Myeloma Associated with Immunoglobulin Lambda-light Chain Derived Amyloid in a Dog

Geisel, O.; Stiglmair‐Herb, Maria T.; Linke, Reinhold P.

doi:10.1177/030098589002700514

Cited by 21 publications

(11 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

Section: Discussionmentioning

confidence: 99%

“…1,5,16,17,24 In one report, the amyloid was identified by immunohistochemistry to originate from λ light chains. 5 This study demonstrated that Cocker Spaniels have a higher incidence of EMP than do other canine breeds. In previous reports, the Cocker Spaniel also had a higher incidence (16%, 11%) of EMP, but statistical analyses were not performed to determine whether the Cocker Spaniel was more susceptible than other dog breeds.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Identification of Immunoglobulin Light Chains in Canine Extramedullary Plasmacytomas by Thioflavine T and Immunohistochemistry

Brunnert

Altman

1991

J VET Diagn Invest

View full text Add to dashboard Cite

Abstract. Extramedullary plasmacytomas were studied in 29 dogs. The site at which tumors occurred and the age and sex of the dogs were similar to those in previous reports. The skin of the digits, chin, ear, and lip represented the most common (17/29) tumor sites. Males and females were equally represented, and tumors occurred in middle-aged to old dogs (mean age, 9.0 years). A breed predilection was seen in the Cocker Spaniel (n = 7; 24%); Cocker Spaniels represented only 4% (210/4,725) of the submissions during the same period. Tumors were stained with immunohistochemical markers (λ light chain, K light chain) and thioflavine T. Immunoreactivity was limited to either λ or K light chains, consistent with a monoclonal plasma cell population. The majority of tumors expressed λ light chains, consistent with previously reported canine plasma cell dyscrasias. Thioflavine T cytoplasmic fluorescence was seen in the majority (18/29) of plasmacytomas and with inflammatory plasma cells present in control specimens. Other round cell neoplasms (lymphosarcoma, histiocytoma, and mastocytoma) were negative with thioflavine T, indicating that positive staining with thioflavine T was specific for plasma cells (neoplastic and inflammatory). This study confirms by immunohistochemistry that canine extramedullary plasmacytomas disproportionately express λ light chains and establishes thioflavine T staining as a rapid histochemical method for diagnosis of these tumors.The morphologic, clinical, and biological features of canine extramedullary plasmacytoma (EMP) have been reported 1,13,16,17,20,24 Most dogs were aged adults, and tumors developed most commonly on the mucocutaneous junction of the mouth, the skin between the digits, and on the external ear. 1,24 More than 90% of the dogs with cutaneous EMP were cured by surgical excision, indicating that these tumors were most likely benign. Multiple EMP were found in a small percentage of dogs but were not associated with progression to multiple myeloma. Only rarely did cases of canine EMP precede the development of multiple myeloma, 14,24 which is different from the clinical course seen in humans.In humans, long-term survival of 15 years without recurrence occurs in the majority of cases of EMP, 28 but in approximately 25% of the cases, EMP will develop into multiple myeloma. 18 When EMP precedes the development of multiple myeloma, an extended period (up to 10 years) may occur before clinical signs of bone involvement are noted. Secondary extramedullary involvement of the skin with primary multiple myeloma is rare. Immunohistochemical characterization of human EMP with immunoglobulin heavy and light chains reveals a monoclonal proliferation of plas-

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Identification of Immunoglobulin Light Chains in Canine Extramedullary Plasmacytomas by Thioflavine T and Immunohistochemistry

Brunnert

Altman

1991

J VET Diagn Invest

View full text Add to dashboard Cite

show abstract

“…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.…”

mentioning

confidence: 99%

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

Hirayama

Miyasho

Ohmachi³

et al. 2010

Vet Pathol

View full text Add to dashboard Cite

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...

show abstract

“…In cases in which an animal amyloid needs to be classifi ed, we use mostly antibodies directed against human amyloids that crossreact with the respective animal amyloids in tissue sections (some ALλ and some AA antibodies seem to be generic for most or all ALλ or AA amyloids), that include for ALλ such species as the horse, dog, cat, and humans, and for AA, all tested mammalian and avian species tested so far (Geisel et al, 1990;Colbatzky et al, 1991;Ofri et al, 1997;Platz et al, 1997;Schulz et al, 1998;Zschiesche and Linke, 1989).…”

Section: Sets Of Antibodiesmentioning

confidence: 99%

Congo Red Staining of Amyloid: Improvements and Practical Guide for a More Precise Diagnosis of Amyloid and the Different Amyloidoses

Linke

Protein Reviews

View full text Add to dashboard Cite

Congo red (CR) is the most popular dye used as a probe for diagnosing amyloidosis, a very heterogeneous group of diseases with more than 23 chemically different amyloid syndromes of men and animals, leading to more than 400 different individual diseases. Congo red binding increases the natural anisotropy of amyloid, indicating that the elongated and planar CR molecules are aligned parallel to the axis of the amyloid α fi brila and to each other, thereby revealing a structure of amyloid. This structure was established to represent fi brils of similar dimensions, although the amyloid fi brils can be composed of many unrelated proteins. This CR-induced (positive) anisotropy displaying a green color is the hallmark of all amyloids, and is therefore used in the diagnosis of amyloidosis. The specifi city of this criterion, however, is based on very stringent conditions of staining and evaluation. This review will focus on the understanding of the CR staining procedure, its mechanism and, in particular, on its recent practical improvements by increasing the sensitivity of the CR procedure, so that minute and the earliest amyloid deposits in the course of amyloidosis can now be reliably detected in patients. This enables a very early diagnosis in the course of the disease before irreversible organ damage might have occurred, and widens the options for a successful therapy. In addition, the central role of the CR diagnostic procedure and evasion of common pitfalls in arriving at a pathogenetically exact classifi cation must only be based on the chemical nature of the amyloid deposits and not on the soluble precursors of the many different amyloidoses will be highlighted. The proposed bench-tobedside algorithm will enable the physician to arrive at the exact diagnosis for therapeutic considerations. Finally, some possible future applications of CR and analogues will be presented.

show abstract

Myeloma Associated with Immunoglobulin Lambda-light Chain Derived Amyloid in a Dog

Cited by 21 publications

References 4 publications

Identification of Immunoglobulin Light Chains in Canine Extramedullary Plasmacytomas by Thioflavine T and Immunohistochemistry

Identification of Immunoglobulin Light Chains in Canine Extramedullary Plasmacytomas by Thioflavine T and Immunohistochemistry

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

Congo Red Staining of Amyloid: Improvements and Practical Guide for a More Precise Diagnosis of Amyloid and the Different Amyloidoses

Contact Info

Product

Resources

About