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Year : 2016  |  Volume : 59  |  Issue : 4  |  Page : 444-445
Soft tissue amyloidoma in association with plasmacytoma

Department of Pathology, Rohilkhand Medical College and Hospital, Bareilly, Uttar Pradesh, India

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Date of Web Publication10-Oct-2016

How to cite this article:
Agrawal R. Soft tissue amyloidoma in association with plasmacytoma. Indian J Pathol Microbiol 2016;59:444-5

How to cite this URL:
Agrawal R. Soft tissue amyloidoma in association with plasmacytoma. Indian J Pathol Microbiol [serial online] 2016 [cited 2021 Jun 22];59:444-5. Available from: https://www.ijpmonline.org/text.asp?2016/59/4/444/191752

Amyloidosis is a heterogeneous group of disorders characterized by extracellular deposition of abnormal amount of specialized protein fibrils in numerous organs as a result of abnormal folding of proteins. [1] In humans, amyloidosis was first recognized in the mid-19 th century when the term amyloid (for starch or cellulose) was coined by Rudolf Virchow to describe the deposition of abnormal extracellular material in the liver on autopsy. [2] As a matter of fact, he was mistaken about the nature of the deposit since all the material deposited comprise predominantly of protein and not carbohydrate. In the early 1970s, the first two amyloid fibril proteins were extracted and then it became apparent that amyloid is chemically heterogeneous. Currently, 19 different proteins have been found to form amyloid fibrils in humans. [3],[4] This diversity in the nature of the protein depositions generated the need for a reliable nomenclature and classification. The classification currently accepted was first proposed in 1990 and later updated in 1998, is based on the chemical structure of amyloid fibril protein, according to which the amyloid fibril protein is designated as protein A with a suffix that identifies the specific protein. Thus, amyloid derived from the immunoglobulin monoclonal light chain is designated AL whereas amyloid derived from protein A is designated AA. [3]

Amyloidosis may be hereditary or acquired with the deposits having varied distribution. Historically, amyloidosis was classified as primary and secondary or systemic and localized. Several amyloid proteins may be associated with both systemic and localized forms. Some amyloids that are typically systemic (AL, amyloid derived from transthyretin [ATTR]) in some patients may form only localized nodules or may involve only a single organ in others. Systemic amyloidosis is of three types: AL, ATTR, and AA. AL type is the only type of systemic amyloidosis associated with a monoclonal protein and usually tends to progress further into a disseminated form. [4] Diagnosis and close follow-up of solitary plasmacytoma are important since most of the cases finally land into disseminated myeloma.

A rare presentation of amyloid deposition is the formation of a discrete mass termed amyloidoma or amyloid tumor. Amyloidoma is defined as a solitary localized tumor-like deposit of amyloid in the absence of systemic amyloidosis. [5] Amyloidomas have most often been described in the nasal sinuses, upper respiratory tract, lungs, spleen, urinary system, gastrointestinal tract, breast, bone, skin, mediastinum, brain, and soft tissues. [5],[6],[7] Only a handful of cases of soft tissue amyloidoma is available in English literature. Primary soft tissue amyloidoma with features of plasmacytoma is a rare entity, and if present, it usually develops into plasma cell dyscrasia on further follow-up. The differential diagnosis in such cases includes multiple myeloma versus lymphoplasmacytoid lymphoma associated with amyloidoma. Occasional cases of amyloidoma may be associated with plasma cell infiltration in the bone marrow. [6] Some of the cases may show an associated marked giant cell reaction leading to a mistaken diagnosis of giant cell tumor of tendon sheath, postsurgical foreign body reaction, or pseudogout. [7]

It is believed that the primary structure of the light chains plays a critical role in amyloidogenesis: certain amino acid substitutions are thought to destabilize the tertiary structure and alter the normal catabolism of light chains, which then tend to accumulate and ultimately convert into a fibrillar form. By definition, AL is associated with plasma cell dyscrasia or multiple myeloma. [8] However, in many patients, detection of light chain amyloid is the first sign of abnormal immunoglobulin production. In the past, the term primary amyloid was used in patients in whom no underlying plasma cell dyscrasia was detected. However, with more sensitive diagnostic tests available, plasma cell dyscrasia is detectable in almost all the patients with AL.

Approximately, 10% of patients with multiple myeloma are known to progress to amyloidosis. Numerous pathologic conditions may be associated with underlying plasma cell dyscrasia, of which amyloid is one of the manifestations. In kidneys, in addition to amyloid, light chain cast nephropathy or nonamyloidotic deposits of light chain deposition disease, immunotactoid, and deposits of cryoglobulins have also been reported. These deposits are nonfibrillar and do not stain with Congo red staining. Immunohistochemical and biochemical studies confirm the that these are not the intrinsic components of the fibril itself. [3]

Diagnosis of amyloid is based on its tinctorial properties and ultrastructural appearance. Due to the varied heterogeneity of amyloid deposits, immunohistochemical typing is the method of choice. The typing of deposits in routine paraffin sections can be difficult, but frozen sections results are good. Biopsy in all suspected cases must be taken from the most frequently involved organ such as kidney, myocardium, gastrointestinal tract, and peripheral nerves. Abdominal fat aspiration or biopsy can also be used for screening purposes. [3]

   References Top

Maheshwari AV, Muro-Cacho CA, Kransdorf MJ, Temple HT. Soft-tissue amyloidoma of the extremities: A case report and review of literature. Skeletal Radiol 2009;38:287-92.  Back to cited text no. 1
Westermark P. Localized AL amyloidosis: A suicidal neoplasm? Ups J Med Sci 2012;117:244-50.  Back to cited text no. 2
Picken MM. The changing concepts of amyloid. Arch Pathol Lab Med 2001;125:38-43.  Back to cited text no. 3
Sipe J. Revised nomenclature for serum amyloid A (SAA). Nomenclature Committee of the International Society of Amyloidosis. Part 2. Amyloid 1999;6:67-70.  Back to cited text no. 4
Yin H, Alhasan N, Ciervo A, Zinterhofer L. Soft tissue amyloidoma with features of plasmacytoma: A case report and review. Arch Pathol Lab Med 2002;126:969-71.  Back to cited text no. 5
Krishnan J, Chu WS, Elrod JP, Frizzera G. Tumoral presentation of amyloidosis (amyloidomas) in soft tissues. A report of 14 cases. Am J Clin Pathol 1993;100:135-44.  Back to cited text no. 6
Bandyopadhyay A, Bhattacharya S, Maiti B, Bose K. Calcified amyloid tumor of neck with exuberant giant cell reaction. J Lab Physicians 2015;7:61-3.  Back to cited text no. 7
[PUBMED]  Medknow Journal  
Yoshida A, Borkar S, Singh B, Ghossein RA, Schöder H. Incidental detection of concurrent extramedullary plasmacytoma and amyloidoma of the nasopharynx on [18F] fluorodeoxyglucose positron emission tomography/computed tomography. J Clin Oncol 2008;26:5817-9.  Back to cited text no. 8

Correspondence Address:
Ranjan Agrawal
Department of Pathology, Rohilkhand Medical College and Hospital, Bareilly, Uttar Pradesh
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Source of Support: None, Conflict of Interest: None

DOI: 10.4103/0377-4929.191752

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