Conflict of interest: none declared. An 8‐year‐old girl was referred with multiple lesions; these had first been noticed by her mother on the left buttock approximately 6 years previously. The lesions were asymptomatic but had gradually increased in number and size since onset. The child had a history of asthma and atopic eczema. There were no reports of obstetric or developmental complications. Physical examination revealed multiple coalescing soft, nontender plaques over the left buttock extending to the natal cleft (Fig. 1). The surface of the lesions was a uniform, cream colour with no other epidermal changes noted. ... A 4‐mm punch biopsy was taken from one lesion (Fig. 2a,b). Histology revealed surface hyperkeratosis, focal parakeratosis and mild epidermal acanthosis. Hamartomatous deposits of adipose tissue with normal elastic fibres were noted within the dermis. ... What is your diagnosis? Naevus lipomatosus cutaneous superficialis. Naevus lipomatosus cutaneous superficialis (NLCS) was first reported by Hoffman and Zurhelle in 1921, when they described multiple soft, congenital lesions on the left buttock of a 25‐year‐old man.1 Presently it is classified as three clinical subtypes: multiple, solitary, and a rare generalized form.2

BACKGROUND:Although people seem to be well educated on the harmful effects of the sun, they continue to intentionally expose themselves without adequate protection.AIMS:To ascertain baseline knowledge regarding skin cancer and review the sun protection behaviours in an Irish population and the effect of doctor-based education on these behaviours.METHODS:Two hundred participants were recruited for a questionnaire-based study on their perceptions regarding skin cancer and their sun protection behaviour. They were divided into two groups, with one group receiving doctor-based education following the initial survey, and a follow-up questionnaire was carried out within 3 months.RESULTS:Ninety per cent of participants knew that sun exposure was the major risk factor for skin cancer, and 95% knew that sun beds were not a safe way to tan. Despite this, < 20% used regular sunscreen, and 30% had used or were currently using sun beds in order to tan.CONCLUSION:Our study indicated that although the participants' knowledge of skin cancer and risk of sun exposure is high, their sun-protective attitudes were not influenced by education in the clinical setting.

Journal Article An erythematous nodule on the sole of the foot Get access M. M. Malik, M. M. Malik Department of Dermatology, Our Lady of Lourdes Hospital, Drogheda, Ireland M. M. Malik, Department of Dermatology, Our Lady of Lourdes Hospital, Drogheda, Ireland. E‐mail: gallian75@hotmail.com Search for other works by this author on: Oxford Academic Google Scholar J. K. Wu, J. K. Wu Department of Dermatology, Our Lady of Lourdes Hospital, Drogheda, Ireland Search for other works by this author on: Oxford Academic Google Scholar C. A. Egan C. A. Egan Department of Dermatology, Our Lady of Lourdes Hospital, Drogheda, Ireland Search for other works by this author on: Oxford Academic Google Scholar Clinical and Experimental Dermatology, Volume 30, Issue 1, 1 January 2005, Pages 105–106, https://doi.org/10.1111/j.1365-2230.2004.01688.x Published: 01 January 2005 Article history Accepted: 04 June 2004 Published: 01 January 2005

IgA is present in the skin in several dermatoses, including dermatitis herpetiformis, linear IgA bullous dermatosis, and Henoch-Schoenlein purpura. The neutrophilic infiltration in the area of the IgA deposition suggests that IgA is responsible for the associated inflammatory events. The mechanism for this process is unproven, but is likely to involve IgA-mediated neutrophil chemotaxis with inhibition of chemotaxis by dapsone. Elucidation of the mechanism of IgA-mediated inflammation will require an animal model. We have established a model for linear IgA bullous dermatosis as a prototype disease to be studied. IgA mouse monoclonal antibodies against a linear IgA bullous dermatosis antigen have been passively transferred to SCID mice with human skin grafts. This has produced neutrophil infiltration and basement membrane vesiculation in 4 of 12 mice tested. We conclude that an animal model for the pathogenesis of IgA dermatoses with IgA deposition and inflammation can be produced by passive transfer of mouse IgA antibodies against a linear IgA antigen.

We report the clinical and immunopathologic findings in a cohort of 35 patients with anti-epiligrin cicatricial pemphigoid (AECP). These patients have a mucosal predominant subepithelial blistering disease that is clinically indistinguishable from other forms of cicatricial pemphigoid. The mucosal surfaces of the mouth and eye are most commonly involved. The skin is also involved in most patients, but usually this is less severe than mucosal involvement. AECP is characterized by the binding of circulating IgG autoantibodies to the dermal side of 1M NaCl split human skin on indirect immunofluorescence microscopy. These IgG antibasement membrane autoantibodies target laminin 5, a heterotrimeric protein consisting of alpha3, beta3, and gamma2 subunits. IgG autoantibodies predominantly target the G domain within the alpha subunit. The presence of circulating IgG autoantibodies are specific for the diagnosis of AECP and are not seen in patients with other autoimmune blistering diseases or normal volunteers. Furthermore, we expand on data previously reported on the finding of an increased relative risk for solid cancer in patients with AECP, especially in the first year after blister onset. The majority of cancers documented in a cohort of 35 patients assembled over 12 years of study were adenocarcinomas that were at an advanced stage at their time of detection. This circumstance is thought to account for a high incidence of mortality among AECP patients who develop an associated cancer. AECP patients also demonstrate a significant risk for mortality as a consequence of treatment with systemic immunosuppressives. The current longitudinal study suggests that only a minority of AECP patients go into remission.

Journal Article Case 3 Get access F. J. Moloney, F. J. Moloney Department of Dermatology, Beaumont Hospital, Dublin, Ireland F. J. Moloney, Clinical Research Centre, RCSI, Beaumont Hospital, Dublin 9, Ireland. E‐mail: fergalmoloney@eircom.net Search for other works by this author on: Oxford Academic Google Scholar C. A. Egan C. A. Egan Department of Dermatology, Beaumont Hospital, Dublin, Ireland Search for other works by this author on: Oxford Academic Google Scholar Clinical and Experimental Dermatology, Volume 28, Issue 6, 1 November 2003, Pages 685–686, https://doi.org/10.1046/j.1365-2230.2003.01407.x Published: 01 November 2003

Journal Article Mycosis fungoides presenting as annular erythema Get access D.S. Lim, D.S. Lim Department of Dermatology, Our Lady of Lourdes Hospital, Drogheda, Co Louth, Ireland Davin S.Lim. E‐mail: davinlim@hotmail.com Search for other works by this author on: Oxford Academic Google Scholar G.M. Murphy, G.M. Murphy Department of Dermatology, Beaumont Hospital, Dublin, Ireland Search for other works by this author on: Oxford Academic Google Scholar C.A. Egan C.A. Egan Department of Dermatology, Beaumont Hospital, Dublin, Ireland Search for other works by this author on: Oxford Academic Google Scholar British Journal of Dermatology, Volume 148, Issue 3, 1 March 2003, Page 591, https://doi.org/10.1046/j.1365-2133.2003.05063.x Published: 01 March 2003 Article history Accepted: 15 July 2002 Published: 01 March 2003

Anti-p200 pemphigoid is a recently defined subepidermal immunobullous disease. It is characterized by the binding of circulating IgG autoantibodies to the dermal side of 1 M NaCl split skin and by reactivity of these autoantibodies to a unique 200-kd antigen on immunoblot of dermal extract. On immunoelectron microscopic examination, these autoantibodies deposit at the lamina lucida-lamina densa interface. We describe the clinical, histologic, and immunopathologic features in a patient with anti-p200 pemphigoid, as well as his favorable response to treatment with systemic glucocorticosteroids and dapsone. (J Am Acad Dermatol 2002;46:786-9.)

Dermatitis herpetiformis is associated with a gluten-sensitive enteropathy in >85% of cases. Both the skin lesions and the enteropathy respond to gluten restriction. Linear IgA bullous dermatosis has a much lower prevalence of histological small bowel abnormalities, and lesions are not known to respond to gluten restriction. We report a patient with linear IgA bullous dermatosis and gluten-sensitive enteropathy. This report addresses the issue of whether linear IgA bullous dermatosis can be associated with gluten-sensitive enteropathy. We evaluated the response to gluten restriction and normal diet by following the status of the patient’s jejunal biopsies and skin lesions. The patient responded to gluten restriction, as shown by resolution of jejunal abnormalities and skin lesions and subsequently by recurrence of jejunal abnormalities and skin lesions with reinstitution of a gluten-containing diet. This report demonstrates that linear IgA bullous dermatosis can respond to gluten restriction if an underlying gluten-sensitive enteropathy is present.

The 180 kDa bullous pemphigoid antigen, BPAg2, is a transmembrane protein that is important in basement membrane cohesion. Circulating antibodies in bullous pemphigoid (BP) patients' sera have been shown to target epitopes that are tightly clustered in the sixteenth noncollagenous domain (NC16A) of the extracellular portion BPAg2 (Zillikens et al., 1997Zillikens D. Rose P.A. Balding S.D. et al.Tight clustering of extracellular BP180 epitopes recognized by bullous pemphigoid autoantibodies.J Invest Dermatol. 1997; 109: 573-579Crossref PubMed Scopus (266) Google Scholar). We have previously shown that some BP patients' sera contain IgG antibodies reactive with the LABD97 antigen which is structurally identical to a portion of the extracellular domain of BPAg2 (Zone et al., 1998Zone J.J. Taylor T.B. Meyer L.J. Petersen M.J. The 97 kDa linear IgA bullous disease antigen is identical to a portion of the extracellular domain of the 180 kDa bullous pemphigoid antigen BPAg2.J Invest Dermatol. 1998; 110: 207-210https://doi.org/10.1046/j.1523-1747.1998.00129.xCrossref PubMed Scopus (187) Google Scholar;Egan et al., 1999Egan C.A. Taylor T.B. Meyer L.J. Petersen M.J. Zone J.J. Bullous pemphigoid sera that contain antibodies to BPAg2 also contain antibodies to LABD97 that recognize epitopes distal to the NC16A domain.J Invest Dermatol. 1999; 112: 148-152https://doi.org/10.1046/j.1523-1747.1999.00490.xAbstract Full Text Full Text PDF PubMed Scopus (38) Google Scholar). These IgG anti-LABD97 antibodies cross-reacted with BPAg2 but did not recognize epitopes in its NC16A domain. In this study, affinity-purified IgG anti-LABD97 antibodies from bullous pemphigoid patients' sera were reacted with three protein constructs that together encode almost the entire extracellular domain of BPAg2. Construct EC2 (amino acids 527–1187) in pCEP-Pu vector was obtained from Dr. Peter Mueller, University of Lubeck, Germany (Areida et al., 1999Areida S.K. Reinhardt D.P. Muller P.K. et al.Properties of the collagen type XVII Ectodomain. Evidence for N-to C-Terminal Triple Helix Folding.J Biol Chem. 1999Google Scholar). Another BPAg2 ectodomain construct, EC3 coding for amino acids 482–616, was wenerated using the sense primer 5′-GCTCTTCGGCCTCATTGCTCT-3′ and the antisense primer 5′-CATGCCAGGATCTCCCACGCT-3′. The Nhe I-Not I digested PCR product was cloned into a modified pCEP-Pu vector that additionally coded for an eight amino acid FLAG peptide that preceded the APLA residues in frame, thereby resulting in a FLAG-tagged EC3 polypeptide. The resulting peptide migrated with a molecular weight of approximately 30 kDa. These two ectodomain constructs were expressed using the HEK 293 EBNA mammalian expression system and selected using 5 μg per ml of the antibiotic puromycin (Sigma, St. Louis, MO). The EC3 protein was purified from conditioned media using an anti-FLAG affinity column (Sigma, St. Louis, MO), while the EC2 protein was obtained by concentrating conditioned media using a Centricon filter (Amicon, Beverly, MA) and then used for western blotting. GST-BP-915, a GST fusion protein, contains 305 amino acids (1193–1497) of the distal region of the BPAg2 extracellular domain as reported previously (Nie and Hashimoto, 1999Nie Z. Hashimoto T. IgA antibodies of cicatricial pemphigoid sera specifically react with C-terminus of BP180.J Invest Dermatol. 1999; 112: 254-255https://doi.org/10.1046/j.1523-1747.1999.00501.xCrossref PubMed Scopus (94) Google Scholar). To produce this recombinant protein, an appropriate cDNA fragment of BPAg2 was obtained by PCR of a KU8 cDNA library and put into a pGST-2T vector for its production. To decrease the degradation of the protein, BL12 was used as the host bacteria and the culture temperature was adjusted to 14°C. The fusion protein was induced by IPTG and purified from bacterial lysates by a glutathione-agarose affinity column. IgG antibodies specific for the LABD97 antigen were affinity purified from sera by elution of antibodies from LABD97 bound to nitrocellulose strips as described byOlmsted, 1981Olmsted J.B. Affinity purification of antibodies from diazontized paper blots of heterogenous protein samples.J Biol Chem. 1981; 256: 11955-11957Abstract Full Text PDF PubMed Google Scholar and modified bySmith and Fisher, 1984Smith D.E. Fisher P.A. Identification, developmental regulation, and response to heat shock of two antigenically related forms of a major nuclear envelope protein in Drosopholia embryos: application of an improved method for affinity purification of antibodies using polypeptides immobilized on nitrocellulose blots.J Cell Biol. 1984; 99: 20-28Crossref PubMed Scopus (437) Google Scholar. Protein in sample buffer was applied to a 10% polyacrylamide gel, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis was performed (Laemmli, 1970Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.Nature. 1970; 227: 680-685Crossref PubMed Scopus (202414) Google Scholar). Proteins were transferred electrophoretically onto nitrocellulose, and the nitrocellulose strips were incubated with sera or eluates for 2 h at room temperature (Towbin et al., 1979Towbin H. Staehelin T. Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proc Natl Acad Sci USA. 1979; 76: 4350-4534Crossref PubMed Scopus (44154) Google Scholar). Immunoblots were developed using a biotin labeled antihuman γ-chain antibody and an avidin-biotin-peroxidase complex. Reaction times for all lanes of individual blots were identical. In this study, 12 BP patients' sera were used (Figure 1). All had a circulating IgG antibody titer of at least 40 binding to the epidermal side of 1 M NaCl split skin on indirect immunofluorescence microscopy. Antibody eluates from nine of these BP sera contained IgG anti-LABD97 specific antibodies, all of which reacted with the EC2 construct containing 660 amino acids from the mid-portion of the BPAg2 ectodomain. Eluates from three patients' sera with IgG antibodies reactive with BPAg2 but not LABD97 on western blot, or eluates from negative control sera, subjected to identical affinity purification procedures, did not react with this construct. Only one patient's affinity-purified IgG anti-LABD97 antibodies reacted with the EC3 construct containing 134 amino acids (including the entire NC16A domain and parts of the transmembrane region and part of the fifteenth collagenous domain). Eluates from all 12 affinity-purified BP patient's sera failed to react with the GST-BP-915 bacterial fusion protein containing the carboxy-terminal 304 amino acids of BPAG2. This study demonstrates that BP patients' sera that contain IgG antibodies reactive with LABD97 react with an epitope or epitopes contained in a 571 amino acid stretch of the mid-portion of the BPAg2 ectodomain. It confirms the findings of our previous study by showing that nearly all of the affinity-purified IgG anti-LABD97 specific antibodies fail to react with the NC16A domain of BPAg2 (Egan et al., 1999Egan C.A. Taylor T.B. Meyer L.J. Petersen M.J. Zone J.J. Bullous pemphigoid sera that contain antibodies to BPAg2 also contain antibodies to LABD97 that recognize epitopes distal to the NC16A domain.J Invest Dermatol. 1999; 112: 148-152https://doi.org/10.1046/j.1523-1747.1999.00490.xAbstract Full Text Full Text PDF PubMed Scopus (38) Google Scholar). One patient's affinity-purified anti-LABD97 antibodies did react with thu EC3 construct. We postulate that these antibodies reacted either with a post-translationally modified epitope not contained in the bacterial fusion protein used previously, or that they recognized an epitope contained in the amino-terminal region of the fifteenth collagenous domain. It is not surprising that none of the patients' affinity-purified antibodies reacted with the bacterial fusion protein containing the carboxy-terminal region of BPAg2. When LABD97 was partially sequenced, no homologous amino acid sequences were detected in the carboxy-terminal 237 amino acids of BPAg2, suggesting that the carboxy-terminus of LABD97 lies in this region of BPAg2 (Zone et al., 1998Zone J.J. Taylor T.B. Meyer L.J. Petersen M.J. The 97 kDa linear IgA bullous disease antigen is identical to a portion of the extracellular domain of the 180 kDa bullous pemphigoid antigen BPAg2.J Invest Dermatol. 1998; 110: 207-210https://doi.org/10.1046/j.1523-1747.1998.00129.xCrossref PubMed Scopus (187) Google Scholar). Therefore, any antibodies in the test patients' sera reactive with epitopes in this region of BPAg2 would not bind to LABD97 and thus would not be affinity purified. The fact that the IgG anti-LABD97 antibodies cross-react with BPAg2 is notable. IgA antibodies targeting LABD97 do not cross-react with BPAg2 (Zone et al., 1990Zone J.J. Taylor T.B. Kadunce D.P. Meyer L.J. Identification of the cutaneous basement membrane zone antigen and isolation of antibody in linear immunoglobulin A bullous dermatosis.J Clin Invest. 1990; 85: 812-820Crossref PubMed Scopus (237) Google Scholar;Dmochowski et al., 1993Dmochowski M. Hashimoto T. Bhogal B.S. Black M. Zone J.J. Nishikawa T. Immunoblotting studies of linear IgA disease.J Dermatol Sci. 1993; 6: 194-200Abstract Full Text PDF PubMed Scopus (100) Google Scholar). Therefore, it seems likely that both antibody isotypes recognize different epitopes on LABD97. The finding of antibodies targeting epitopes other than the NC16A domain of BPAg2 in BP patients' sera is well documented (Perriard et al., 1999Perriard J. Jaunin F. Favre B. et al.IgG autoantibodies from bullous pemphigoid (BP) patients bind antigenic sites on both the extracellular and the intracellular domains of the BP antigen 180.J Invest Dermatol. 1999; 112: 141-147https://doi.org/10.1046/j.1523-1747.1999.00497.xAbstract Full Text Full Text PDF PubMed Scopus (93) Google Scholar;Egan et al., 1999Egan C.A. Taylor T.B. Meyer L.J. Petersen M.J. Zone J.J. Bullous pemphigoid sera that contain antibodies to BPAg2 also contain antibodies to LABD97 that recognize epitopes distal to the NC16A domain.J Invest Dermatol. 1999; 112: 148-152https://doi.org/10.1046/j.1523-1747.1999.00490.xAbstract Full Text Full Text PDF PubMed Scopus (38) Google Scholar;Schumann et al., 2000Schumann H. Baetge J. Tasanen K. et al.The shed ectodomain of collagen XVII/BP180 is targeted by autoantibodies in different blistering skin diseases.Am J Pathol. 2000; 156: 685-695Abstract Full Text Full Text PDF PubMed Scopus (158) Google Scholar). This may just represent the phenomenon of epitope spreading (Chan et al., 1998Chan L.S. Vanderlugt C.J. Hashimoto T. et al.Epitope spreading: lessons from autoimmune skin diseases.J Invest Dermatol. 1998; 110: 103-109Crossref PubMed Scopus (270) Google Scholar). The pathogenic relevance of these IgG antibodies to LABD97 in BP is unknown, however. In a mouse model of BP, using rabbit IgG anti-BPAg2 antibodies,Liu et al., 1995Liu Z. Diaz L.A. Swartz S.J. Troy J.L. Fairley J.A. Giudice G.J. Molecular mapping of a pathogenically relevant BP180 epitope associated with experimentally induced murine bullous pemphigoid.J Immunol. 1995; 155: 5449-5454PubMed Google Scholar have demonstrated that pathogenic antimurine BPAg2 antibodies bind to a site within the murine NC14A domain, which is equivalent to the NC16A domain of human BPAg2. These antibodies bind to neonatal mouse skin basement membrane and induce complement activation leading to an inflammatory infiltrate with neutrophils leading to subepidermal separation with rapid sloughing of epidermis. We are currently developing an animal model of BP using human skin engrafted immunodeficient mice. Preliminary results suggest that passive transfer of mouse IgG class monoclonal antibodies to LABD97 induces subepidermal graft separation with an inflammatory infiltrate of eosinophils, mirroring the disease process in humans. 1Egan CA, Taylor TB, Foutz MW, Florell SR, Meyer LJ, Peterson MJ, Zone JJ: Development of an animal model of bullous pemphigoid characterized by basement membrane zone separation and an eosinophilic inflammatory infiltrate. J Invest Dermatl 112:531 1999 (abstr.) This suggests that antibodies to the LABD97 antigen region of BPAg2 (i.e., antibodies targeting epitopes outside the NC16A domain) may be important in the pathogenesis of BP. In summary, we have characterized the binding specificity of anti-LABD97 IgG class antibodies in BP patients' sera and demonstrated that they selectively bind to a region in the mid-portion of the BPAg2 ectodomain that is potentially different from the epitope recognized by IgA antibodies in linear IgA bullous dermatosis. Moreover, this region is distinct from antibody reactive sites previously described on the BPAg2 ectodomain in BP patients' sera. This work was supported by a Dermatology Foundation Leaders Society Dermatologist Investigator Research Fellowship (C.A.E.) and by Department of Veterans Affairs Medical Research Funds (J.J.Z. and L.J.M.) and National Institutes of Health Grant #R01 DK50678–01A1 (J.J.Z.).

A 1‐year‐old girl presented for evaluation of a linear plaque on her forehead. She was born at 36 weeks' gestation following an uncomplicated pregnancy and delivery. At birth, she was noted to have an enlarged right cheek. She had no seizure history, but developed grand mal seizures 1 year later.On examination, she had a yellow plaque on her forehead which extended onto her nose. Under her right jaw, extending onto her anterior neck, there was a café‐au‐lait macule within which there was a yellow plaque which followed the lines of Blaschko. Her right cheek was enlarged and was erythematous (Fig. 1).Epidermal nevus on the forehead and right hemifacial hypertrophyimageMagnetic resonance imaging (MRI) of her face showed a mass in the right cheek deep to the subcutaneous fat tissue layer. The signal from the mass was identical to that from the fat, indicating that the mass represented a lipoma. This was later excised surgically and was histologically a lipoma. MRI of the brain demonstrated enlargement of the right lateral ventricle in addition to enlargement of the right cerebral hemisphere. There was also evidence of abnormal gyral architecture. Computerized tomography (CT) three‐dimensional reconstruction of the skull demonstrated overgrowth of the right maxilla, right mandible, and right orbit (Fig. 2).Computerized tomography reconstruction of skull showing overgrowth of the bones on the right sideimage

Epidermolysis bullosa acquisita (EBA) is an autoimmune subepidermal blistering disease characterized by IgG anti-basement membrane autoantibodies to collagen VII. Since autoantibody formation in EBA patients is thought to be T-cell-dependent, the degree of T cell activation in three patients (all males, ages 33–44 years) was assessed by quantitation of soluble Tac, a fragment of the α-subunit of the high-affinity IL-2 receptor (CD25). Soluble Tac levels in all patients were elevated [highest random values, 2430, 920, and 560 IU/ml (normal range, 112–502)]. Based on such findings, these patients were treated with the humanized murine monoclonal anti-Tac antibody daclizumab (1 mg/kg, 6–12 iv treatments at 2- to 4-week intervals). All patients had a significant, rapid, and persistent decrease in lymphocyte CD25 expression. Though a moderate decrease in lymphocyte expression of 7G7, an IL-2 receptor epitope not bound by daclizumab, was noted, stable levels of CD3 cells and in vitro saturation studies indicated that daclizumab effectively bound CD25 and did not promote clearance of such cells from peripheral blood. There were no complications and no patient developed antibodies against daclizumab. While no apparent clinical benefit was seen in two patients with dermolytic disease, one patient with inflammatory EBA had a favorable response. While on daclizumab, this patient stopped prednisone, significantly reduced dapsone, and improved clinically. Furthermore, his disease flared when treatment was stopped, and resumption of daclizumab again effected improvement within 2 weeks. Daclizumab therapy is safe and well tolerated in EBA patients. It may be effective as a corticosteroid sparing agent in patients with inflammatory EBA.

Cicatricial pemphigoid (CP) is a rare, acquired, autoimmune, subepithelial blistering disease. It primarily affects mucous membranes but it also may involve the skin. Morbidity is associated with the propensity for scar formation and may be especially severe when mucosal surfaces such as the conjunctivae, larynx, esophagus, or urethra are involved. On direct immunofluorescence microscopy, CP is characterized by the linear deposition of immunoreactants, principally IgG and C3, along epithelial basement membranes. Over the last 10 years, studies in a number of laboratories have shown that circulating autoantibodies in patients with CP may target one of several different autoantigens. One subset of patients with the CP-phenotype have IgG anti-basement membrane autoantibodies against laminin 5 (alpha3beta3gamma2) (i.e., patients with anti-epiligrin CP [AECP]). This review discusses recent advances in the understanding of CP and emphasizes salient features of AECP pathophysiology.

Acute generalized exanthematous pustulosis (AGEP) is characterized by acute onset of a widespread pustular eruption in association with fever. It is usually seen as a medication reaction. We describe a 17-month-old boy with AGEP secondary to exposure to amoxicillin. This is an uncommon condition in children.

Autoimmune blistering diseases are generally distinct entities characterized by relatively consistent clinical, histologic, and immunopathologic findings. These disorders may cause impaired adhesion of epidermis to epidermal basement membrane (eg, the pemphigoid group of disorders [bullous, gestational, and mucous membrane]) or impaired adhesion of epidermal cells to each other (eg, the pemphigus group of disorders). Recent studies have shown that these disorders are characterized by autoantibodies that often display pathogenic (ie, blister-forming) activity in passive transfer models. Interestingly, the autoantigens targeted by these patients' autoantibodies represent important structural proteins that promote cell matrix (eg, pemphigoid) or cell-to-cell (eg, pemphigus) adhesion in skin. Autoimmune blistering diseases are characterized by substantial morbidity (pruritus, pain, disfigurement), and in some instances, mortality (secondary to loss of epidermal barrier function). Treatment with systemic immunosuppressives has reduced morbidity and mortality in patients with these diseases.