Amyloid in prostatic corpora amylacea. 1992

P A Cross, and C J Bartley, and J McClure
Department of Pathological Sciences, University of Manchester Medical School.

OBJECTIVE To determine the presence and nature of amyloid in prostatic corpora amylacea using immunohistological studies. METHODS Prostatic tissue from 18 transurethral and two open resection specimens was studied. Paraffin wax embedded tissue sections were stained with haematoxylin and eosin and the alkaline Congo red method with and without previous treatment with potassium permanganate. Sections were also stained with antibodies to amyloid A, beta 2 microglobulin, lambda and kappa light chains, prealbumin IgA, G, M, S100 protein, prostatic specific antigen, amyloid P component and CAM 5.2 (control and blocking studies were performed). RESULTS The prostatic corpora amylacea universally showed the presence of amyloid. In all instances this contained beta 2 microglobulin. CONCLUSIONS Prostatic corpora amylacea represents a localised amyloidosis of beta 2 microglobulin origin that is unrelated to chronic renal failure and haemodialysis.

UI MeSH Term Description Entries
D008297 Male Males
D011467 Prostate A gland in males that surrounds the neck of the URINARY BLADDER and the URETHRA. It secretes a substance that liquefies coagulated semen. It is situated in the pelvic cavity behind the lower part of the PUBIC SYMPHYSIS, above the deep layer of the triangular ligament, and rests upon the RECTUM. Prostates
D011469 Prostatic Diseases Pathological processes involving the PROSTATE or its component tissues. Disease, Prostatic,Diseases, Prostatic,Prostatic Disease
D011470 Prostatic Hyperplasia Increase in constituent cells in the PROSTATE, leading to enlargement of the organ (hypertrophy) and adverse impact on the lower urinary tract function. This can be caused by increased rate of cell proliferation, reduced rate of cell death, or both. Adenoma, Prostatic,Benign Prostatic Hyperplasia,Prostatic Adenoma,Prostatic Hyperplasia, Benign,Prostatic Hypertrophy,Prostatic Hypertrophy, Benign,Adenomas, Prostatic,Benign Prostatic Hyperplasias,Benign Prostatic Hypertrophy,Hyperplasia, Benign Prostatic,Hyperplasia, Prostatic,Hyperplasias, Benign Prostatic,Hypertrophies, Prostatic,Hypertrophy, Benign Prostatic,Hypertrophy, Prostatic,Prostatic Adenomas,Prostatic Hyperplasias, Benign,Prostatic Hypertrophies
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000682 Amyloid A fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease. Amyloid Fibril,Amyloid Fibrils,Amyloid Substance,Fibril, Amyloid,Fibrils, Amyloid,Substance, Amyloid
D001613 beta 2-Microglobulin An 11-kDa protein associated with the outer membrane of many cells including LYMPHOCYTES. It is the small subunit of MHC CLASS I MOLECULES. Association with beta 2-microglobulin is generally required for the transport of class I heavy chains from the endoplasmic reticulum to the cell surface. Beta 2-microglobulin is present in small amounts in serum, CEREBROSPINAL FLUID, and urine of healthy individuals, and to a much greater degree in the urine and plasma of patients with tubular PROTEINURIA, renal failure, or kidney transplants. Thymotaxin,beta 2 Microglobulin

Related Publications

P A Cross, and C J Bartley, and J McClure
July 1956, The Journal of urology,
P A Cross, and C J Bartley, and J McClure
January 1955, Transactions. American Urological Association. South Central Section,
P A Cross, and C J Bartley, and J McClure
January 1955, Postgraduate seminar. American Urological Association. North Central Section,
P A Cross, and C J Bartley, and J McClure
September 1966, Monographs in the surgical sciences,
P A Cross, and C J Bartley, and J McClure
January 1965, Surgical forum,
P A Cross, and C J Bartley, and J McClure
April 2003, International journal of surgical pathology,
P A Cross, and C J Bartley, and J McClure
January 1985, Applied pathology,
P A Cross, and C J Bartley, and J McClure
January 2010, Indian journal of pathology & microbiology,
P A Cross, and C J Bartley, and J McClure
January 1979, Scanning electron microscopy,
P A Cross, and C J Bartley, and J McClure
January 1972, Acta pathologica et microbiologica Scandinavica. Supplement,
Copied contents to your clipboard!