Localized amyloidosis of seminal vesicles: report of three cases in surgically obtained material.
ABSTRACT Localized amyloidosis of the seminal vesicles (ASV) is reported as an incidental finding in surgical specimens from three elderly men. In two cases, the amyloid deposits were bilateral, subepithelial, and clinically inapparent, features similar to other cases in the literature. In one case, the diagnosis was made on a transrectal prostatic needle biopsy that included a small portion of seminal vesicle; to our knowledge, this has not been previously reported. Electron microscopy in one case demonstrated nonbranching fibrils characteristic of amyloid, and pretreatment of tissue sections using the permanganate method in two cases showed almost complete ablation of congophilia. Evidence suggests that ASV is a permanganate-sensitive, non-AA (amyloid, protein A) type of amyloid that may be different from all other types of amyloid previously characterized.
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ABSTRACT: Three specimens of localized amyloidosis of the seminal vesicle surgically removed for prostatic cancer were immunohistochemically analyzed to clarify the nature of the permanganate-sensitive congophilic subepithelial deposition. A variety of known amyloidogenic substances and secretory products in the seminal fluid were screened using the indirect immunoperoxidase method. In addition to reactivities with antibodies to amyloid P component and human seminal plasma, the amyloid material was immunoreactive for lactoferrin using a rabbit antiserum and two of three mouse monoclonal antibodies. All the antibodies labeled some of the normal seminal vesicle epithelial cells for this ironbinding, bacteriostatic glycoprotein. In the prostate without accompanying amyloid deposition, a considerable proportion of the glandular epithelium and secretory material were positive for lactoferrin. Pre-embedding immunoelectron microscopy showed lactoferrin immunoreactivity on the amyloid fibrils. Focal staining of the amyloid for gross cystic disease fluid protein-15 was also observed in two lesions. These findings strongly suggest that lactoferrin is the major constituent in localized senile amyloidosis of the seminal vesicle.Pathology International 08/1996; 46(7):491-7. · 1.59 Impact Factor
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ABSTRACT: Amyloidosis is a rare disease with various etiologies with extracellular amyloid protein depositions. At present, at least 26 distinctive amyloid forms have been detected with different clinical importance and treatment. They have characteristic staning fetaures with Congo red. Amyloid may be detected in 2-10% of prostates that have been removed because of hyperplasia or carcinoma. Amyloidosis of seminal vesicles is accepted as senil amyloidosis and it is not accompanied by systemic amyloidosis or clinical symptoms. This condition is the most common form of localized amyloidosis. In this study we aimed to investigate incidence and histologic characteristics of amyloidosis of seminal vesicles in radical prostatectomy materials of the patients whose prostate carcinomas were treated surgically. Amyloid depositions in seminal vesicles of 207 radical prostatectomy materials that prostates had been removed due to localized prostate carcinoma. Amyloid depositions were confirmed with Congo red staining and polarization microscope. Amyloidosis of seminal vesicles was detected in 10 (4.8%) of cases. Mean age of the patients is 66.2 years. Amyloid depositions tend to be nodular and bilateral in subepithelial region of affected seminal vesicles. Amyloid depositions were not detected in blood vessels in seminal vesicles or prostate parenchyma. Localized amyloidosis of seminal vesicles is not an unusual finding. amyloidosis of seminal vesicles incidence in Turkish patients included in this study and histopathologic characteristics of these patients are not different from the other studies. Systemic AA amyloidosis is the most common form of amyloidosis in our country. To be aware of amyloidosis of seminal vesicles is of importance in discrimination from the other forms of amyloidosis.Turk Patoloji Dergisi 01/2012; 28(1):44-8.