Prostatic Acid Phosphatase (PAP) Differentiated Ultracytochemically from Lysosomal Acid Phosphate in the Rat with a PAP/Specific Substrate, Phosphorylcholine

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.

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The Demonstration of Human Prostatic Acid Phosphatase (Pap) With Phosphorylcholine

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100090427 ◽

1976 ◽

Vol 34 ◽

pp. 88-89

Author(s):

José A. Serrano ◽

Hannah L. Wasserkrug ◽

Anna A. Serrano ◽

Arnold M. Seligman

Keyword(s):

Acid Phosphatase ◽

Prostate Gland ◽

Prostatic Acid Phosphatase ◽

Human Prostate ◽

Rat Tissues ◽

Specific Substrate ◽

Acid Phosphatases ◽

Lysosomal Acid ◽

Cacodylate Buffer

As previously reported (1, 2) phosphorylcholine (PC) is a specific substrate for prostatatic acid phosphatase (PAP) as opposed to other acid phosphatases, e.g., lysosomal acid phosphatase. The specificity of PC for PAP is due to the pentavalent nitrogen in PC, a feature that renders PC resistant to hydrolysis by all other acid phosphatases. Detailed comparative cytochemical results in rat tissues are in press. This report deals with ultracytochemical results applying the method to normal and pathological human prostate gland.Fresh human prostate was obtained from 7 patients having transurethral resections or radical prostatectomies. The tissue was fixed in 3% glutaraldehyde- 0.1 M cacodylate buffer (pH 7.4) for 15 min, sectioned at 50 μm on a Sorvall TC-2 tissue sectioner, refixed for a total of 2 hr, and rinsed overnight in 0.1 M cacodylate buffer (pH 7.4)-7.5% sucrose.

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Diagnostic Value of Prostatic Acid Phosphatase (Pap) and Prostate-Specific Antigen (Psa) in Patients with Prostatic Cancer

Urologia Journal ◽

10.1177/039156039205900126 ◽

1992 ◽

Vol 59 (1) ◽

pp. 101-103

Author(s):

T. Zambolin ◽

L. Tralce ◽

A. Cozzoli ◽

E. Frego ◽

C. Simeone ◽

...

Keyword(s):

Acid Phosphatase ◽

Prostatic Carcinoma ◽

Specific Antigen ◽

Prostatic Acid Phosphatase ◽

Diagnostic Value ◽

High Risk Population ◽

Specific Substrate ◽

Clinical Value ◽

Receiver Operating Characteristic Curves ◽

Clinical Accuracy

Prostatic acid phosphatase (PAP) and specific prostatic antigen (PSA) in the serum of patients with prostatic carcinoma were determined and their clinical value compared. 128 patients were examined, 60 (46.9%) of whom had prostatic carcinoma (4 in stage T2, 27 in T3 and 29 in T4) and 68 with benign prostatic pathology. ROC (receiver operating characteristic) curves were plotted from resulting data and the underlying areas calculated to evaluate the clinical accuracy of the two markers. The area for PSA (0.90 +/-0.03) was significantly greater than that for PAP (0.71 +/-0.05), showing that PSA was better at detecting patients with or without prostatic carcinoma. Maximum clinical accuracy was 0.883 obtained with discriminating values of 0.8 U/L for PAP and 10 ug/L for PSA, confirming the superiority of PSA. However, PAP determination using thymolphthalein monophosphate as the specific substrate for the prostatic isoenzyme, showed greater clinical specificity (98.5%) so that association of the two markers made it possible to eliminate false positive results. In conclusion, results suggest the possibility of using PSA for diagnosing prostatic carcinoma in a selected high risk population. However, the simplicity of the method used for determining PAP and the greater clinical specificity of PAP and PSA combined, suggest determining both parameters for diagnostic purposes.

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The Role of the Radioimmunoassay for Prostatic Acid Phosphatase in Prostatic Carcinoma

Urologic Clinics of North America ◽

10.1016/s0094-0143(21)00153-1 ◽

1980 ◽

Vol 7 (3) ◽

pp. 645-652 ◽

Cited By ~ 1

Author(s):

Andrew W. Bruce ◽

Donald E. Mahan ◽

William D. Belville

Keyword(s):

Acid Phosphatase ◽

Prostatic Carcinoma ◽

Prostatic Acid Phosphatase

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Diagnostic Utility of P504S/p63 Cocktail, Prostate-Specific Antigen, and Prostatic Acid Phosphatase in Verifying Prostatic Carcinoma Involvement in Seminal Vesicles: A Study of 57 Cases of Radical Prostatectomy Specimens of Pathologic Stage pT3b

Archives of Pathology & Laboratory Medicine ◽

10.5858/2009-0277-oa.1 ◽

2010 ◽

Vol 134 (7) ◽

pp. 983-988 ◽

Cited By ~ 2

Author(s):

Aaron M. Harvey ◽

Beverly Grice ◽

Candice Hamilton ◽

Luan D. Truong ◽

Jae Y. Ro ◽

...

Keyword(s):

Acid Phosphatase ◽

Radical Prostatectomy ◽

Seminal Vesicle ◽

Prostate Specific Antigen ◽

Prostatic Carcinoma ◽

Specific Antigen ◽

Prostatic Acid Phosphatase ◽

Growth Patterns ◽

Nuclear Staining ◽

Pathologic Stage

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.

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High Degree of Homology Between Primary Structure of Human Lysosomal Acid Phosphatase and Human Prostatic Acid Phosphatase

Biological Chemistry Hoppe-Seyler ◽

10.1515/bchm3.1989.370.1.177 ◽

1989 ◽

Vol 370 (1) ◽

pp. 177-182 ◽

Cited By ~ 16

Author(s):

Christoph PETERS ◽

Carola GEIER ◽

Regina POHLMANN ◽

Abdul WAHEED ◽

Kurt VON FIGURA ◽

...

Keyword(s):

Acid Phosphatase ◽

Primary Structure ◽

Prostatic Acid Phosphatase ◽

Lysosomal Acid ◽

High Degree

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Immunohistochemical prostatic acid phosphatase level as a prognostic factor of prostatic carcinoma

The Prostate ◽

10.1002/pros.2990190307 ◽

1991 ◽

Vol 19 (3) ◽

pp. 265-272 ◽

Cited By ~ 20

Author(s):

Hideki Sakai ◽

Kazutaka Shiraishi ◽

Yuzo Minami ◽

Yoshiaki Yushita ◽

Hiroshi Kanetake ◽

...

Keyword(s):

Acid Phosphatase ◽

Prognostic Factor ◽

Prostatic Carcinoma ◽

Prostatic Acid Phosphatase

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

Clinical Chemistry ◽

10.1093/clinchem/34.10.2172 ◽

1988 ◽

Vol 34 (10) ◽

pp. 2172-2174 ◽

Cited By ~ 3

Author(s):

J A Schifferli ◽

P Roth ◽

G Steiger ◽

J P Paccaud ◽

M Schmidt

Keyword(s):

Acid Phosphatase ◽

Enzymatic Activity ◽

Half Life ◽

Prostatic Carcinoma ◽

Malignant Disease ◽

Prostatic Acid Phosphatase ◽

Inappropriate Therapy ◽

Laboratory Result ◽

High Concentration ◽

Histological Evidence

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.

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Rapid radioimmunoassay for prostate-specific acid phosphatase in human serum.

Clinical Chemistry ◽

10.1093/clinchem/26.11.1544 ◽

1980 ◽

Vol 26 (11) ◽

pp. 1544-1547 ◽

Cited By ~ 33

Author(s):

P Vihko ◽

A Kostama ◽

O Jänne ◽

E Sajanti ◽

R Vihko

Keyword(s):

Acid Phosphatase ◽

Benign Prostatic Hyperplasia ◽

Prostatic Carcinoma ◽

Reference Group ◽

Prostatic Acid Phosphatase ◽

Prostatic Hyperplasia ◽

Serum Concentrations ◽

Healthy Men ◽

Monospecific Antisera ◽

Group Serum

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.

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