{'fraction_non_alphanumeric': 0.040341578327444054, 'fraction_numerical': 0.011189634864546525, 'mean_word_length': 5.279112754158965, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Vesicular senile systemic amyloidosis

Senile systemic amyloidosis (SSA) typically occurs in men over 60 years of age and the pathologic deposits are composed of wild-type (i.e. unmutated) transthyretin (TTR). Most often, the heart represents the principal site of deposition, though, less commonly, the lung may be involved. We now report a case of SSA in an 81-year-old Caucasian male in whom the urinary bladder was the major organ affected. Chemical characterization of amyloid extracted from a submucosal lesion showed the presence of native TTR-related peptides and analyses of the patient’s serum and TTR-encoding DNA revealed that the fibrils were derived from unmutated protein. Taken together, our findings provide confirmatory evidence of an unusual (i.e. non-cardiac) form of SSA. Introduction: Senile systemic amyloidosis (SSA) results from the pathologic deposition of unmutated (wild-type) transthyretin (TTR), mainly in the heart and, less commonly, the lung [1,2]. This process typically is associated with aging (460 years) and, as shown at autopsy, the frequency of cardiac deposits can be as high as 25% [3], though SSA TTR-related amyloid also occurs in the renal papilla and walls of small arteries [2]. We now report that the amyloid found in the bladder of an elderly male was composed of unmutated TTR. Methods: Case report: An 81-year-old male was referred for urologic examination due to sudden onset of gross hematuria. Ten years previously, he had received interstitial brachytherapy for a prostatic adenocarcinoma; in the interim, there were no signs of recurrence. Cystoscopy revealed patchy, erythematous, raised submucosal lesions throughout the bladder, which biopsy proved to be amyloid. There was no evidence of radiation-induced cystitis. Other diagnostic studies included 2D electrocardiogram (Interventricular septum (IVS) 1⁄4 1.3 cm) and chest CT. Amyloid fibrils, extracted with 8 M Gu/HCl from 4 mm-thick sections cut from the biopsy-derived, formalin-fixed, paraffin-embedded block, were reduced and alkylated, digested with trypsin, and the resultant peptides analyzed by tandem mass spectrometry (MS/MS), as detailed previously [4]. For immunohistochemistry, deparaffinized sections were subjected to antigen retrieval by boiling in Citra-Plus and then incubated overnight at 48C with a goat anti-human TTR antibody, followed by exposure to a biotinylated anti-goat IgG reagent, and then to streptavidin horseradish peroxidase (HRP). The reaction was developed with ImmPACT diaminobenzidine. The patient’s serum TTR was isolated by immunoprecipitation using an anti-TTR antibody and, after disassociation, was subjected to mass spectrometry (MS/MS). Genomic DNA was obtained from peripheral blood leukocytes and amplified by PCR using primers specific for TTRencoding exons 2, 3, and 4 [5]. The resultant products were sequenced at the University of Tennessee’s Molecular Biology Facility. Results and discussion: As illustrated in Figure 1, examination by polarizing microscopy of the Congored-stained bladder biopsy sections revealed the presence of extensive congophilic deposits that exhibited the characteristic tinctorial feature of amyloid and, further, were immunostained by an Figure 1. Left: Congo red stain of bladder biopsy, and Right: immunostaining of the amyloid by an anti-TTR antiserum (ABC method). Original magnifications,6 100. 178