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Iocalized amyloidosis of the seminal vesicle: Identification of lactoferrin immunoreactivity in the amyloid material
Author(s) -
Tsutsumi Yutaka,
Serizawa Akihiko,
Hori Sadaaki
Publication year - 1996
Publication title -
pathology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.73
H-Index - 74
eISSN - 1440-1827
pISSN - 1320-5463
DOI - 10.1111/j.1440-1827.1996.tb03643.x
Subject(s) - lactoferrin , seminal vesicle , pathology , amyloidosis , amyloid (mycology) , chemistry , immunoelectron microscopy , prostate , biology , immunohistochemistry , biochemistry , medicine , cancer
Three specimens of localized amyloidosis of the seminal vesicle surgically removed for prostatic cancer were immuno‐histochemically analyzed to clarify the nature of the permanganate‐sensitive congophilic subeplthelial deposition. A variety of known amyloidogenic substances and secretory products in the seminal fluid were screened using the indirect immunoperoxldase 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 iron‐binding, bacteriostatJc 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.