.02 0.11t0.02

are means 2 SE of 4 experiments. Adenylate with 1 PM GTP presented in all assay tubes.

cyclase

was

mine increased adenylate cyclase activity -4O-100% (13). The activation of adenylate cyclase in crude membranes of OK cells by dopamine agonists and isoproterenol is shown in Table 3. Dopamine and SKF 825265 (10m5 M) stimulated adenylate cyclase -2.5- and l.&fold, respectively, compared with the basal value. In contrast, isoproterenol had no stimulatory effect. DISCUSSION

I

0

II II

I

l(yg

I

lo-*

I

I

I

1o-7

1o-6

IO-+

1

ANTAGONIST(M) 5. Inhibition of SKF 82526J-stimulated CAMP production by dopamine receptor antagonists. OK cells were incubated with Sch 23390 (filled circles) and spiperone (filled triangles) for 3 min, and then low5 M SKF 825265 was added for a further 10 min. Data represent means t SE of 4 experiments. FIG.

The present study has clearly demonstrated the existence of DA1-receptors that are associated with the stimulation of CAMP production and adenylate cyclase activity in the OK cell line. Kebabian and Calne (22) have subclassified dopamine receptors on the basis of their ability to alter CAMP content. Thus the DAl-receptor is associated with an agonist-induced increase in CAMP formation, whereas the DAz-receptor is not linked to stimulation in CAMP formation. At present, the OK cell is the only continuous cell line that expresses DA1-

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DOPAMINEl

RECEPTOR

receptors. In addition, OK cells have also been shown to possess the properties of renal proximal tubule (23, 24). Therefore the OK cell line may provide a useful experimental model to study functions and regulation of DA1receptor. Our results showed that dopamine stimulated CAMP formation and that Sch 23390, a specific DA1-receptor antagonist, abolished this stimulation. Spiperone, a selective DAz-receptor antagonist, did not inhibit dopamine-stimulated CAMP production. In addition, ,&adrenergic antagonists had no effect on dopamine-stimulated CAMP. These results demonstrated that dopamine stimulated CAMP formation by DA1-receptor activation and not by ,&adrenergic receptor activation. In support of these conclusions, we found that the DAl-receptor agonist, SKF 825265, but not DAz-receptor agonist, Ly 171555, stimulated CAMP formation. Furthermore, this stimulatory effect of SKF 825265 was inhibited by Sch 23390 but not by ,&adrenergic antagonists nor by a DA2receptor antagonist. These results provide additional confirmation of the existence of DA1-receptors linked to increase CAMP formation in OK cells. In the present study, epinephrine and norepinephrine also enhanced CAMP formation, although not as effectively as dopamine. The rank order of potency is dopamine > norepinephrine > epinephrine. The stimulatory effect of norepinephrine was inhibited completely by a DA1-receptor antagonist Sch 23390 and not at all by the ,&adrenergic blocker propranolol. Furthermore, isoproterenol could not stimulate CAMP production in OK cells. These results indicated that epinephrine and norepinephrine stimulated CAMP formation through its interactions with the DA1-receptor. In addition, this study also demonstrated that OK cells do not possess ,&adrenergic receptors related to CAMP production. The order of potency for antagonist inhibition of DAstimulated CAMP production was Sch 23390 > butaclamol >> haloperidol >>>> spiperone. These data clearly indicated a DA1-receptor profile (l&33). This result was similar to antagonist affinities for 3H-labeled Sch 23390 binding studies in bovine parathyroid glands and canine striatum (33). In addition, the Ki value (Table 1) for Sch 23390-inhibitable DA-stimulated CAMP in OK cells was at least 50-100 times lower than the Ki value observed in affinity binding analysis in rat renal cortical homogenates (14). Species differences might account for these observations. The specific DA1-receptor agonist, SKF 825265, increased CAMP formation in OK cells. These results were consistent with the finding that SKF 825265 stimulated adenylate cyclase in isolated rabbit proximal tubule (11). Our results showed that the stimulatory effect of SKF 825265 was less than dopamine. The reasons for the low potency of this ligand in the present studies are not clear. In cultured rat mesangial cells, SKF 825265 and dopamine had almost similar potency (34). In the dog mesenteric vascular bed the rank order of potency of dopamine agonists is SKF 825265 > dopamine >> SKF 38393, whereas in the rabbit splenic artery the rank order of potency is dopamine >>> SKF 38393 = SKF 82526 (18). These findings suggested that two subtypes of vascular

AND CAMP PRODUCTION

F881

DA1-receptors may exist (1, 18). Alternatively, it is possible that the vascular and tubular DA1-receptors are different. The direct role of dopamine on sodium reabsorption in the renal proximal tubule remains controversial. Dopamine has been known to mediate physiological effects by activating specific dopamine receptors (15, 22) or cyand ,&adrenergic receptors in kidney (15). It is also reported that a- and ,&adrenergic receptors as well as dopamine receptors are present in the proximal tubule (2). In the isolated proximal tubule, dopamine applied to the basolateral surface of the pars recta decreased sodium transport (3). In contrast, dopamine directly stimulated sodium uptake in renal proximal tubule cells (25). Therefore the effect of dopamine on sodium transport could be offset by the effects of stimulation of adrenergic receptors. Indeed, it has been reported that dopamine could stimulate and inhibit fluid reabsorption in the proximal tubule (3,17). The involvement of ,&adrenergic receptors was implied in a study where dopamine stimulated fluid reabsorption (17). In the present study, we found that OK cells do not possess ,&adrenergic receptors linked to adenylate cyclase activity. Therefore OK cells may prove to be a useful model to study the regulation of sodium transport and other transport processes by DA1-receptors. Further studies are required to evaluate whether these effects are through the change in CAMP level by DA1-receptor as seen in this study or through the change in phospholipase C activity (9, 10). In conclusion, the present study has demonstrated for the first time that OK cell line with properties of renal proximal tubule possesses a DA1-receptor that is coupled to the adenylate cyclase system. The authors thank Drs. J. L. Kinsella and C. Filburn for their critical reviews and suggestions. The excellent secretarial assistance of M. J. Ricewick in the preparation of this manuscript is gratefully acknowledged. Address for correspondence: L. Cheng, Laboratory of Biological Chemistry, Gerontology Research Center, NIA/NIH, 4940 Eastern Ave., Baltimore, MD 21224. Received 12 May 1989; accepted in final form 7 November 1989. REFERENCES 1. ALKADHI, K. LOKHANDWALA.

A., M. H. SABOUNI, A. F. ANSARI, AND M. F. Activation of DA1 receptors by dopamine or fenoldopam increases cyclic AMP levels in the renal artery but not in the superior cervical ganglion of the rat. J. Pharmacol. Exp. Ther.

238: 547~553,1986. 2. BELLO-REUSS,

E. Effect of catecholamines on fluid reabsorption by the isolated proximal convoluted tubule. Am. J. Physiol. 238 (Renal Fluid Electrolyte Physiol. 7): F347-F352, 1980. 3. BELLO-REUSS, E., Y. HIGASHI, AND Y. KANEDA. Dopamine decreases fluid reabsorption in straight portions of rabbit proximal tubule. Am. J. Physiol. 242 (Renal Fluid Electrolyte Physiol. 11): F634-F640,1982. 4. CAVERZASIO, J., R. RIZZOLI, AND J. P. BONJOUR. Sodium-dependent phosphate transport inhibited by parathyroid hormone and cyclic AMP stimulation in an opossum kidney cell line. J. Biol. Chem. 261: 3233-3237,1986. 5. CHENG, L., C. T. LIANG,

P. PRECHT, AND B. SACKTOR. an-Adrenergic modulation of the parathyroid hormone-inhibition of phosphate uptake in OK cells. Biochem. Biophys. Res. Commun. 155:

74-82,1988. 6. CHENG, L.,

P. PRECHT, C. T. LIANG, D. FRANK, AND B. SACKTOR. Dopamine stimulation of CAMP production in cultured OK cells

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(Abstract). Kidney Int. 35: 153, 1989. 7. CHENG, Y. C., AND W. H. PRUSOFF. Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50 per cent inhibition (I& of an enzymatic reaction. Biochem. PharmacoZ. 22: 3099-31081973. 8. COLE, J. A., S. L. EBER, R. E. POELLING, P. K. THORNE, AND L. R. FORTE. A dual mechanism for regulation of kidney phosphate transport by parathyroid hormone. Am. J. Physiol. 253 (Endocrinol. Metab. 16): E221-E227, 1987. 9. FELDER, C. C., M. BLECHER, AND P. A. JOSE. Dopamine-l-mediated stimulation of phospholipase C activity in rat renal cortical membranes. J. Biol. Chem. 264: 8739-8745,1989. 10. FELDER, C. C., A. M. MCKELVEY, M. S. GITLER, G. M. EISNER, AND P. A. JOSE. Dopamine receptor subtypes in renal brush border and basolateral membranes. Kidney Int. 36: 183-193, 1989. 11. FELDER, R. A., M. BLECHER, P. L. CALCAGNO, AND P. A. JOSE. Dopamine receptors in the proximal tubule of the rabbit. Am. J. PhysioZ. 247 (Renal Fluid Electrolyte Physiol. 16): F499-F505,1984. 12. FELDER, R. A., M. BLECHER, G. M. EISNER, AND P. A. JOSE. Cortical tubular and glomerular dopamine receptors in the rat kidney. Am. J. Physiol. 246 (Renal Fluid Electrolyte Physiol. 15): F557-F568,1984. 13. FELDER, R. A., C. C. FELDER, G. M. EISNER, AND P. A. JOSE. The dopamine receptor in adult and maturing kidney. Am. J. Physiol. 257 (Renal Fluid Electrolyte Physiol. 26): F315-F327, 1989. 14. FELDER, R. A., AND P. A. JOSE. Dopaminel receptors in rat kidneys identified with 1251-Sch 23982. Am. J. Physiol. 255 (Renal Fluid Electrolyte Physiol. 24): F970-F976, 1988. 15. GOLDBERG, L. I. Cardiovascular and renal actions of dopamine potential clinical applications. Phurmucol. Rev. 24: l-29, 1972. 16. GOLDBERG, L. I., AND J. D. KOHLI. Peripheral dopamine receptors: a classification based on potency series and specific antagonism. Trends Phurmucol Sci. 4: 64-66, 1983. 17. GREVEN, J., AND H. KLEIN. Effects of dopamine on whole kidney function and proximal transtubular volume fluxes in the rat. Nuunyn-Schmiedebergs Arch. Phurmucol. 296: 289-292,1977. 18. HILDITCH, A., AND G. M. DREW. Peripheral dopamine receptor subtypes. Trends Phurmucol. Sci. 6: 396-400,1985. 19. HUO, T., AND D. P. HEALY. Autoradiographic localization of dopamine DA1 receptors in rat kidney with [3H]Sch 23390. Am. J. Physiol. 257 (Renal Fluid Electrolyte Physiol. 26): F414-F423,1989. 20. INSEL, P. A., AND M. D. SNAVELY. Catecholamines and the kidney: receptors and renal function. Annu. Rev. Physiol. 43: 625-636, 1981. 21. JOSE, P. A., R. A. FELDER, J. E. ROBILLARD, C. G. FELDER, AND G. M. EISNER. Dopamine-2 receptor in the canine kidney (Ab-

AND

CAMP

PRODUCTION

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