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A 14-year-old domestic longhaired cat presented with a 2-year history of nasal discharge and a recent onset of inappetence and submandibular lymphadenopathy. The cat was humanely destroyed after developing severe respiratory distress. Necropsy examination revealed thickened nasal turbinates and soft palate, and friable red-tan material within the frontal sinus, nasal cavity and nasopharynx. The lungs contained multifocal irregular friable tan nodules. Multiple lymph nodes were enlarged, friable and red-tan in colour. Histopathology revealed a mature type extramedullary plasmacytoma (EMP) within the frontal sinus, nasal cavity, soft palate, larynx, trachea, lungs and multiple lymph nodes. The lymph nodes and larynx also contained marked granulomatous inflammation with extensive intrahistiocytic (and lesser amounts of extracellular) lambda light chain amyloid, confirmed by electron microscopy and immunohistochemistry. Neoplastic cells expressed CD79a and MUM1. This is the first report of an infiltrative EMP of the feline respiratory tract with lymph node metastasis and predominantly intrahistiocytic amyloid., (Copyright © 2016 Elsevier Ltd. All rights reserved.)

Intestinal extramedullary plasmacytomas (EMPs) are rare tumours in dogs. Three cases of canine intestinal EMP with amyloid deposits are described in this report. These tumours, which were located in the rectal submucosa, had variable numbers of well-differentiated plasma cells and fewer multinucleated giant cells of plasmacytoid and histiocytic morphology, admixed with abundant amyloid. Two cases had metaplastic cartilage and bone within the amyloid deposits. Immunohistochemically, the plasma cells of all three tumours reacted for lambda-light chains of immunoglobulins but not for kappa-chains, indicating monoclonality. Plasma cells of two tumours were also positive to CD79a antiserum. Amyloid deposits were labelled with an A lambda (amyloid of immunoglobulin lambda-light chain origin) antiserum but not with antisera against its precursor protein, the immunoglobulin lambda-light chains, indicating possible conformational changes of amyloidogenic proteins during their transformation into amyloid.

Samples from rectal plasmacytoma in three adult dogs that were diagnosed by light microscopy and immunohistochemistry were examined by electron microscopy. The most common cell type had typical plasmacytoid features. A second cell type was a plasmacytoid giant cell with single or multiple eccentric nuclei, irregular nuclear membrane, abundant and dilated rough endoplasmic reticulum, and numerous electron-dense granules. The third cell type was a histiocytic giant cell that intermingled with plasmacytoid cells. All three tumors had abundant amyloid, mainly in the interstitium but also within histiocytic cells and less commonly in plasma cells or plasmacytoid giant cells. Extracellular and intracellular amyloid fibrils and the contents of membrane-bound electron-dense bodies of plasma cells reacted with antibody to lambda-light chain of immunoglobulins by immunogold staining.

Amyloid deposits from equine cutaneous nodular amyloidosis associated with extramedullary plasmacytoma were classified immunohistochemically as equine immunoglobulin lambda-light chain-derived and designated eA lambda (HIP). For chemical identification, the amyloid fibril proteins were separated on Sephadex G-100 in 6M guanidine.HCl. Polypeptides of predominantly 24 kDa and 50 kDa were found by polyacrylamide gel electrophoresis. They have preponderance of immunoglobulin lambda-antigenic determinants as detected by immunodiffusion and immunoblotting. Since the N-terminus of the major proteins was blocked, peptides were generated with trypsin and endoproteinase Asp-N and then isolated using reversed-phase high-performance liquid chromatography. Automatic amino-acid sequence determination of seven peptides showed novel sequences. Data bank comparison indicated that these peptides were derived from a monoclonal immunoglobulin lambda-light and a gamma-heavy chain. The light chain was considered to be the leading amyloidogenic polypeptide, since it was the predominant component in a virtually pure amyloid fibril preparation. Thus, immunoglobulin lambda-light chain-derived amyloidosis, so far established only in man and cat, has now also been identified in the horse.

Cutaneous plasmacytomas associated with local deposition of amyloid were diagnosed by light microscopy in a series of six older dogs (mean age 10.7 years) consisting of two Cocker Spaniels, a Poodle, a Weimeraner, and two mixed-breed dogs. The neoplasms occurred on the digits (2 dogs), forelimb (2 dogs), lip (1 dog), and ear (1 dog). In most cases, groups of neoplastic plasma cells were widely separated by large homogeneous islands of amyloid. The neoplastic cells had characteristic plasmacytoid features, but the degree of pleomorphism varied greatly between different neoplasms. In four of the six tumors, the diagnosis of plasmacytoma was confirmed by the demonstration of a monoclonal plasma cell population using immunofluorescent staining for anti-canine immunoglobulins. In these tumors, the neoplastic cells reacted with only one class of immunoglobulins (IgG). The amyloid did not react with any of the reagents used. The suspicion that the amyloid was of immunoglobulin origin (primary amyloid) was supported by its retention of birefringence under polarized light after treatment with potassium permanganate and staining with Congo red.