TY - JOUR
T1 - Clinicopathologic and Proteomic Analysis of Amyloidomas Involving the Ocular Surface and Adnexa
AU - Jamshidi, Pouya
AU - Levi, Jonathan
AU - Suarez, Maria Jose
AU - Rivera, Roxana
AU - Mahoney, Nicholas
AU - Eberhart, Charles G.
AU - Rosenberg, Avi
AU - Rodriguez, Fausto J.
N1 - Publisher Copyright:
© 2021 American Society for Clinical Pathology, 2021. All rights reserved.
PY - 2022/4/1
Y1 - 2022/4/1
N2 - Objectives: Ocular amyloidoma is a rare disorder characterized by deposition of insoluble proteinaceous fibrils in the extracellular space of the ocular adnexa. This study details the clinicopathologic features and proteomic characteristics of periocular amyloid deposition. Methods: Specimens (1991-2020) were retrieved and reviewed. All available H&E slides and special stains were reviewed. Proteomic analysis was performed using immunohistochemistry (IHC) for IgG, IgG4, IgA, IgD, IgM, CD20, CD3, CD138, and κ/λ, as well as chromatography-electrospray tandem mass spectrometry on formalin-fixed, paraffin-embedded tissue. Results: There were 14 patients (7 men, 7 women). The depositions involved eyelid (n = 3), conjunctiva (n = 8), and orbit (n = 3). All patients were adults with a median age at diagnosis of 56 (range, 39-88) years. The deposits were predominantly λ light chain restricted (n = 6) and mixed light chains (n = 2), and one case was κ predominant. Two of the cases with a mixture of κ and λ light chains had an excess of transthyretin by mass spectrometry. Four of the cases did not have adequate material for proteomic subtyping. Conclusions: Amyloidomas involving ocular adnexa contain a variety of amyloid-related and immunoglobulin-associated peptides. The λ light chain predominates as in other body sites, but mixed patterns and rarely κ light chain restriction may be encountered.
AB - Objectives: Ocular amyloidoma is a rare disorder characterized by deposition of insoluble proteinaceous fibrils in the extracellular space of the ocular adnexa. This study details the clinicopathologic features and proteomic characteristics of periocular amyloid deposition. Methods: Specimens (1991-2020) were retrieved and reviewed. All available H&E slides and special stains were reviewed. Proteomic analysis was performed using immunohistochemistry (IHC) for IgG, IgG4, IgA, IgD, IgM, CD20, CD3, CD138, and κ/λ, as well as chromatography-electrospray tandem mass spectrometry on formalin-fixed, paraffin-embedded tissue. Results: There were 14 patients (7 men, 7 women). The depositions involved eyelid (n = 3), conjunctiva (n = 8), and orbit (n = 3). All patients were adults with a median age at diagnosis of 56 (range, 39-88) years. The deposits were predominantly λ light chain restricted (n = 6) and mixed light chains (n = 2), and one case was κ predominant. Two of the cases with a mixture of κ and λ light chains had an excess of transthyretin by mass spectrometry. Four of the cases did not have adequate material for proteomic subtyping. Conclusions: Amyloidomas involving ocular adnexa contain a variety of amyloid-related and immunoglobulin-associated peptides. The λ light chain predominates as in other body sites, but mixed patterns and rarely κ light chain restriction may be encountered.
KW - Adnexa
KW - Amyloid
KW - Immunoglobulin
KW - Mass spectrometry
KW - Ocular
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U2 - 10.1093/ajcp/aqab161
DO - 10.1093/ajcp/aqab161
M3 - Article
C2 - 34698334
AN - SCOPUS:85128161065
SN - 0002-9173
VL - 157
SP - 620
EP - 627
JO - American journal of clinical pathology
JF - American journal of clinical pathology
IS - 4
ER -