Desmosomes are disc-like structures of 0.1–0.5 
m in diameter and are located principally in epithelial cells where they play a major role in cell-cell adhesion as well as cell communication (Garrod, 1993;Kouklis et al, 1994;Garrod, 1996;Green and Jones, 1996). Viewed under standard transmission electron microscopy desmosomes present with a distinctive ultrastructure consisting of two major domains. The first, termed the extracellular core domain or "desmoglea", is approximately 30 nm in width and is separated by an electron-dense mid line region. This extracellular core domain consists of the extracellular heads of the desmosomal cadherins that provide cellular adhesion to neighboring cells (North et al, 1999). The second domain consists of an electron-dense cytoplasmic plaque that can be further separated into an outer dense plaque and an inner dense plaque, which are separated from one another by an electron lucent zone. The cytoplasmic plaque is composed of the desmosomal plaque proteins desmoplakin, plakoglobin, the plakophilins and the amino terminal domains of the intermediate filament proteins. Early studies on desmosomes identified a group of glycoproteins and evidence suggested that they mediated the specific recognition and adhesion functions of desmosomes (Cohen et al, 1983). With the resulting isolation and characterization of these glycoproteins it was demonstrated that they were related to the calcium dependent class of single pass transmembrane cell adhesion molecules, the cadherins (Nilles et al, 1991) and were subsequently named "desmosomal cadherins".
Similar to the classical cadherins, the desmosomal cadherins possess five homologous extracellular domains containing putative calcium-binding sites, a single transmembrane spanning domain, and a carboxy-terminal cytoplasmic tail (Wheeler et al, 1991). The cytoplasmic tails of the desmogleins and desmocollins contain many motifs including an intracellular anchor domain (IA), an intracellular cadherin-typical segment (ICS) and a major binding site that contributes to the binding of the desmosomal plaque protein, plakoglobin (Schmidt et al, 1994). The desmocollins exist in "a" and "b" isoforms, the shorter "b" isoform lacking the major binding site that eliminates its ability to bind plakoglobin (Troyanovsky et al, 1993;Troyanovsky et al, 1994a;Troyanovsky et al, 1994b). In addition, molecules in the desmoglein subgroup contain a unique carboxy-terminal extension containing a "repeat unit domain" (RUD) that comprises a repeating motif of approximately 29 amino acids (Koch et al, 1990;Wheeler et al, 1991) that is predicted to form 
-strands. In order to avoid confusion the nomenclature was simplified by renaming the human proteins such that there were six desmocollins (i.e., 1a, 1b, 2a, 2b, 3a, and 3b), and three desmogleins (i.e., 1, 2, and 3) (Buxton et al, 1993).
The largest desmosomal cadherins are desmocollin 2 and desmoglein 2; they are the essential desmosomal cadherins common to all desmosome-possessing tissues, including simple epithelia, myocardium and many cell cultures (Koch et al, 1992;Theis et al, 1993;Schmidt et al, 1994). In contrast, the epidermal isoforms desmocollins 1 and 3, and desmogleins 1 and 3 are restricted to specialized epithelia, mostly stratified squamous ones (Koch et al, 1992;Schafer et al, 1994;Schmidt et al, 1994;Schafer et al, 1996). Within the epidermis the three desmocollin/glein isoforms are expressed in a differentiation-specific manner, with desmocollin 2 and desmoglein 2 being basal, desmoglein 3 and desmocollin 3 being basal layer and first suprabasal layer, and desmoglein 1 and desmocollin 1 being upper spinous and granular layer of epidermis (Arnemann et al, 1993;King et al, 1993;Theis et al, 1993;Schmidt et al, 1994;King et al, 1995;Nuber et al, 1995;Yue et al, 1995;Adams et al, 1998;Denning et al, 1998). In addition to its role in cell adhesion in deep stratified squamous epithelia, desmoglein 3 is also critical in anchoring the telogen hair to the outer root sheath of the hair follicle and thus demonstrates that desmosomes are important in maintaining the normal structure and function of the hair (Koch et al, 1998).
The human desmoglein genes comprise either 15 or 16 exons (Silos et al, 1996;Frank et al, 2001;Hunt et al, 2001) that are clustered within a region of approximately 150 kb in the order 5'-DSG1-DSG3-DSG2-3' (Simrak et al, 1995). The human desmocollin genes comprise 17 exons (Whittock et al, 2000b;Cserhalmi-Friedman et al, 2001), where exon 16 is alternatively spliced, giving rise to the "a" and "b" forms of the protein (Collins et al, 1991;Greenwood et al, 1997). However, the genomic organization of the desmocollin genes is closer to that of the classical cadherins than the desmogleins (Greenwood et al, 1997). The entire DSC/DSG gene complex occupies approximately 700 kb on 18q12.1, and the genes are arranged in the order cen-3'-DSC3-DSC2-DSC1-5'-5'-DSG1-DSG3-DSG2-3'tel, where the two gene clusters are transcribed outward from the interlocus region (Arnemann et al, 1991;King et al, 1993;Cowley et al, 1997;Hunt et al, 1999).
Desmosome integrity is critical for normal cell-cell adhesion. This is clearly highlighted in a group of disorders whereby defects occur within desmosomal proteins that lead to the loss of this adhesion. The genetic diseases of desmosomes cover a range of disorders that can be inherited in autosomal dominant or recessive modes and that can range from affecting just palmoplantar skin to those that affect skin, hair and heart and can lead to death during the second or third decade of life. In addition, desmosomal proteins are targets for the autoimmune diseases pemphigus vulgaris, pemphigus foliaceous and paraneoplastic pemphigus, as well as substrates in staphylococcal scalded skin syndrome (SSSS).
Here we present the identification of an additional human desmoglein which we term desmoglein 4 and demonstrate tissue specific expression. Based on gene structure and protein identity we show that desmoglein 4 is closely related to desmoglein 3.
Materials and Methods
Reverse transcription PCR (RT-PCR) and cDNA expression studies
Total RNA was extracted from normal skin biopsy using the Perfect RNA kit (Eppendorf AG, Cambridge, UK) according to manufacturer's instructions. RNA was reverse transcribed using random primers with the Thermo-script cDNA kit (Invitrogen Ltd, Paisley, UK) according to the manufacturer's instructions. Gene-specific primers used for overlapping RT-PCR of desmoglein 4 are available on request. Gene-specific intron crossing primers were designed for use in RT-PCR based cDNA expression studies to exclude amplification of genomic DNA. Primers used for desmoglein 4 were cDNA4F (forward-situated in exon 4) 5'-GTA GGG ATT GAT CGA CCA CC-3' and cDNA7R (reverse-situated in exon 7) 5'-CTTGATTCTACAGTCACACTC-3' to yield a 507-bp product. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was amplified using the primers 5'-TGA AGG TCG GAG TCA ACG GAT TTG GT-3' (forward) and 5'-CAT GTG GGC CAT GAG GTC CAC CAC-3' (reverse). PCR was performed in a 50-L reaction mixture containing 20 pmol forward and reverse primers, 10 nmol each of dTTP, dCTP and dATP, 7.6 nmol dGTP, 2.5 nmol deaza GTP, 2.5 L DMSO, 50 mol betaine, 10 mM Tris–HCl, 50 mM KCl, 1.5 mM MgCl2 and 1.0 U Amplitaq Gold Taq polymerase (Applied Biosystems, Warrington, UK). After an initial denaturation of 95°C for 12 min, 40 cycles were performed of 95°C for 1 min, 55°C for 1 min, and 72°C for 2 min, with a final extension step of 72°C for 10 min. The PCR products were examined by 1.5% agarose gel electrophoresis, purified using spin columns (Qiagen, Crawley, England) and directly sequenced using Big Dye terminators on an ABI 377 genetic analyzer (Applied Biosystems) and analyzed using Sequence Navigator 1.0.1. software (Applied Biosystems). To determine the expression of desmoglein 4 a multiple tissue RNA panel II (adult) (BD Clontech, Basingstoke, UK) was reverse transcribed and amplified as described above.
RACE PCR
The 5' and 3' ends of the desmoglein 4 cDNA were isolated from skin and testis total RNA using the Smart Race amplification kit (BD Clontech) according to the manufacturer's instructions. Primers used to amplify the 5' and 3' ends of desmoglein 4 were EX1B RACE 5'-CTG AAG AAG AGC CAA TCC ATT CCT TTG GG-3', and 3UTRRACEA 5'-GCA TCC CTT GAT ACT GTC TAA CGA ATA GC-3'. RACE PCR was performed using the Advantage II PCR kit (BD Clontech) according to the manufacturer's instructions, and PCR products were purified and sequenced as above.
Results
Sequence analysis reveals a novel human desmosomal cadherin
Analysis of the annotated human genome data (http://www.genome.ucsc.edu) for chromosome 18 demonstrated several predicted genes in the 100 kb gap between DSG1 and DSG3 using various algorithms. These included ENST00000308128 (Ensembl), chr18.29.005.a and chr18.30.001.a (Twinscan), and NT_010966.11 (Genescan). All of these predicted genes demonstrated varying levels of homology with the known desmoglein genes, DSG1-3. In addition, the predicted mRNA's and proteins showed a high level of homology to desmogleins 1–3. However, it was clear based on exon size conservation with other DSG genes and amino acid sequence that the gene prediction algorithms had incorrectly identified several exons and most importantly had not correctly identified exon 1 and its associated promoter. In order to locate exon 1, five regions containing high homology with the syntenic mouse region were identified as HumMus.18.14374, 14379, 14381, 14382, and 14383. Sequence analysis of HumMus.18.14374, 14379, 14382, and 14383 revealed no potential first exon; however, analysis of HumMus.18.14381 revealed a region predicted to encode 16 amino acid residues with high homology to desmoglein 1 followed by a donor splice site. To determine whether these predicted genes were indeed expressed in skin and to confirm the correct exons, overlapping RT-PCR was used on skin biopsy total RNA from nonlesional skin. Sequence analysis of the desmoglein 4 cDNA indicated a transcript of at least 3.6 kb containing an open reading frame of 3120 bp (Figure 1). Exon/intron organization revealed that the new gene, DSG4, comprised 16 exons spanning approximately 37 kb of human chromosome 18 with the entire desmoglein gene complex spanning approximately 250 kb of 18q12 (Figure 2). The exons varied from 36 bp (exon 2) to 765 bp coding (exon 16) in size, and the introns varied from 8176 bp (intron 1), to 153 bp (intron 13) in size (Table 1). By gene structure alone DSG4 is more closely related to DSG3 as they both consist of 16 exons whereas DSG1 and DSG2 comprise 15 exons (Table 2). In addition, the sizes of exons for DSG3 and DSG4 are the same for exons 1, 2, 3, 4, 5, 6, 8, 9, 10, 13 and 14, demonstrating a high level of conservation (Table 2).
Figure 1.
Nucleotide and predicted amino acid sequence of human desmoglein 4. Horizontal arrows under the amino acid sequence show the beginning of each domain. The putative signal sequence is double striked. The presumed recognition site for proteolytic cleavage (RRQKR) is single striked. The RAL sequence, which corresponds to the HAV sequence of typical cadherins is underlined and boxed. Putative calcium binding sites (DXNDN and A/VXDXD) are bold and underlined. The transmembrane domain is underlined. The related NVXVTE repeats in the repeat unit domain are bold and double-underlined. Potential N-glycosylation sites are boxed. The translation initiation codon (ATG) is at nucleotide position 1, and the predicted translation termination codon (TAA) is marked with an asterisk (*). EC-extracellular domain, EA- extracellular anchor domain, TM-transmembrane domain, IA-intracellular anchor domain, ICS-intracellular cadherin-typical segment domain, LD-linker domain, RUD-repeat unit domain, TD-terminal domain.
Full figure and legend (144K)Figure 2.
Predicted gene and protein details of human desmoglein 4. (a) Schematic representation of the human desmoglein complex. DSG4 lies between DSG1 and DSG3 with the entire desmoglein complex occupying approximately 250 kb (b) Genomic organization of the human DSG4. Exons are represented by vertical boxes, introns by horizontal lines. The gene consists of 16 exons, spanning approximately 37 kb of genomic DNA. The size of the individual exons and introns are presented in Table 1. (c) The encoded protein, desmoglein 4, comprises a signal (S) and preprotein (p) domain followed by 5 extracellular domains (EC1-4, EA), a transmembrane domain (TM), an intracellular anchor domain (IA), an intracellular cadherin-typical segment domain (ICS), a linker domain (LD), a repeat unit domain (RUD) containing two repeats, and a terminal domain (TD).
Full figure and legend (26K)
Analysis of the deduced amino acid sequence of human desmoglein 4 and comparison with the desmoglein family
The 3120 bp open reading frame of the human desmoglein 4 cDNA encodes a precursor protein of 1040 residues with a predicted molecular weight of 113812 Da and isoelectric point of 4.42 (Figure 1). This precursor comprises a 21 amino acid signal sequence followed by a 28 amino acid prosequence that includes a NXS/T glycosylation site and ends in a basic putative proteolysis sequence RRQKR. Cleavage at this sequence would result in a mature desmoglein 4 unglycosylated peptide of 991 amino acids with a molecular mass of 107822 Da and a pI of 4.38. The extracellular region of desmoglein 4 (578 amino acids), by homology with other desmogleins is divided into four domains of about equal size, EC1 to EC4 that have homology with each other, followed by an extracellular anchor domain (EA). The highly conserved sequence HAV of typical cadherins, which is thought to be involved in cell adhesion, is represented in desmoglein 4 by the conservatively substituted sequence RAL. Other conserved sequences in the extracellular domains of desmoglein 4 and other desmogleins with potential function include putative calcium binding motifs (DXNDN and A/VXDXD). In addition, there are two further potential N-glycosylation sites (NXS/T) in the extracellular domain of desmoglein 4, in EC1 that is conserved in the equivalent positions of desmogleins 1–3, and in EA that is conserved only in desmoglein 3. The extracellular domain is followed by a 25 amino acid predicted transmembrane domain. The cytoplasmic domain of desmoglein 4 (388 amino acids) comprises an intracellular anchor domain (IA), an intracellular cadherin-typical segment (ICS), an intracellular linker domain (LD), a repeat unit domain (RUD) and a terminal domain (TD). The RUD domain contains one NVXVTE repeat and a highly related NVIYAE predicting two repeats as found in desmoglein 3. The overall protein identity of desmoglein 4 with human desmoglein 1 (Nilles et al, 1991;Wheeler et al, 1991) is 41%, with human desmoglein 2 (Koch et al, 1991;Arnemann et al, 1992) is 37%, and human desmoglein 3 (Amagai et al, 1991) is 50% (Table 3) (Figure 3). We therefore conclude that desmoglein 4 is a member of the cadherin family and that it is more closely related to the desmogleins than the typical cadherins. Comparison of the individual regions for desmoglein 4 with desmoglein 1, desmoglein 2 and desmoglein 3 demonstrates that desmoglein 4 is more identical to desmoglein 1 over the extracellular domain whereas it is more identical with desmoglein 3 over the intracellular domain (Table 3).
Figure 3.
Multiple amino acid sequence alignment of human desmogleins 1–4. Horizontal arrows above the amino acid sequence show the beginning of each domain. Desmoglein 1 (Nilles et al, 1991), desmoglein 2 (Koch et al, 1991), and desmoglein 3 (Amagai et al, 1991) are from published sequences. Conserved amino acids are represented by asterisks (*) under the sequence. For abbreviations see Figure 1 legend.
Full figure and legend (104K)RT-PCR on multiple tissue panel reveals tissue specific expression
To determine whether the desmoglein 4 transcript is expressed in other human tissues in addition to skin we examined its tissue-specific expression profile using RT-PCR on a cDNA panel derived from several adult tissues. The gene was highly expressed in testis, prostate, and skin, but was less abundant in salivary gland (Figure 4). No expression was detected in thymus, uterus, skeletal muscle, thyroid, trachea, spleen, liver, lung, placenta, fetal brain, heart, adrenal gland, bone marrow, cerebellum, whole brain, or kidney.
Figure 4.
Tissue specific expression of human desmoglein 4. Intron crossing primers for desmoglein 4 and GAPDH (control – not shown) were used to amplify cDNA from a multiple adult human tissue panel (BD Clontech). Specific expression of desmoglein 4 was observed in salivary gland, testis, prostate, and skin. The negative control consisted of no cDNA.
Full figure and legend (43K)GenBank accession number
Human desmoglein 4 genomic DNA and desmoglein 4 cDNA sequences have been deposited in the GenBank sequence database under Accession Nos AY177663 and AY177664, respectively.
Discussion
Desmosomes are essential adhesion structures in most epithelia and consist of a specific subset of proteins necessary to attach the intermediate filament network of one cell to the intermediate filament network of a neighboring cell, thus forming a strong connection.
The amino-terminal domains of both the desmocollins and desmogleins comprise the extracellular core domain of the desmosome (North et al, 1999). However, the carboxy-terminal domains of the desmosomal cadherins protrude into the outer dense plaque at varying distances due to their different lengths. The carboxy-terminal domains of the desmogleins reach at least the inner edge of the outer dense plaque approximately 20 nm from the plasma membrane and may even reach into the inner dense plaque. Within the desmosome the cytoplasmic tail of the desmogleins bind the 'arm' repeat domain of plakoglobin (Troyanovsky et al, 1993;Mathur et al, 1994;Troyanovsky et al, 1994a;Troyanovsky et al, 1994b). Specifically, "arm" repeats 1–3 and perhaps repeat 4 are required for binding of desmoglein (Kapprell et al, 1988;Ozawa et al, 1995;Troyanovsky et al, 1996;Wahl et al, 1996;Witcher et al, 1996;Andl and Stanley, 2001). The stoichiometry of binding between the desmosomal cadherins and plakoglobin has been extensively studied. Initial reports indicated that the cytoplasmic tail of desmocollins could bind one molecule of plakoglobin only, whereas the cytoplasmic tail of desmogleins could bind 6–7 plakoglobin molecules (Kowalczyk et al, 1996;Witcher et al, 1996). A recent study, however, has demonstrated that the desmogleins bind no more than 2 plakoglobin molecules (Bannon et al, 2001). Indeed it was demonstrated that desmogleins 2 and 3 bound only one molecule of plakoglobin, where as the differentiation specific isoform, desmoglein 1, bound 2 molecules of plakoglobin. The authors suggest that the isoform specific binding of plakoglobin may exert control over processes related to differentiation, junctional assembly and homeostasis in epithelia (Bannon et al, 2001).
The requirement for functionally intact desmosomes has been demonstrated with the characterization of a significant group of inherited disorders caused by mutations in the genes of the desmosomal proteins. These disorders include the genetically heterogeneous autosomal dominant condition, striate palmoplantar keratoderma, that can be caused by mutations in the desmosomal cadherin, desmoglein 1, the constitutive desmosomal plaque member desmoplakin, or the type II epidermal keratin, keratin 1 (Armstrong et al, 1999;Rickman et al, 1999;Whittock et al, 1999;Hunt et al, 2001;Kljuic et al, 2003;Whittock et al, 2002a). Mutations in the desmosomal plaque member plakophilin 1 can result in an autosomal recessive condition characterized by ectodermal dysplasia and skin fragility (McGrath et al, 1997;McGrath et al, 1999;Whittock et al, 2000a;Hamada et al, 2002), and more recently, mutations in plakoglobin and desmoplakin have been shown to underlie a group of autosomal recessive conditions involving skin, hair and heart (McKoy et al, 2000;Norgett et al, 2000;Whittock et al, 2002b).
Indeed, the involvement of desmosomal proteins in human disease does not end with inherited disorders, as desmoglein 1, desmoglein 3, and desmoplakin are targets for the autoimmune blistering diseases pemphigus foliaceous, pemphigus vulgaris, and paraneoplastic pemphigus (Stanley et al, 1984;Labib et al, 1990;Amagai et al, 1991;Oursler et al, 1992;Joly et al, 1994;Olague-Alcala et al, 1994;Emery et al, 1995;Lin et al, 1997a;Lin et al, 1997b;Allen and Camisa, 2000;Lin et al, 2000). The extracellular domain of desmoglein 1 is also the target of exfoliative toxins ETA and ETB from Staphylococcal aureus that cause the generalized skin blistering disease staphylococcal scalded skin dyndrome (SSSS) (Melish and Glasgow, 1970;Melish et al, 1972;Amagai et al, 2000;Amagai et al, 2002). It therefore follows that mutations in other undiscovered desmosomal proteins may underlie inherited disorders or themselves be targets for autoimmune blistering disease and microbial attack.
Using genetic analysis we have identified a novel human desmoglein gene, desmoglein 4, sharing significant homology with all cadherins, but most markedly with desmoglein 3. Like all other members of the cadherin family, desmoglein 4 has a putative signal sequence and a well-conserved sequence of basic amino acids that presumably serves as a signal for cleavage to a mature protein, followed by five extracellular domains, of which EC1, EC2, EC3, and EC4 show variable homology with each other. Like the typical cadherins, EA shows minimal or no significant homology with the other extracellular domains. Near the amino terminus of the mature protein, the area important for homophilic binding in typical cadherins, desmoglein 4 shows much greater identity to corresponding domains of desmoglein 1 than to those of desmogleins 2 and 3. Like desmoglein 1 and desmoglein 3, desmoglein 4 has an RAL site in EC1 that corresponds to the conserved HAV site in an equivalent position in typical cadherins. Desmoglein 4 also has several conserved putative calcium binding domains with all cadherins as well as several conserved N-glycosylation sites with desmoglein 1 and desmoglein 3. Amongst the desmoglein genes, the desmoglein 4 gene is most similar to desmoglein 3, as both comprise 16 exons.
Expression studies using RT-PCR on a human cDNA panel demonstrated weak expression of desmoglein 4 in salivary gland. It has previously been shown using RNA protection assays that only desmoglein 2, and not desmoglein 1 or desmoglein 3, is expressed in the salivary gland (Schmidt et al, 1994). As well as skin, the desmoglein 4 transcript is also highly expressed in testis and prostate gland. Comparative data for the other desmoglein isoforms is only available for prostate gland, which shows that only desmoglein 2 is expressed (Schmidt et al, 1994). The tissue specific transcript expression of desmoglein 4 in testis and prostate has added significance due to the fact that loss of heterozygosity (LOH) at 18q is found in both testicular and prostate cancers. The spectrum of genetic alterations in human cancer affect specific genes that play crucial roles in a varied range of cellular processes such as cell adhesion, signal transduction, development, DNA-repair and differentiation. Testicular germ cell tumors (TGCT) are probably the most prevalent type of tumor among adolescent and young adult males. Suggestive linkage between disease and genetic markers has been reported for several chromosomes including loss of genetic material at 18q12-ter (al-Jehani et al, 1995;Lothe et al, 1995;Ottesen et al, 1997;Looijenga et al, 2000;Skotheim et al, 2001). Prostatic carcinoma is the most common form of male cancer found in the Western world and LOH has been found for at least two locations on 18q12-21 (Bostwick et al, 1998;Verma et al, 1999;Padalecki et al, 2000;Chu et al, 2001;Yin et al, 2001). The role of cell-cell adhesion molecules in cancer is well understood as mutations in E-cadherin underlie diffuse gastric cancers and lobular breast cancers (Berx et al, 1998), and in most cases, the mutations occur in combination with LOH of the wild-type allele. Loss of heterozygosity has also been reported at 18q12 in esophageal carcinomas as well as cancer of the head and neck (Papadimitrakopoulou et al, 1998;Karkera et al, 1999;Pack et al, 1999). It is therefore possible that mutations in desmoglein 4 in combination with LOH may underlie some forms of testicular or prostate cancer.
In summary, using genetic analysis of human genomic data we have identified a novel member of the human desmoglein gene family that demonstrates highest homology to desmoglein 3, and using RT-PCR demonstrate that the transcript and presumably its protein is expressed only in specific tissues. Further work is now required to confirm desmoglein 4 expression at the protein level and to identify in which cell layers desmoglein 4 is expressed. In addition, studies are required to determine whether some cases of inherited disorders of desmosomes such as striate palmoplantar keratoderma are caused by mutations in desmoglein 4, to see whether desmoglein 4 is a target antigen of autoantibodies in pemphigus vulgaris or pemphigus foliaceus, and to determine whether the extracellular domain of desmoglein 4 is cleaved by either or both exfoliative toxins A and B.
Electronic-database information
URLs for data in this article are as follows:
Online Mendelian Inheritance in Man (OMIM), http://www3.ncbi.nlm.nih.gov/Omim/
Human Genome Working Draft, http://www.genome.ucsc.edu/
The Protein Machine, http://www2.ebi.ac.uk/
Biology WorkBench 3.2, http://www.biowb.sdsc.edu/
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Acknowledgments
This work was funded by Action Research (Salary to NW). We also wish to thank the Royal Devon and Exeter Hospital.
