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Endocrinology Vol. 138, No. 3 1282-1288
Copyright © 1997 by The Endocrine Society

Articles

Localization of Dopamine D1A Receptor Protein and Messenger Ribonucleic Acid in Rat Adrenal Cortex1

Anna M. Aherne, Carl J. Vaughan, Robert M. Carey and Damian P. O’Connell

Department of Pharmacology and Therapeutics, University College Cork, Cork, Ireland; and the Department of Medicine, University of Virginia Health Sciences Center (R.M.C.), Charlottesville, Virginia 22908

Address all correspondence and requests for reprints to: Dr. Damian P. O’Connell, Department of Pharmacology and Therapeutics, Clinical Investigation Wing, Cork University Hospital, Cork, Ireland E-mail: damian{at}ucc.ie


   Abstract
Top
 Abstract
Introduction
 Materials and Methods
 Results
 Discussion
 References
 
Pharmacological, physiological, and autoradiographic studies have suggested the presence of dopamine receptors in the adrenal gland. Dopaminergic ligands have been shown to modulate adrenocortical aldosterone biosynthesis and secretion as well as adrenomedullary catecholamine production and release. Using a combination of light microscopic immunochemistry and in situ amplification and hybridization, the present study sought to determine the site-specific expression of the recently cloned D1A receptor subtype in rat adrenal gland.

Light microscopic immunohistochemistry was conducted using polyclonal antisera raised to the putative rat D1A receptor. Immunoreactive product was detected using an avidin-biotin immunoperoxidase method. D1A receptor messenger RNA (mRNA) was detected using a transcription-based isothermal in situ amplification and hybridization approach using receptor-specific mRNA oligonucleotide probes. The amplified product was localized using an alkaline phosphatase 4-nitro blue tetrazolium chloride/5-bromo-4-chloro-3-indolyl-phosphate technique. This combined experimental approach, using both receptor subtype-selective antibodies and oligonucleotide probes, allows for the site-specific localization of the D1A receptor subtype, which would otherwise not be possible with the pharmacological methods currently available. The D1A receptor protein and mRNA were expressed solely in the zona glomerulosa of the rat adrenal gland, with no signal evident in any of the other cortical layers or in the medulla. Such a distribution raises the possibility that the D1A receptor subtype could modulate, at least in part, some of the known effects of dopamine on aldosterone secretion.


   Introduction
Top
 Abstract
 Introduction
Materials and Methods
 Results
 Discussion
 References
 
DOPAMINE (DA), first identified in the central nervous system, is a member of the family of compounds found in the brain that function as transmitters between nerve cells. DA influences many important physiological functions, including hormone synthesis, ion fluxes, and blood pressure (1). Classically DA receptors have been subdivided into two major subtypes within the central nervous system (D1 and D2) and in the periphery (DA1 and DA2). This classification was developed from pharmacological profiles and signal transduction mechanisms activated by the receptor subtypes (2, 3). More recently, this pharmacological classification has been confirmed by a molecular characterization through the use of recombinant DNA cloning that has revealed multiple DA receptor subtypes. The demonstration that these newly cloned receptors have the pharmacological and biochemical activities of the native receptor has been achieved through their expression in heterologous cell lines (4).

The presence of peripheral dopaminergic receptors has been described by many research groups, including our own, in such tissues as the kidney (5), the gastrointestinal tract (6), and the heart (7, 8). An extensive literature suggests the presence of DA receptors in the adrenal gland [reviewed by Missale et al. (9)], where it has been proposed that DA regulates adrenocortical aldosterone secretion (9) and adrenomedullary catecholamine release (10). With pharmacological and receptor-ligand binding methods using [3H]ADNT and [3H]SCH 23390 as D1-like receptor ligands, [3H]spiperone and [3H](-)sulpiride as D2-like receptor ligands, and [3H]DPAT and [3H]clozapine as D3- and D4-like receptor ligands, respectively, dopaminergic receptors have been identified in bovine, rat, and human adrenal glands (11, 12, 13). These studies are reviewed in detail by Missale (9). Functional studies have demonstrated that aldosterone secretion can be inhibited by dopaminergic agonists such as bromocriptine (14), whereas DA antagonists such as metoclopramide can stimulate secretion when used in in vivo studies in humans and experimental animals (15). Recent studies have indicated that adrenocortical DA is derived from the circulating precursor L-DOPA, rather than from free or conjugated plasma DA or by de novo synthesis from tyrosine (16). In this manner, the formation and action of DA may be analogous to that observed in the kidney, in which DA is synthesized from filtered L-DOPA, stored, and released to act on adjacent DA receptors localized in the renal vasculature, glomeruli, and tubule system (17). Based on the potential similarities of a paracrine/autocrine model of DA function in both the renal and adrenal cortex and given our recent demonstration that the kidney expresses the D1A receptor (5), we sought to determine whether the rat adrenal cortex also contains D1A-specific messenger RNA (mRNA) and receptor protein. As peripheral tissues, such as the kidney and adrenal gland, express receptor-specific mRNA in substantially lower quantities than are demonstrable in the brain, we employed a novel transcription-based amplification system to amplify in situ a unique portion of the rat D1A complementary DNA (cDNA), which was subsequently detected by nonradioactive in situ hybridization. The present experiments are, to our knowledge, the first to localize simultaneously a specific DA receptor protein and mRNA in the adrenal gland according to their recent molecular classification. We do not know of any other studies that have used both immunochemistry and in situ mRNA histochemistry to define the nature of adrenal DA receptors. These studies confirm previous work, using ligand-binding techniques, that has suggested the presence of a DA1-like receptor in the adrenal cortex (11) and support functional studies that have implicated a DA1-like receptor in the control of aldosterone secretion (18).


   Materials and Methods
Top
 Abstract
 Introduction
 Materials and Methods
Results
 Discussion
 References
 
Wistar-Kyoto rats, weighing between 250–500 g, were anesthetized by ip injection with sodium pentobarbital (50 mg/kg). Animals were obtained from a biological services unit attached to the department and were housed using conventional barrier methods at 14–21 C and 40–60% humidity with a 12-h light, 12-h dark cycle. The animals were fed a standard rat chow (Wm. Connolly and Sons, Red Mills, Kilkenny, Ireland) and allowed water ad libitum. The animals were perfused transcardially with a regimen of 0.9% saline, followed sequentially by 4% paraformaldehyde in 0.12 M phosphate buffer. After perfusion, the adrenal glands were removed, dissected free of any fat, postfixed in a 4% paraformaldehyde solution at 4 C, and thereafter cryoprotected overnight in 30% sucrose in 0.12 M phosphate buffer. All solutions were ribonuclease free. The adrenal gland was orientated on a cryostat chuck with the aid of OCT tissue embedding medium (Miles, Elkhart, IN) to permit sectioning of representative cross-sections of both adrenal cortex and medulla and then placed in the cryostat (Microm HM 500 OM, MICROM Laborgeräte GmbH, Waldorf, Germany ) set at -28 C. Once frozen, adrenal sections were cut at 5–7 µm and mounted on poly-L-lysine-coated slides, allowed to air-dry for 15 min, and then stored at -70 C until processed for immunohistochemistry or in situ hybridization. Adjacent sections were used throughout these studies for comparison of immunohistochemical results with those obtained in the in situ hybridization studies. Within an experiment, all sections were run in triplicate. Full coronal sections of rat brain in the region of the corpus striatum were similarly processed to provide representative positive tissue control sections for the D1A receptor.

Light microscopic immunohistochemistry was conducted with affinity-purified polyclonal antisera that had been raised against the synthetic peptide sequences: 166KPTWPLDGNFTSLEDTEDDNC186,241CQTTAGNGNPVE252 and 299GSEETQPFC307 corresponding to epitopes located on the third intracellular and second and third extracellular loops, respectively, of the putative rat D1A receptor amino acid sequence (Fig. 1AGo). The chosen peptide sequences have no significant homology to other G protein-coupled receptors in the rat as verified by search of the Swiss Protein Database. The specificity of the antisera was verified by attenuation of the enzyme-linked immunosorbent assay response after preincubation of the antiserum with its immunization peptide and by the ability of the antiserum to recognize the native receptor expressed in a murine fibroblast (LTK-) cell line, stably transfected with the full-length cDNA of the rat D1A receptor (5). An immunoperoxidase immunohistochemical protocol that we have previously described (5) was employed thereafter, in which the adrenal sections were incubated with one of the different D1A antipeptide antisera as described above. Adrenal sections underwent two washes in Tris saline (0.05 M) and saponin (SAP; 0.001%; Sigma Chemical Co., Dorset, UK) for 5 min each. This was followed by a blocking step with 1% H2O2 in methanol for 45 min. The sections were washed in 1% normal goat serum (NGS; Sigma Chemical Co.) in TS-SAP before another blocking step, this time with 3% NGS in TS-SAP for 1 h. All sections were washed again, and the primary antibody was prepared. A number of concentrations of the D1A antibodies were used by dilution in TS buffer, and aliquots were added to the appropriate sections. As a control, similar dilutions of the preimmune serum were prepared and added to sections. All slides were incubated in a humid chamber at 4 C overnight. The following day, a number of wash steps with 1% NGS in TS-SAP were carried out before the addition of the biotinylated secondary antibody, which was left incubating for 45 min. The ABC avidin biotin solution (Vectastain ABC reagent, Vector Laboratories, Peterborough, UK) was made up and added to the sections, which then underwent a further 45-min incubation period. Diaminobenzidine (Sigma Chemical Co.) was prepared (0.1%) and applied to the sections. Finally, the adrenal sections were lightly counterstained with hematoxylin, dehydrated by passing through a graded series of ethanol dilutions, delipidated with xylene, and coverslipped in DPX (BDH Laboratory Supplies, Poole, UK).



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  		Figure 1. A, Putative rat D1A two dimensional receptor model showing epitopes to which antisera were raised, as indicated by the shaded areas. *, Third extracellular loop. B, Map of the D1A receptor cDNA depicting nontranslated (open box) and translated (hatched box) portions of the mRNA with the translation start site being denoted as +1. The annealing sites of forward and reverse primers used in the in situ amplification protocol are also indicated (for details refer to Materials and Methods). In addition, the oligonucleotide probe used in the in situ hybridization step can be seen to be complementary to a unique sequence within the amplified product.

 
The in situ amplification and hybridization was achieved by amplifying a 308-bp region of both 5' nontranslated as well as a portion of mRNA encoding the N-terminus of the D1A receptor (Fig. 1BGo), as previously described (7). The forward primer, containing a T7 promoter was 5'-GCAACTGGGGCTGAACAAGA-3', the reverse primer was 5'-CTAAAGAGATGACAAAGA-3'. The antisense probe directed to the amplified 308-bp sense product was 5'-AAAGGAGAAATCCCTCTCCGCTGG-3' (R&D Systems Europe, Oxford, UK). All primers and probes were designed using a computer-based biocomputing software package (Lasergene, DNASTAR, Madison, WI). Sequence similarity searches were conducted for the primers to confirm their specificity using the GENEMAN module of this software package and the GenBank nucleotide database. A mixture of 4 x SSC (standard saline citrate)-50% formamide (Sigma Chemical Co.), and the reverse primer at 1 ng/25 ml was placed on the adrenal sections. Unannealed primer was washed off. Sections then had added a solution containing deoxy (d)-NTP/rNTP mix at 5 and 1.5 mM, respectively (Promega, Southhampton, UK) reaction buffer, both forward and reverse primers at 1 ng/25 ml, diethylpyrocarbonate-treated water, and an enzyme mix containing AMV-RT (30 IU), T7 RNA polymerase (100 IU), and ribonuclease H (3 IU; Promega). Transcriptional amplification was allowed to proceed on the slides at 42 C for 2 h in an OmniSlide In Situ system (Hybaid Limited, Middlesex, UK).

In situ hybridization was conducted using 24-mer HPLC-purified antisense and sense probes complimentary to a D1A mRNA sequence lying within the amplified product coding for N-terminal amino acid residues. The oligonucleotides were labeled by tailing the 3'-end with digoxigenin-11-dUTP using terminal transferase (DIG Oligonucleotide 3' end-labeling kit, Boehringer Mannheim, East Sussex, UK). Prehybridization of both amplified and nonamplified tissue sections was carried out in a humid chamber at room temperature for 1 h. Thereafter, the hybridization solution, containing either the antisense or sense probe, was applied to the appropriate sections and incubated overnight at 37 C in the OmniSlide In Situ system. After hybridization, the tissue sections were washed in decreasing concentrations of SSC buffer, including a stringency wash of 0.5 x SSC at 37 C for 30 min. After the posthybridization washes, the sections were immersed in a series of different buffers, and tissue-bound alkaline phosphatase activity was detected by incubating the tissue sections in 4-nitro blue tetrazolium chloride/5-bromo-4-chloro-3-indolyl-phosphate (NBT/BCIP) color solution (Sigma Chemical Co.) for 2–24 h. The enzymatic reaction was stopped by rinsing the sections in PBS. Finally, the sections were counterstained with 0.2% neutral red and coverslipped as already described. In addition to the sense control, other slides had either no labeled oligonucleotide or no antidigoxigenin secondary antibody added, both of which served to control for nonspecific hybridization signal and background. All of these treatments resulted in the loss of the hybridization signal. Tissue areas for immuno- and in situ histochemistry were examined using a Leica DMR Photomicroscope at various magnifications (x100–1000). Photographs were made using color film (Fujichrome 100 ASA color film).


   Results
Top
 Abstract
 Introduction
 Materials and Methods
 Results
Discussion
 References
 
The antibodies used in the immunohistochemical studies were directed to epitopes located on the third intracellular and second and third extracellular loops of the rat D1A receptor. These peptide sequences were chosen because of predicted antigenicity and uniqueness in terms of sequence homology to other known receptors, especially the DA receptor subtypes. These polyclonal antibodies produced specific adrenal staining when incorporated in the avidin-biotin-peroxidase immunohistochemical procedure to identify the D1A receptor sites. The density of immunohistochemical staining varied with the antibody used. However, no regional variations in staining patterns were observed between antibodies, and for the purposes of clarity, the results obtained with antibody directed against the third extracellular loop, as denoted by the asterisk in Fig. 1AGo, are discussed.

Figure 2Go illustrates the results obtained for rat adrenal sections processed for light immunohistochemistry using the avidin-biotin peroxidase reaction to identify the D1A receptor sites. Positive staining is represented by the brown diaminobenzidine substrate reaction. Figure 2AGo indicates the presence of positive receptor protein in rat adrenal cortex. The staining pattern is confined to the zona glomerulosa. Figure 2BGo illustrates a higher magnification of zona glomerulosa staining. Figure 2CGo shows a high power magnification of positively stained glomerulosa cells. Figure 2DGo illustrates the preimmune serum control of a consecutive section at a similar magnification as Fig. 2AGo, showing absence of the signal. The specificity of the D1A receptor antiserum was verified by demonstration of immunostaining in rat brain sections known to contain D1A receptor protein. Figure 4AGo illustrates positive staining that was obtained in the rat brain cortex in an area rich in dopaminergic neurons expressing this DA receptor subtype.



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  		Figure 2. Light photomicrographs of rat adrenal sections processed for immunohistochemistry, demonstrating positive staining for the dopamine D1A receptor protein. A, Positive staining was noted in the adrenal cortex, but not in the adrenal medulla (magnification, x100). B, Higher magnification view (x400) of adrenal cortex, revealing immunostaining confined to the zona glomerulosa. C, High power view of individual cells within the zona glomerulosa demonstrating positive cytoplasmic immunostaining (magnification, x1000). D, Preimmune control shows the absence of immunostaining (magnification, x150).

 


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  		Figure 4. Light photomicrographs of rat brain control sections probed for D1A receptor protein and mRNA using immunohistochemistry and in situ hybridization. A, Positive neuronal staining in rat cortical tissue. B, Equivalent mRNA signal in an identical rat cortical region.

 
The antisense and sense oligonucleotide probes that were used in the in situ hybridization for the D1A receptor were specifically chosen because of their complementarity to a mRNA sequence lying within both the native and amplified mRNA products and their uniqueness in terms of sequence homology to known receptors or other mRNAs in the rat. Positive staining is represented by the blue/purple NBT/BCIP substrate reaction. Background labeling was minimal or nonexistent in all sections examined.

Sections processed for nonradioactive in situ hybridization for D1A mRNA revealed positive signal in the zona glomerulosa region of the adrenal cortex, (Fig. 3AGo). Those cells labeled with D1A antibodies by immunocytochemistry in consecutive sections also were shown to contain D1A mRNA (Fig. 3BGo). In addition, hybridization signal was absent from the other adrenocortical cell layers as well as from the medulla. Consecutive adrenal sections probed with sense oligonucleotide (Fig. 3CGo) or the absence of antidigoxigenin secondary antibody failed to reveal any hybridization signal. The specificity of the D1A mRNA hybridization in the adrenal sections was again verified by demonstration of positive hybridization signal in rat brain sections shown previously to express D1A receptor protein. Figure 4BGo illustrates the positive staining that was obtained in the rat brain neocortex in a region known to contain D1A receptor mRNA (4).



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  		Figure 3. Light photomicrographs of rat adrenal sections processed for in situ amplification and probed with a digoxigenin-dUTP-labeled antisense oligonucleotide. A positive hybridization signal was detected with an alkaline phosphatase-NBT/BCIP reaction as manifested by a purple substrate signal. A, Positive staining for mRNA in an adrenal section probed with the D1A antisense oligonucleotide (magnification, x400). B, Higher magnification (x1000) of individual cells within the zona glomerulosa, showing extensive cytoplasmic mRNA signal. C, Negative control adrenal section probed with the D1A sense oligonucleotide (magnification, x400).

 

   Discussion
Top
 Abstract
 Introduction
 Materials and Methods
 Results
 Discussion
References
 
This study characterized the site-specific localization of the D1A receptor subtype in the rat adrenal gland by means of both light microscopic immunochemistry and in situ hybridization. For the immunochemical studies, the antibodies used were raised against synthetic peptide sequences corresponding to unique epitopes located within the predicted rat D1A receptor protein amino acid sequence as derived from the published cDNA. These antibodies were designed to be D1A receptor subtype specific, and the sequences to which they are directed share no known homology to any other known receptor. The light immunohistochemical studies of adrenal sections revealed the presence of the D1A receptor protein in the cortical region of the gland; more specifically, in the zona glomerulosa layer. Sections processed for in situ amplification and hybridization confirmed and augmented the light microscopic results. The mRNA for the D1A receptor subtype also was located exclusively in the zona glomerulosa, with no digoxigenin signal evident in any of the remaining cortical layers or in the adrenal medulla.

The experimental approach adopted in this study is effective in defining the site-specific localization of the D1A receptor in the rat adrenal gland. Both immunohistochemistry and in situ amplification allow for the specific detection of a receptor subtype. Receptor protein and mRNA, respectively, are targeted by both antibodies and oligonucleotide probes directed exclusively to the receptor. Our laboratories have successfully employed this experimental approach to localize the D1A receptor in a number of peripheral tissues, including rat and human kidney, rat colon, and rat myocardium (5, 6, 7, 8). In addition, the use of receptor-specific antibodies in the localization of DA receptors has been successfully employed by other groups to define regional and cellular distribution patterns of such receptors (19, 20). In contrast, techniques such as autoradiography and radioligand binding can only identify the general receptor grouping, e.g. D1-like, because the ligands cannot target the DA receptor subtypes (D1A and D1B, specifically). Such general experimental approaches have previously identified the presence of DA1 and DA2 receptors in both the adrenal cortex and medulla (10, 11, 12, 13).

The zona glomerulosa has been shown to be the exclusive site within the adrenal gland for the synthesis and secretion of aldosterone (21). Aldosterone secretion can be influenced by circulating plasma potassium, ACTH, and angiotensin II levels, all of which play a stimulatory role (22). There is substantial evidence to suggest that DA also plays a role in the modulation of aldosterone secretion (9, 15, 22). Evidence that dopaminergic mechanisms might be involved in the control of aldosterone secretion came originally from in vivo studies in humans and animals using metoclopramide, a competitive DA antagonist in both the central nervous system and the periphery (23, 24). It is now well documented that administration of metoclopramide results in an increase in the plasma aldosterone concentration independent of changes in PRA and circulating sodium, potassium, and ACTH concentrations (9, 15). In addition, experimental evidence suggests that alterations in angiotensin-induced adrenocortical responsiveness with different sodium balance states may be related to dopaminergic modulation (25). The DA agonist, bromocriptine, has been shown to inhibit the aldosterone responses to acute diuresis and to the infusion of angiotensin II or ACTH (14, 26), but has no effect on basal aldosterone secretion (27). Ibopamine, an orally active DA agonist, inhibits aldosterone secretion and blunts the metoclopramide-induced release of this hormone (28).

The dopaminergic modulation of aldosterone secretion is due to a direct interaction of DA or dopaminergic ligands with the zona glomerulosa aldosterone-secreting mechanism (29). Moreover, this modulation is transduced by specific dopaminergic receptor activation. The transductional capability of DA receptors in rat adrenal glomerulosa homogenates has been analyzed with the measurement of cAMP formation in response to selective agonists (30). The results obtained suggested the presence of DA1 and DA2 receptors with opposing roles in the formation of cAMP in the adrenal glomerulosa. In addition, in vitro binding studies have demonstrated saturable, reversible, and stereospecific DA1 and DA2 binding sites in the adrenal cortex (11, 12, 13). Several studies have provided compelling evidence for a role for DA2 receptors in the inhibitory action of DA on aldosterone secretion (9). DA may act by decreasing the glomerulosa intracellular calcium concentration, as DA reduces angiotensin-stimulated calcium influx. It appears that the effect of angiotensin II on aldosterone secretion is calcium dependent, involving mobilization of both extracellular and intracellular calcium induced by direct receptor activation of phospholipase C (18). Studies also have shown that DA blocks voltage-dependent T-type calcium channels in cultured rat adrenal zona glomerulosa cells in a sustainable and reversible manner (31). Experiments on isolated rat zona glomerulosa cells have demonstrated that DA blocks angiotensin II-induced calcium influx and decreases inositol phosphate production (18, 32). Further studies in primary cultures of rat adrenal glomerulosa cells have demonstrated that DA can stimulate aldosterone secretion in conjunction with enhanced cAMP production and to have an additive effect on angiotensin-stimulated aldosterone secretion. These effects were DA1 receptor specific, in that they were completely suppressed by a specific DA1 antagonist and were unaffected by a ß-adrenergic antagonist (18). Further, this DA1 effect appeared to be calcium dependent, in that it could be blocked by calcium channel antagonists. These latter studies would suggest a more complex effect of DA on aldosterone secretion than previously suspected, with potential interactions between DA1 and DA2 receptor subtypes in an manner analogous to that observed for the effect of DA on the arachidonic cascade (33).

The results of the present experiments raise the possibility that the effects of DA may be mediated at least in part by the newly cloned D1A receptor. Support for this hypothesis comes from investigation of the signal transduction pathways of the human D1A receptor, which has demonstrated that this receptor can induce multiple cell-specific signals, including elevation of cAMP, cAMP-dependent activation and potentiation of the opening of voltage-dependent calcium channels, and a phosphatidyl inositol-linked mobilization of intracellular calcium (34, 35).

In summary, we have shown that the D1A receptor subtype is present in the zona glomerulosa of the rat adrenal cortex. The receptor protein was localized by light microscopic immunohistochemistry. The mRNA for the D1A receptor subtype was localized to the same region by means of the novel transcription-based amplification system, followed by in situ hybridization. We speculate that the D1A receptor subtype may modulate the previously described dopaminergic effects on aldosterone secretion from the adrenal cortex.


   Footnotes
 
1 This work was supported by grants from The Health Research Board of Ireland (to A.M.A., C.J.V., and D.P.O.). Back

Received June 14, 1996.


   References
Top
 Abstract
 Introduction
 Materials and Methods
 Results
 Discussion
 References
 

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