Macro-prostatic acid phosphatase in a patient's serum.

1988 ◽  
Vol 34 (10) ◽  
pp. 2172-2174 ◽  
Author(s):  
J A Schifferli ◽  
P Roth ◽  
G Steiger ◽  
J P Paccaud ◽  
M Schmidt

Abstract A patient without prostatic carcinoma had a high concentration of prostatic acid phosphatase (PAP; EC 3.1.3.2) in his serum. This PAP was bound to IgG ("macro-PAP"), and IgG autoantibodies against PAP were demonstrated in serum. The patient's IgG prolonged the biological half-life of radiolabeled PAP in rats, suggesting that the formation of IgG-PAP complexes was responsible for decreased PAP catabolism. Furthermore, macro-PAP was inactivated in serum more slowly than PAP. These factors accounted for the increases in the enzymatic activity and antigenic concentration of PAP measured in the patient's serum. Inappropriate therapy was prescribed on the basis of this laboratory result. The diagnosis of prostatic carcinoma requires clinical or histological evidence of malignant disease, and should not rely solely on PAP measurements.

Author(s):  
W. Allen Shannon ◽  
José A. Serrano ◽  
Hannah L. Wasserkrug ◽  
Anna A. Serrano ◽  
Arnold M. Seligman

During the design and synthesis of new chemotherapeutic agents for prostatic carcinoma based on phosphorylated agents which might be enzyme-activated to cytotoxicity, phosphorylcholine, [(CH3)3+NCH2CH2OPO3Ca]Cl-, has been indicated to be a very specific substrate for prostatic acid phosphatase (PAP). This phenomenon has led to the development of specific histochemical and ultracytochemical methods for PAP using modifications of the Gomori lead method for acid phosphatase. Comparative histochemical results in prostate and kidney of the rat have been published earlier with phosphorylcholine (PC) and β-glycerophosphate (βGP). We now report the ultracytochemical results.Minced tissues were fixed in 3% glutaraldehyde-0.1 M phosphate buffered (pH 7.4) for 1.5 hr and rinsed overnight in several changes of 0.05 M phosphate buffer (pH 7.0) containing 7.5% sucrose. Tissues were incubated 30 min to 2 hr in Gomori acid phosphatase medium (2) containing 0.1 M substrate, either PC or βGP.


1980 ◽  
Vol 7 (3) ◽  
pp. 645-652 ◽  
Author(s):  
Andrew W. Bruce ◽  
Donald E. Mahan ◽  
William D. Belville

2010 ◽  
Vol 134 (7) ◽  
pp. 983-988 ◽  
Author(s):  
Aaron M. Harvey ◽  
Beverly Grice ◽  
Candice Hamilton ◽  
Luan D. Truong ◽  
Jae Y. Ro ◽  
...  

Abstract Context.—Seminal vesicle invasion by prostatic carcinoma is directly associated with tumor staging; verification is challenging when the tumor demonstrates cribriform or papillary growth patterns or there are back-to-back small-gland proliferations. P504S is overexpressed in prostatic carcinoma and high-grade prostatic intraepithelial neoplasia with cytoplasmic immunoreactivity. p63 has positive immunoreactivity in basal cell nuclei of benign prostatic glands. Many researchers use a combination of these antibodies and their different colors. Objective.—To evaluate the usefulness of a single-color P504S/p63 cocktail immunostain in verifying prostatic carcinoma within the seminal vesicle. Design.—Sections from 57 radical prostatectomy specimens of pathologic stage pT3b that contain seminal vesicle with prostatic carcinoma involvement were immunostained with primary antibodies against prostate-specific antigen (PSA) and prostatic acid phosphatase (PAP) and a cocktail of antibodies against P504S and p63. Results.—Prostatic carcinoma cells from all 57 cases were diffusely positive for P504S, PSA, and PAP with cytoplasmic staining and no p63 nuclear staining. Seminal vesicle epithelium from all 57 cases was negative for all 3 markers with distinct p63 nuclear staining of the basal cells. Benign prostatic tissue was positive for PSA and PAP, as well as for p63, but negative for P504S. Conclusions.—The P504S/p63 one-color cocktail is a practical and cost-effective stain to differentiate prostatic carcinoma that involves the seminal vesicle from seminal vesicle epithelium. It is superior to PSA or PAP when sections contain both seminal vesicle and benign glands because PSA and PAP cannot distinguish benign from malignant glands.


The Prostate ◽  
1991 ◽  
Vol 19 (3) ◽  
pp. 265-272 ◽  
Author(s):  
Hideki Sakai ◽  
Kazutaka Shiraishi ◽  
Yuzo Minami ◽  
Yoshiaki Yushita ◽  
Hiroshi Kanetake ◽  
...  

1985 ◽  
Vol 13 (3) ◽  
Author(s):  
J. Wadstr�m ◽  
M. Wenk ◽  
P. Huber

1980 ◽  
Vol 26 (11) ◽  
pp. 1544-1547 ◽  
Author(s):  
P Vihko ◽  
A Kostama ◽  
O Jänne ◽  
E Sajanti ◽  
R Vihko

Abstract We describe a rapid radioimmunoassay for human prostatic acid phosphatase (EC 3.1.3.2) in serum, with use of monospecific antisera raised in rabbits against the primary highly purified acid phosphatase (pl 4.9) from human prostates, and with a second antibody-polyethylene glycol porecipitation. This radioimmunoassay is sensitive and can be performed within 5 h. Concentrations of the immunoreactive acid phosphatase in sera of healthy men (n = 394) ranged from 0.3 to 3.6 microgram/L (mean 1.94, SD 0.66 microgram/L). Concentrations of the enzyme in sera of men with benign prostatic hyperplasia (n = 56) or with carcinoma of nonprostatic origin (n = 24) were identical with those of the reference group. Serum concentrations of immunoreactive prostatic acid phosphatase of patients with occult, non-metastatic, and metastatic prostatic carcinoma varied from 1.7 to 9.3 (n = 9), 4.2 to 59.4 (n = 12), and 20 to 198 (n = 10) microgram/L, respectively. The amount of immunoassayable prostatic acid phosphatase was unchanged for at least five days in serum stored at 4 degrees C.


1983 ◽  
Vol 55 (3) ◽  
pp. 306-311 ◽  
Author(s):  
SOPHIE DOROTHEA FOSSA ◽  
A. SKINNINGSRUD ◽  
O. KAALHUS ◽  
A. ENGESET

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