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IMAGES IN PATHOLOGY
Year : 2011  |  Volume : 1  |  Issue : 2  |  Page : 70-71

Primary localized laryngeal amylodosis presenting with hoarseness of voice


Department of Pathology, Bharati Vidyapeeth Deemed University Medical College, Dhankawadi, Pune, Maharashtra, India

Date of Web Publication19-Sep-2011

Correspondence Address:
Ravi M Swami
Flat no. B4, Vruddheshwar Society, Near Bhagali Orthopedic Hospital, Bibwewadi, Pune - 411 037, Maharashtra
India
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Source of Support: None, Conflict of Interest: None


DOI: 10.4103/2230-9748.85067

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How to cite this article:
Karandikar M, Swami RM. Primary localized laryngeal amylodosis presenting with hoarseness of voice. J Laryngol Voice 2011;1:70-1

How to cite this URL:
Karandikar M, Swami RM. Primary localized laryngeal amylodosis presenting with hoarseness of voice. J Laryngol Voice [serial online] 2011 [cited 2021 Apr 21];1:70-1. Available from: https://www.laryngologyandvoice.org/text.asp?2011/1/2/70/85067

A 54-year-old male, teacher by occupation, came with complaints of hoarseness of voice and dysphonia since 6 months. On laryngoscopic examination, a firm white nodule of 5 mm was seen on left true vocal cord which was excised and subjected to histopatholical examination. Histopathological examination showed mucosa lined by stratified squamous epithelium. The epithelium showed hyperkeratosis and acanthosis with degeneration of superficial layer. Subepithelium showed a thick band of acellular, homogeneous, eosinophilic hyaline material [Figure 1] which stained positively with congo red [Figure 2] and showed apple green birefringence under polarized light. Hence, the diagnosis of amyloidosis was done. Patient was kept on follow-up and shown to have no recurrence after 3 months with excellent return of voice.
Figure 1: H and E photographs showing subepithlial amyloid (×10) on left and homogenous eosinophilc amyloid (×100) on right.

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Figure 2: H and E photographs showing congo red-positive amyloid (×10) on left and subepithalial congo-positive amyloid (×100) on right.

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   Discussion Top


Amyloidosis is a benign, slowly progressive condition that is characterized by the presence of extracellular fibrillar proteins in a variety of organs and tissues. The cause for deposition is immunological. Deposits of amyloid in the larynx are rare, accounting for between 0.2 and 1.2% of benign tumors of the larynx. [1] It affects males slightly more than females, between 40 and 60 years of age. Amyloidosis was first well described by Rokitansky in 1842. Virchow, who gave amyloid its name, found that it stained violet with iodine and sulfuric acid and he attributed this to its cellulose or starch-like nature. [2] Patients with amyloidosis usually present as localized disease but may be a part of systemic disease, the result of a familial condition, a primary disorder, or secondary to an underlying disease or tumor proliferation. [3] Histopathologic examination of amyloid is essential for the diagnosis and classification of amyloidosis. The sensitivity and specificity of the histopathologic diagnosis depend on the biopsy site and the adequacy of the tissue. [4]

Amyloidosis is an extracellular accumulation of insoluble, fibrillar protein. Depending on the extent of deposition, it is classified into systemic (generalized) involving multiple organs and localized involving one or two organs or sites. Different types of amyloid proteins get deposited in localized amyloidosis. In localized laryngeal amyloidosis, monoclonal light chains of immunoglobulin molecules secreted by plasma cells are deposited. The systemic amyloidosis is further classified as primary or secondary amyloidosis. The primary amyloidosis is characterized by deposition of light chains, while secondary amyloidosis results as a complication of chronic diseases such as chronic osteomyelitis, tuberculosis, or rheumatoid arthritis. Whatever be the chemical nature of amyloid, the cross b-pleated configuration seen on X-ray crystallography is responsible for the positive congo red staining and apple green birefringence under polarized light. The gross tissue diagnosis of amyloid is done with Lugol's iodine which imparts mahogany brown color to it. Various other microscopic special stains are also used for the diagnosis of amyloid such as P.A.S., thioflavin, and toludine blue. The exact etiology of primary amyloidosis is unknown, but mostly it occurs due to mis-folding of proteins which is not dissolved by normal proteolysis. Amyloid associated fibrils in secondary amyloidosis are derived from the acute-phase reactant serum amyloid-associated protein (SAA) synthesized in liver through a process of cleavage, misfolding, and aggregation. [5] SAA is an apolipoprotein constituent of high-density lipoprotein that is synthesized by hepatocytes under the transcriptional regulation of proinflammatory cytokines. [6] The definitive method of diagnosing amyloidosis is tissue biopsy. The disease can recur locally and become systemic or multicentric. Renal failure is a frequent cause of death in amyloidosis. Laryngeal amyloidosis is a rare variant and may be a part of systemic amyloidosis. It is important to recognize this entity as this condition has excellent prognosis.

 
   References Top

1.Thompson LD, Derringer GA, Wenig BM. Amyloidosis of the larynx: A clinicopathologic study of 11 cases. Mod Pathol 2000;13:528-35.  Back to cited text no. 1
    
2.Walter JB, Israel MS. Amyloidosis (B- fibrillosis). In: General Pathology. 6 th ed. London: Churchill Livingstone; 1987. p. 606-12.  Back to cited text no. 2
    
3.Chen KT. Amyloidosis presenting in the respiratory tract. Pathol Annu 1989;24:253-73.   Back to cited text no. 3
    
4.Cengiz MÝ, Baðcý H, Bal S, Yiðit S, Cengiz K. Periodontal disease in familial Mediterranean fever patients: From inflammation to amyloidosis. J Periodontal Res 2009;44:354-61.   Back to cited text no. 4
    
5.Lachmann HJ, Goodman HJ, Gilbertson JA, Gallimore JR, Sabin CA, Gillmore JD, et al. Natural history and outcome in systemic AA amyloidosis. N Engl J Med 2007;356:2361-71.  Back to cited text no. 5
    
6.Urieli-Shoval S, Linke RP, Matzner Y. Expression and function of serum amyloid A, a major acute-phase protein, in normal and disease states. Curr Opin Hematol 2000;7:64-9.  Back to cited text no. 6
    


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  [Figure 1], [Figure 2]



 

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