Identification of λ light chain amyloid in eight canine and two feline extramedullary plasmacytomas

Platz, Siegfried; Breuer, W.; Geisel, O.; Linke, Reinhold P.; Hermanns, W.

doi:10.1016/s0021-9975(97)80042-4

Cited by 44 publications

(43 citation statements)

References 29 publications

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“…21,51 Localized amyloid deposits with or without association with neoplasia also have been described in the human mammary gland, 41,52 respiratory tract, 26,34 gastrointestinal tract, 5,38 genitourinary tract, 13,17 skin, 24,25 and bone. 23 In animals, localized amyloidosis has been associated with neoplastic conditions such as calcifying epithelial odontogenic tumor (CEOT), 2,29 pancreatic endocrine tumor, 28 medullary thyroid carcinoma, 15 ameloblastoma, 10 mammary carcinoma, 43 intestinal carcinoid, 40 extramedullary plasmacytoma, 31,36 and myeloma. 12 CEOT is a rare neoplasm of the tooth-forming apparatus that produces a mineralized substance and amyloid.…”

mentioning

confidence: 99%

Biochemical and Immunohistochemical Characterization of the Amyloid in Canine Amyloid-Producing Odontogenic Tumor

Hirayama

Miyasho

Ohmachi³

et al. 2010

Vet Pathol

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The amyloid of canine amyloid-producing odontogenic tumor (APOT) was evaluated biochemically and immunohistochemically. The N-terminal amino-acid sequence of purified amyloid protein from a canine APOT was strikingly similar to the sequence in both rat ameloblastin and porcine sheathlin. Immunohistochemically, the amyloid in APOT from 9 dogs was strongly reactive with anti-rat ameloblastin, anti-porcine sheathlin, and anti-canine APOT amyloid and weakly reactive with anti-porcine amelogenin but negative for antibodies to cytokeratins, vimentin, desmin, a-smooth muscle actin, amyloid A, glial fibrillary acidic protein, or S100 protein. The neoplastic epithelial cells of APOT were focally reactive with antibodies to ameloblastin, sheathlin, amelogenin, and canine APOT amyloid. The similarity in amino-acid sequence of the amyloid protein of canine APOT to that of enamel proteins, such as ameloblastin, sheathlin, and amelogenin, and the expression of these antigens in both APOT amyloid and in the neoplastic cells suggest that the amyloid of canine APOT is derived from enamel proteins secreted by ameloblasts. Keywords ameloblasts, amyloid, dogs, enamel proteins, odontogenic tumorAmyloidosis is a heterogeneous group of disorders characterized by the deposition of amyloid proteins derived from any of at least 25 different precursor molecules. Amyloid is considered a pathologic substance that appears histologically as an extracellular, amorphous, congophilic protein with applegreen birefringence under polarized light. Amyloidosis can be categorized as systemic or localized. Common human types of localized amyloidosis include amyloidosis of endocrine organs associated (or not) with neoplastic conditions and cerebral amyloidosis of Alzheimer's disease. 21,51 Localized amyloid deposits with or without association with neoplasia also have been described in the human mammary gland, 41,52 respiratory tract, 26,34 gastrointestinal tract, 5,38 genitourinary tract, 13,17 skin, 24,25 and bone. 23 In animals, localized amyloidosis has been associated with neoplastic conditions such as calcifying epithelial odontogenic tumor (CEOT), 2,29 pancreatic endocrine tumor, 28 medullary thyroid carcinoma, 15 ameloblastoma, 10 mammary carcinoma, 43 intestinal carcinoid, 40 extramedullary plasmacytoma, 31,36 and myeloma. 12 CEOT is a rare neoplasm of the tooth-forming apparatus that produces a mineralized substance and amyloid. 30 The origin of the amyloid in human and animal CEOT is often debated but is still unknown. 2,19,27,29,37,42,46 Recent studies indicate that the amyloid in human CEOT is secreted by the neoplastic epithelial cells, but its precise nature remains unclear. 27,39,42 CEOT in veterinary medicine is classified as amyloidproducing odontogenic tumor (APOT). 9,14 In the present study, we partially sequenced the amino acids of the major amyloid protein of canine APOT and compared the amino-terminal sequence with that of the enamel proteins rat ameloblastin and porcine sheathlin, which are transcribed in cells of the epi...

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confidence: 99%

Biochemical and Immunohistochemical Characterization of the Amyloid in Canine Amyloid-Producing Odontogenic Tumor

Hirayama

Miyasho

Ohmachi³

et al. 2010

Vet Pathol

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“…3,7,29,30 Judging from the existing case reports involving only one or two animals, the incidence of EMP in cats seems to be low. Feline EMPs have been described as occurring in the skin, 4,5,13,19 gastrointestinal tract, 24,31 retroperitoneal space, 14 upper lip, gingiva, 9 and orbita. 28 Affected cats were generally more than 10 years old; the average age of the animals was 10.6 years.…”

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confidence: 99%

Histopathologic and Immunophenotypic Characterization of Extramedullary Plasmacytomas in Nine Cats

et al. 2003

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Abstract. To contribute to the existing body of knowledge in the literature on the apparently rare extramedullary plasmacytoma in cats, lymphoid tumors with plasmacytic cellular morphology taken from nine cats were examined. The paraffin-embedded material was investigated by standard hematoxylin and eosin, and special staining techniques (Giemsa, Congo-red, and periodic acid-Schiff reaction). The tumors also were examined immunohistochemically for the presence of immunoglobulin G, immunoglobulin A, immunoglobulin M, immunoglobulin light chains (, ), various amyloid proteins, and FeLV-antigen (p27 protein). An immunoglobulin-producing tumor of plasmacellular origin (extramedullary plasmacytoma [EMP]) could be diagnosed in all cases on the basis of immunohistochemical light-chain expression. All but one of the neoplasms occurred in the skin of older, predominantly male cats. As in humans and dogs, the following types could be identified according to their morphologic features: mature type (two), cleaved type (two), asynchronous type (four), and polymorphous type (one). The tumor tissue of three cats revealed amyloid deposits, which were immunohistochemically diagnosed as AL-amyloid in all three cases.

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“…AA amyloid has been described in liver, spleen, lung, pancreas and kidney (van der Linde-Sipman et al, 1997;Zini et al, 2008). On the contrary, AL amyloidosis in the cat has been reported localized within neoplastic tissue of extramedullary plasmacytomas (Platz et al, 1997). For the purpose of this chapter we will discuss only renal amyloidosis in cats.…”

Section: Glomerular Amyloidosismentioning

confidence: 95%

“…Another form is immunoglobulin-derived amiloidosis (primary or AL), in which amyloid is produced from immunoglobulin light chains in plasma cell dyscrasias as a product of monoclonal B-cell proliferation (Obici et al, 2005;Merlini et al, 2011). This type of amyloidosis is uncommon in domestic animals but has been described in the dog, cat and horse (Platz et al, 1997;Kim et al, 2005). Both AA and AL amyloidosis occur in systemic or localized forms (Merlini et al, 2011).…”

Section: Glomerular Amyloidosismentioning

confidence: 99%

Glomerular Injury in Domestic Cats and the Iberian Lynx (Lynx pardinus): A Comparative Review

Jiménez¹,

Sánchez²,

Peña³

2011

An Update on Glomerulopathies - Etiology and Pathogenesis

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Identification of λ light chain amyloid in eight canine and two feline extramedullary plasmacytomas

Cited by 44 publications

References 29 publications

Biochemical and Immunohistochemical Characterization of the Amyloid in Canine Amyloid-Producing Odontogenic Tumor

Biochemical and Immunohistochemical Characterization of the Amyloid in Canine Amyloid-Producing Odontogenic Tumor

Histopathologic and Immunophenotypic Characterization of Extramedullary Plasmacytomas in Nine Cats

Glomerular Injury in Domestic Cats and the Iberian Lynx (Lynx pardinus): A Comparative Review

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