acid-phosphatase and Prostatic-Diseases

The prostate gland secretes many proteins in a prostatic fluid that combines with seminal vesicle derived fluids to promote sperm activation and function. Proximal fluids of the prostate that can be collected clinically are seminal plasma and expressed-prostatic secretion (EPS) fluids. EPS represents the fluid being secreted by the prostate following a digital rectal prostate massage, which in turn can be collected in voided urine post-exam. This collection is not disruptive to a standard urological exam, and it can be repeatedly collected from men across all prostatic disease states. A direct EPS fluid can also be collected under anesthesia prior to prostatectomy. While multiple genetic assays for prostate cancer detection are being developed for the shed epithelial cell fraction of EPS urines, the remaining fluid that contains many prostate-derived proteins has been minimally characterized. Approaches to optimization and standardization of EPS collection consistent with current urological exam and surgical practices are described, and initial proteomic and glycomic evaluations of the of EPS fluid are summarized for prostate specific antigen and prostatic acid phosphatase. Continued characterization of the prostate specific protein components of EPS urine combined with optimization of clinical collection procedures should facilitate discovery of new biomarkers for prostate cancer.

Topics: Acid Phosphatase; Biomarkers; Body Fluids; Electrophoresis, Gel, Two-Dimensional; Epithelial Cells; Gene Expression Regulation, Neoplastic; Glycomics; Humans; Male; Prostate; Prostatic Diseases; Prostatic Neoplasms; Protein Tyrosine Phosphatases; Proteomics; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Time Factors

Acid phosphatase is a ubiquitous lysosomal enzyme that hydrolyses organic phosphates at an acid pH. Although the postpuberteral prostatic epithelial cell contains a uniquely high concentration of acid phosphatase, cellular components of bone, spleen, kidney, liver, intestine, and blood also contain this enzyme. The discovery that prostatic carcinoma cells often retain a high concentration of acid phosphatase characteristic of the normal postpubertal gland led to the recognition of the first clinically useful tumor marker. Recognition that the serum of patients with prostatic malignancy frequently contains an increased concentration of this enzyme has resulted in persistent efforts to identify the source, to accurately quantitate the level of serum acid phosphatase, and to determine the clinical significance of those levels. A variety of enzymatic and immunologic techniques have been employed to measure acid phosphatase. In the past, various substrates and inhibitors were utilized to increase specificity and sensitivity. Emphasis has now shifted to the development of radioimmunoassay and counterimmunoelectrophoresis in an attempt to enhance those parameters. Judgment of their efficacy awaits further testing and evaluation. The clinical significance of normal and abnormal serum acid phosphatase is constantly being reevaluated. In order to maximize the value of laboratory measurements, the clinical and pathologic status of the patient, the techniques employed in obtaining and storing the blood sample and the procedures used in analysis must be known and considered. Traditionally, the serum prostatic acid phosphatase has been thought to originate in the prostatic cancer cell and has been used to stage the disease. Until recently, elevated serum values have been accepted as an indication of extraprostatic disease, and were thought to rule out lesions confined to the prostate. The elevation of acid phosphatase levels in patients with disseminated disease or the failure of elevated levels to return to normal with treatment have been assumed to indicate a poor prognosis. However, unequivocal documentation of the validity of these statements is not available. Newer immunologic techniques for measuring acid phosphatase may significantly alter our current concept of its role as a tumor marker.

Topics: Acid Phosphatase; Bone Marrow; Clinical Enzyme Tests; Counterimmunoelectrophoresis; Humans; Male; Prostatic Diseases; Prostatic Neoplasms; Radioimmunoassay

Topics: Acid Phosphatase; Aged; Aged, 80 and over; Biomarkers; Case-Control Studies; Chronic Disease; Humans; Kidney Diseases; Male; Middle Aged; Predictive Value of Tests; Prostate-Specific Antigen; Prostatic Diseases; Protein Tyrosine Phosphatases; Up-Regulation

In 6 patients, ranging in age from 26 to 71 years, we analyzed aspirated fluid and histologically studied cystic lesions located at the midline of the prostate.. Digital rectal examination, ultrasonography, magnetic resonance imaging, and aspiration of cystic fluid were performed to evaluate size, contents, and location of the cystic lesion. A 22-gauge needle was inserted into the cystic lesion perineally under ultrasound guidance. After extracting fluid for cytology and measurement of prostate-specific antigen (PSA) and prostatic acid phosphatase (PAP), a specimen from the prostate involving the cystic wall was collected. Hematoxylin-eosin staining and immunohistochemical staining for PSA were performed.. All aspirated fluid specimens were yellowish and clear without any sperm or malignant cells. The PSA levels in the fluid ranged between 90 and 670 x 10(4) ng/ml, while the PAP levels were between 168 and 4,000 ng/ml. These levels of PSA and PAP were significantly higher as compared with those in the serum. The cystic wall was lined with cuboidal or columnar epithelium. Some epithelial cells from the cystic wall showed positive immunostaining for PSA.. Not all cystic lesions located at the midline of the prostate are müllerian duct cysts, and there is a high probability that the lesion could be a cystadenoma or a simple cyst of the prostate.

Topics: Acid Phosphatase; Adult; Aged; Anti-Bacterial Agents; Biopsy, Needle; Body Fluids; Cysts; Endosonography; Follow-Up Studies; Humans; Magnetic Resonance Imaging; Male; Middle Aged; Minocycline; Mullerian Ducts; Prostate; Prostate-Specific Antigen; Prostatic Diseases; Retrospective Studies

The prostate gland normally secretes neutral mucosubstances that can be detected within the lumina of acini and ducts; adenocarcinomas often produce both acidic and neutral mucins, a feature that has been suggested to be of some diagnostic use. The presence of mucin-filled cells is not, however, a feature of the normal prostate. Over the last few years, we have observed tall, columnar, mucin-secreting cells in a variety of conditions in 12 benign prostates. All cases were stained histochemically for mucin with Mayers' mucicarmine, alcian blue (pH 2.7), and periodic-acid-Schiff with diastase digestion. In four cases, immunoperoxidase stains for prostate-specific antigen (PSA) and prostatic acid phosphatase (PAP) were performed. Mucin-secreting cells were found in the foci of sclerotic atrophy (n = 5), transitional cell metaplasia (n = 3), basal cell hyperplasia (n = 2), prostatrophic hyperplasia (n = 1), and nodular hyperplasia (n = 1). In all examples, the cells stained intensely with PAS, mucicarmine, and alcian blue. The cells were nonreactive for PSA and PAP in the cases studied. To our knowledge, the presence of tall, columnar, mucin-secreting cells has not been previously described in atrophy or basal cell hyperplasia. These observations expand our appreciation of the histologies that may be seen in the prostate gland; in addition, the recognition of acidic mucin-secreting cells in benign lesions points to the nonspecificity of this finding in the diagnosis of malignancy.

Topics: Acid Phosphatase; Atrophy; Humans; Hyperplasia; Male; Metaplasia; Mucins; Prostate; Prostate-Specific Antigen; Prostatic Diseases

Sclerosing adenosis of the prostate is a rare lesion characterized by the proliferation of variably sized glands in a cellular stroma. We report light microscopic, immunohistochemical, and ultrastructural studies in 22 examples from 15 patients. Two cases were identified in 100 consecutive prostates embedded by a whole organ method, giving a prevalence of 2%. Antibodies directed against the following antigens were used: high-molecular-weight cytokeratin (CKH; 34 beta E12); cytokeratin (CK; AE1/AE3), prostatic acid phosphatase (PAP), prostate-specific antigen (PSA), S-100 protein, muscle-specific actin (HHF35), and vimentin (Vim). Cells within the glandular component demonstrated positive reactivity for CK, CHH, PSA, and PAP, indicating a prostatic epithelial origin. In addition, a distinct population of cells reacting for muscle-specific actin and S-100 protein was identified within this glandular element. Adequate material for ultrastructural study was available in five cases; all showed the presence of flattened cells located between the basement membrane and secretory epithelial cells, which had features typical for myoepithelial differentiation. Although the prostate gland does not normally contain myoepithelial cells, we have documented their consistent presence in this unusual lesion; we believe these cells arise by a metaplastic process from the prostatic basal cells.

Topics: Acid Phosphatase; Actins; Aged; Aged, 80 and over; Antigens, Neoplasm; Cell Differentiation; Epithelium; Humans; Immunohistochemistry; Keratins; Male; Microscopy, Electron; Middle Aged; Muscles; Prostate; Prostate-Specific Antigen; Prostatic Diseases; S100 Proteins; Sclerosis; Vimentin

We determined the pre-analytical and biological variation of prostatic acid phosphatase and prostate-specific antigen in the same patient samples. Prostatic acid phosphatase and prostate-specific antigen were both stable when stored for at least 3 weeks with acidification (acetate buffer) or without acidification, except for prostate-specific antigen in samples stored unacidified at 4 degrees C. A significant elevation of prostate-specific antigen was noted in four patients with benign prostatic hyperplasia between 1/2 and 6 hours after prostatic massage. No significant effect was shown of changes in the glomerular filtration rate on prostate-specific antigen concentration, in spite of its low molecular mass. The estimate of within-subject biological variation showed a coefficient of variation of 33.8% for prostatic acid phosphatase and 14% for prostate-specific antigen. Desirable analytical imprecisions based on these findings were about 17% for prostatic acid phosphatase and 7% for prostate-specific antigen, these goals being achieved in practice for marker values higher than or equal to the upper reference limit.

Topics: Acid Phosphatase; Adenocarcinoma; Antigens, Neoplasm; Biomarkers, Tumor; Glomerular Filtration Rate; Humans; Male; Physical Examination; Prostate-Specific Antigen; Prostatic Diseases; Prostatic Hyperplasia; Prostatic Neoplasms

A prostatic lesion, histologically identical to sclerosing adenosis of the breast, was found in five (1.9%) of 263 patients who underwent transurethral resection, open prostatic adenectomy, radical prostatectomy, or total cystoprostatectomy. This uncommon lesion was a localized proliferation of crowded small glands, small solid nests, and individual cells embedded in a cellular stroma, mimicking a small acinar prostatic adenocarcinoma. The proliferating glands were lined by a single layer of secretory cells surrounded by an eosinophilic membranous structure. Basal cells were disclosed in individual glands or as small nests and even individual cells with immunostainability for basal cell-specific cytokeratin (EAB903), S-100 protein, and muscle-specific actin (HHF35). These findings indicate the benign nature of the lesion with myoepithelial differentiation of the basal cells. In contrast, all 25 small acinar adenocarcinomas examined as controls lacked positive stains for the above three antibodies, verifying the usefulness of these antibodies to distinguish between this benign lesion from adenocarcinoma.

Topics: Acid Phosphatase; Actins; Adenocarcinoma; Aged; Aged, 80 and over; Antigens, Neoplasm; Diagnosis, Differential; Humans; Immunohistochemistry; Keratins; Male; Prostate-Specific Antigen; Prostatic Diseases; Prostatic Neoplasms; S100 Proteins; Sclerosis

To study the significance of prostatic acid phosphatase (PAP), gamma-seminoprotein (gamma-Sm) and prostatic specific antigen (PA) in urine, we have determined the urinary levels of these proteins in women and infants, in patients without prostatic disease, in patients with benign prostatic hypertrophy, and in patients with prostatic adenocarcinoma. Women and infants were found to excrete little PAP (27.9 +/- 4.8 ng/mg) and undetectable levels of gamma-Sm except one case, and undetectable levels of PA in the urine. The excretion of PAP in patients with prostatic carcinoma who were either castrated, or treated with endocrine therapy was lower than the levels in women and infants, or the levels in patients without prostatic diseases, or the levels in patients with BPH. Urinary excretion levels of gamma-Sm and PA were undetectable in the patients with well-controlled prostatic carcinoma. The present study suggests that the determination of PAP, gamma-Sm and PA in the urine of patients with prostatic carcinoma may become a useful tool for monitoring of the primary locus of the carcinoma, but additional assays of urinary PAP, gamma-Sm and PA should be measured at regular intervals to be concluded.

Topics: Acid Phosphatase; Adenocarcinoma; Adolescent; Adult; Aged; Aged, 80 and over; Antigens, Neoplasm; Biomarkers, Tumor; Child; Child, Preschool; Female; Humans; Male; Middle Aged; Prostate; Prostate-Specific Antigen; Prostatic Diseases; Prostatic Hyperplasia; Prostatic Neoplasms; Prostatic Secretory Proteins; Proteins; Seminal Plasma Proteins

The concentrations of three secretory proteins of the human prostate, including prostatic secretory protein of 94 amino acid residues (PSP94), prostate-specific antigen (PSA) and prostatic acid phosphatase (PAP), were measured by enzyme-linked immunosorbent assay (ELISA) in semen from a collective of patients suffering from various inflammatory diseases of the genital tract. In addition, levels of the conventional markers citrate, glucosidase and fructose were determined. As compared with semen from men exhibiting no inflammatory condition, only levels of glucosidase in cases of epididymitis and concentrations of PSP94 in the collective suffering from prostatitis showed significant reductions. The changes in the secretion of PSA, PAP, fructose and citrate in the semen of patients with inflammation of genital tract tissue were not significant at the 95% range of confidence.

Topics: Acid Phosphatase; Antigens, Neoplasm; Biomarkers; Carrier Proteins; Citrates; Citric Acid; Enzyme-Linked Immunosorbent Assay; Fructose; Genital Diseases, Male; Glucosidases; Humans; Male; Prostate; Prostate-Specific Antigen; Prostatic Diseases; Prostatic Secretory Proteins; Semen

The authors analyzed 3,079 serum determinations for prostate specific antigen (PSA) and prostatic acid phosphatase (PAP) that had been performed in 1,470 patients. The control group was comprised of 370 patients, 444 comprised the patient group with benign non-prostatic disease, 201 had malignant nonprostatic disease, 290 had benign prostatic disease (85 uncomplicated benign prostatic hypertrophy, 125 complicated benign prostatic hypertrophy, 50 acute prostatitis, 30 chronic prostatitis), 78 had untreated prostate carcinoma, and 165 were patients with prostate carcinoma under treatment. Quantification of PSA and PAP was performed by double antibody radioimmunoassay. The upper limit for normal values was set at 10 ng/ml. for PSA and 2.5 ng/ml. for PAP. Statistical analyses were performed with a personal computer using the SPSC program. Non-parametric tests were utilized throughout in the absence of a normal distribution of values for both tumor markers. In the control group, no significant differences in PSA and PAP levels were observed relative to the age group for the female patients; however, for the male patients, a significant increase was observed after age 15 for both markers. Furthermore, after age 50 PAP values became stable whereas a slight increase was observed for PSA. With regard to tumor mass, a significant correlation was found between PSA levels and the different patient groups while no remarkable differences were observed for PAP levels in those patients without or with single metastasis. We can conclude from the foregoing findings that PSA is currently the most useful tumor marker in diagnosing, staging, and monitoring prostate cancer. However, we believe that PSA and PAP are different manifestations of the prostate cell.(ABSTRACT TRUNCATED AT 250 WORDS)

Topics: Acid Phosphatase; Antigens, Neoplasm; Biomarkers, Tumor; Carcinoma; Female; Humans; Male; Prostate; Prostate-Specific Antigen; Prostatic Diseases; Prostatic Neoplasms

The daily variation of serum levels of prostate-specific antigen (PSA) and prostatic acid phosphatase (PAP) was investigated simultaneously in 10 patients with osseous metastatic prostatic cancer, 10 patients with benign prostatic hyperplasia, and 10 volunteers without prostatic disease. Duplicate serum samples were obtained from all patients on the same day at 8 AM, 12 PM, 4 PM, and 8 PM. Statistical analysis (two-factor analysis of variance comparing time period to disease group) of the mean PSA and PAP levels at the four sampling times on all patient groups demonstrated no evidence of circadian rhythmic variation or any other distinct pattern for the observed sample times. Overall, the variability in PSA levels was significantly less than that observed for PAP. There was no significant difference in mean percent variation between patient groups (cancer, benign, and normal prostate glands) for both the PSA and PAP assays. Our data reveal that serum PSA measurements fluctuate unpredictably over the course of a day in patients with and without prostatic disease, but to a lesser extent than that seen for serum PAP values. These findings illustrate the potential inaccuracy of single determinations of serum PAP or PSA levels for monitoring disease recurrence and treatment response in patients with prostate cancer.

Topics: Acid Phosphatase; Aged; Antigens, Neoplasm; Circadian Rhythm; Humans; Male; Middle Aged; Prostate; Prostate-Specific Antigen; Prostatic Diseases; Prostatic Hyperplasia; Prostatic Neoplasms

Topics: Acid Phosphatase; Blood Preservation; Clinical Enzyme Tests; Freezing; Humans; Kinetics; Male; Prostate; Prostatic Diseases

A 55-year-old man was admitted to our hospital because of pollakisuria and dysuria. Rectal examination revealed a normal prostate and did not show fluctuation or tenderness. Cystography and cystoscopic examination revealed a lesion projecting into the bladder cavity. An echogram showed an irregular internal echo at the left lobe of the prostate, but prostatic biopsy revealed benign prostatic hypertrophy. Transvesical removal of the prostatic cyst was performed. The cyst was about 3 cm in diameter and filled with yellow fluid (5.8 ml). The fluid contained no sperm and its acid phosphatase and zinc levels were high. The cystic wall was lined by cubo-collumnar cells and partly by flattened epithelium.

Topics: Acid Phosphatase; Cystoscopy; Cysts; Cytodiagnosis; Humans; Male; Middle Aged; Prostatic Diseases; Ultrasonography; Urodynamics

Topics: Acid Phosphatase; Aged; Colorimetry; Humans; Immunoenzyme Techniques; Male; Prostatic Diseases; Radioimmunoassay; Reagent Kits, Diagnostic

We evaluated the distribution of values for prostatic acid phosphatase (EC 3.1.3.2) activity and zinc concentration in semen of 80 men without clinical evidence of prostatic disease. Both substances have log normal distributions. Reference intervals were defined by parametric tests after logarithmic transformation of data and by nonparametric tests. There is a correlation between zinc concentration and prostatic acid phosphatase activity in semen.

Topics: Acid Phosphatase; Adult; Humans; Male; Middle Aged; Prostatic Diseases; Reference Values; Semen; Zinc

Flow cytometry can differentiate benign from malignant lesions of the prostate through deoxyribonucleic acid distribution analysis. A method has been developed that permits simultaneous cytometric determination of deoxyribonucleic acid and acid phosphatase activity in the cell cycle compartments of prostatic biopsy specimens. Histograms of prostatic carcinoma reveal higher acid phosphatase activity and greater deoxyribonucleic acid content in the S and S + G2/M populations than the histograms representing benign lesions. This compartmental difference may have prognostic usefulness.

Topics: Acid Phosphatase; Biopsy; DNA; DNA, Neoplasm; Flow Cytometry; Humans; Male; Prostate; Prostatic Diseases; Prostatic Neoplasms

Acid phosphatase in serum was measured in 116 patients with prostatic disease, benign in 59 and malignant in 57 cases. Comparisons were made between radioimmunoassay (RIA) and an enzymatic method. The correlation coefficient between the respective values was 0.96 in patients with untreated prostatic cancer, indicating that no significant difference between results with the two methods was to be expected. The correlation coefficient between RIA values and cancer stage was 0.48, and between catalytic activity and cancer stage it was 0.50. The validity of the two methods consequently was equal. RIA, however, was the more sensitive method, giving elevated values in 10 of 11 patients with untreated stage III or stage IV prostatic cancer, as compared with only 4 of the same 11 in the enzymatic assay. This seeming paradox most probably was attributable to differing intrinsic properties of the methods when the upper limits of normal range were established. Neither RIA nor enzymatic analysis discriminated early prostatic cancer (stages I and II) from benign lesions.

Topics: Acid Phosphatase; Aged; Humans; Male; Middle Aged; Prostatic Diseases; Prostatic Neoplasms; Radioimmunoassay

Topics: Acid Phosphatase; Clinical Enzyme Tests; Humans; Kidney; Kidney Diseases; Male; Organ Specificity; Prostate; Prostatic Diseases

Topics: Acid Phosphatase; Adult; Aged; Clinical Enzyme Tests; Female; Humans; Male; Middle Aged; Prostate; Prostatic Diseases; Prostatic Neoplasms; Radioimmunoassay

Topics: Acid Phosphatase; Adolescent; Adult; Aged; Child; Clinical Enzyme Tests; Evaluation Studies as Topic; Humans; Male; Middle Aged; Prostate; Prostatic Diseases; Prostatic Neoplasms; Radioimmunoassay

Topics: Acid Phosphatase; Adolescent; Adult; Age Factors; Aged; Child; Child, Preschool; Clinical Enzyme Tests; Cross Reactions; Female; Humans; Immunoenzyme Techniques; Infant; Isoenzymes; Liver; Male; Middle Aged; Prostate; Prostatic Diseases; Prostatic Hyperplasia; Puberty; Radioimmunoassay; Reference Values; Tissue Distribution

A prospective study comparing a new radioimmunologic and a classical enzymatic assay for prostatic acid phosphatase was done to evaluate their respective roles in patients with prostatic diseases. We studied 50 patients with cancer of the prostate, 101 with benign prostatic hypertrophy and 17 with prostatitis as well as patients with nonprostatic malignancy, and various hematological and bone diseases. The results showed a low incidence of elevated values in patients with early cancer of the prostate and a high incidence of false positive values with the radioimmunoassay in patients with benign prostatic diseases, especially prostatitis. These data suggest that tests for serum prostatic acid phosphatase levels remain disappointing in the assessment of prostatic disease regardless of the technique used.

Topics: Acid Phosphatase; Aged; False Positive Reactions; Humans; Male; Prospective Studies; Prostatic Diseases; Prostatic Hyperplasia; Prostatic Neoplasms; Prostatitis; Radioimmunoassay

In this assay we used polystyrene-tube-attached rabbit antibodies against prostatic acid phosphatase (PAP) that had been purified to homogeneity from human prostate. The amount of immunoreactive acid phosphatase was determined directly by its enzymic activity in the solid-phase-bound immune complex. The detection limit was 0.05 U/L (0.13 microgram/L), the CVs between 4.3 and 10.8%. Investigating the organ specificity of PAP, we found that some cross-reacting acid phosphatase activity could be so measured in human kidney, leukocytes, and platelets, all of which probably contribute to the circulating "prostatic" acid phosphatase that normally is present in serum. Diurnal and day-to-day variations in serum PAP activity were as much as 100% in healthy subjects. Individuals without prostatic diseases (n = 92) had values for serum PAP activity up to 0.36 U/L (0.94 microgram/L), in an age-independent distribution; patients with benign prostatic hyperplasia (n = 62) showed values up to 0.48 U/L (1.25 micrograms/L). With PAP activity of 0.38 U/L or 1.0 microgram/L (90th percentile of the prostatic group) as the upper limit of "normality," overall sensitivity (stages A-D) for detection of prostatic cancer in 33 essentially untreated patients was 65%. Examples for the followup of therapy of prostatic cancer by measurement of serum PAP with this assay are described.

Topics: Acid Phosphatase; Adolescent; Adult; Aged; Blood Platelets; Cross Reactions; Evaluation Studies as Topic; Humans; Immunoenzyme Techniques; Kidney; Leukocytes; Male; Middle Aged; Prostate; Prostatic Diseases; Reference Values

Topics: Acid Phosphatase; Aged; Female; Humans; Male; Prostate; Prostatic Diseases; Radioimmunoassay

Topics: Acid Phosphatase; Adult; Aged; Evaluation Studies as Topic; Female; Humans; Male; Middle Aged; Prostate; Prostatic Diseases; Prostatic Neoplasms; Radioimmunoassay; Reagent Kits, Diagnostic

Topics: Acid Phosphatase; Adult; Aged; Female; Humans; Male; Prostate; Prostatic Diseases; Radioimmunoassay; Reagent Kits, Diagnostic

282 human prostatic fluid samples have been investigated for their pH value, zinc, and citrate concentration and their acid phosphatase, leucine aminopeptidase, diamine oxidase, and beta-glucuronidase activities. The results have been analysed in terms of the clinical status of the patients. Significant differences between patient categories were found with all but diamine oxidase and beta-glucuronidase. These differences were mainly found between men with apparently healthy prostates and prostatitis patients; the pH being raised and the acid phosphatase, leucine aminopeptidase, zinc and citrate being reduced. The diagnostic value of these parameters was evaluated, each could be used to classify correctly 90% of patients from these 2 groups. Zinc, citrate and leucine aminopeptidase showed no age relationship and were better than acid phosphatase and pH in discriminating between BPH and prostatitis. Evidence was also found for a return of normal secretory function sometime after an episode of prostatitis. Zinc and citrate are likely to be the most useful parameters for clinical evaluation.

Topics: Acid Phosphatase; Age Factors; Citrates; Citric Acid; Humans; Hydrogen-Ion Concentration; Leucyl Aminopeptidase; Male; Prostate; Prostatic Diseases; Semen; Zinc

Topics: Acid Phosphatase; Female; Humans; Male; Prostate; Prostatic Diseases; Prostatic Hyperplasia; Radioimmunoassay

Topics: Acid Phosphatase; Clinical Enzyme Tests; Humans; Male; Massage; Palpation; Prostatic Diseases; Prostatic Hyperplasia; Prostatitis

Topics: Acid Phosphatase; Body Fluids; Carcinoma; Humans; L-Lactate Dehydrogenase; Male; Polyamines; Prostate; Prostatic Diseases; Prostatic Hyperplasia; Prostatic Neoplasms; Proteins

Topics: Acid Phosphatase; Humans; Male; Physical Examination; Prostatic Diseases

The availability of a radioimmunoassay for prostate-specific acid phosphatase has allowed a correlative study between this technique and conventional colorimetric assays in the four clinical stages of prostatic adenocarcinoma. Results of such a study show an increased diagnostic sensitivity of the radioimmunoassay in all stages, but in 14% of Stage IV adenocarcinomas there was no increase in prostatic acid phosphatase above the ranges ordinarily expected for all methods. In cases of benign prostatic hyperplasia, there was an increase associated with in vivo tissue cytolysis, comparable to Stage II and III adenocarcinoma. The sensitivity of the test in Stage I is still low, but testing for combinations of tumor markers might increase the diagnostic yield. Conversely, a different clinical approach might be to establish baseline values in the "at-risk" patient, followed by regular determinations of prostate-specific acid phosphatase activity. Increases in activity within the normal expected range may be interpreted by the clinician as a herald of disease.

Topics: Acid Phosphatase; Adult; Age Factors; Aged; Clinical Enzyme Tests; Colorimetry; Female; Humans; Male; Middle Aged; Prostate; Prostatic Diseases; Radioimmunoassay; Reference Values; Sex Factors

We purified human prostatic acid phosphatase (hPAP) from prostatic tissues by affinity chromatography, DEAE cellulose and gel filtration and also examined physicochemical properties of highly purified PAP. We developed a double-antibody radioimmunoassay for hPAP in serum, with use of antiserum raised in rabbit against highly purified PAP. The antiserum did not cross react with acid phosphatase from platelets and red blood cells. Experimental detail are outlined to assess the reproducibility and reliability of the method under various conditions. The upper limit of the serum PAP levels in the present assay was set at 3.0 ng/ml by 162 determinations of samples. The serum PAP levels of 2 untreated patients with prostatic carcinoma were higher than 3.0 ng/ml and 39 patients with benign prostatic hyperplasia were an average value of 1.9 ng/ml.

Topics: Acid Phosphatase; Adult; Chemical Phenomena; Chemistry, Physical; Female; Humans; Male; Middle Aged; Prostate; Prostatic Diseases; Radioimmunoassay

Prostatic acid phosphatase from human seminal fluid was purified to homogeneity. The enzyme was characterized as to its purity, molecular weight and amino acid composition. Analytical isoelectric focusing of purified enzyme on polyacrylamide gels resolved the enzyme activity into eleven discrete bands, apparently due to various amounts of sialic acid associated with the glycoprotein. Antisera raised against the purified enzyme produced only one precipitan arc on immunoelectrophoresis. A double antibody radioimmune assay was developed and used to evaluate serum prostatic acid phosphatase in 226 patients without prostatic disease, in 186 patients with benign prostatic hyperplasia and in 93 patients with prostatic carcinoma. No statistical difference was noted in serum prostatic acid phosphatase between patients with benign prostatic hyperplasia and in those without prostatic disease Serum prostatic acid phosphatase was elevated in 94% of the patients with metastatic prostatic carcinoma. Significant elevations were also found in carcinoma patients without metastases.

Topics: Acid Phosphatase; Amino Acids; Carcinoma; Humans; Hydrogen-Ion Concentration; Male; Molecular Weight; Prostate; Prostatic Diseases; Prostatic Hyperplasia; Prostatic Neoplasms; Radioimmunoassay; Semen

The minor enzyme of human prostatic acid phosphatases (pI 5.5) with high specific activity (orthophosphoric monoester phosphohydrolase, acid optimum, EC 3.1.3.2) has been purified for the first time as a pure enzyme protein. The enzyme was a single protein when examined by polyacrylamide gel electrophoresis and isotachophoresis. The specific activity was 1080 micromole per (min X mg) for hydrolysis of 5.5 mmole per liter of p-nitrophenylphosphate at pH 4.8 and 37 C. The purification coefficient was 540 and the recovery of enzyme activity was 2 per cent. The molecular weight of the enzyme subunit when measured by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate was 54,000. The Km of the purified enzyme was 3 X 10(-4) mole per liter for p-nitrophenylphosphate. An antiserum to this enzyme was prepared. The enzyme was cross-reactive with the main enzyme (pI 4.9) of human prostatic acid phosphatases in immunoelectrophoresis. No precipitin arc with the acid phosphatase in the serum of a prostatic carcinoma patient could be shown. Antiserum to the main enzyme caused a precipitin line with the same serum sample.

Topics: Acid Phosphatase; Electrophoresis, Polyacrylamide Gel; Humans; Immune Sera; Immunoelectrophoresis; Male; Methods; Prostate; Prostatic Diseases

Topics: Acid Phosphatase; Adult; Animals; Antibody Specificity; Female; Humans; Immune Sera; Male; Prostate; Prostatic Diseases; Rabbits

The authors have evaluated a new kinetic acid phosphatase method in which the substrate is alpha-naphthyl phosphate. The original claim that this substrate was highly specific for the prostatic isozyme has been strongly challenged. Therefore, large numbers of patients in the following groupings were included in the evaluation: 52 urology clinic patients, 17 patients with uremia, 11 patients with multiple myeloma and 231 patients who had undergone prostatic biopsies. Two hundred seventy of these patients were found to be free of prostatic cancer. Of these, seven had acid phosphatase values above the upper limit of normal. Five of these seven patients had diagnoses of fibromuscular glandular hyperplasia. One was a woman who had multiple myeloma, and one was a uremic patient. Fifteen of 17 patients who had metastatic cancer of the prostate had elevated acid phosphatase activities, whereas one of 24 patients who had cancer of the prostate but no evidence of metastases had an elevated value.

Topics: Acid Phosphatase; Adolescent; Adult; Clinical Enzyme Tests; Female; Humans; Kinetics; Male; Middle Aged; Naphthalenes; Neoplasm Metastasis; Organophosphorus Compounds; Prospective Studies; Prostate; Prostatic Diseases; Prostatic Neoplasms; Retrospective Studies

A clinical investigation was carried out to analyze the frequency of elevated serum acid phosphatase (SAP) levels after ejaculation and needle biopsy of the prostate gland. Major mechanical manipulative procedures such as needle biopsy caused marked acute elevations in SAP levels but return to normal within twenty-four hours. It is demonstrated that SAP levels remained essentially unchanged after ejaculation. It has been previously shown that procedures such as prostatic massage, catheterization, and endoscopic examination normally do not elicit abnormal SAP levels. Hence any elevation of SAP warrants further evaluation for serious urologic disease.

Topics: Acid Phosphatase; Biopsy, Needle; Clinical Enzyme Tests; Ejaculation; Humans; Male; Prostate; Prostatic Diseases; Time Factors

Topics: Acid Phosphatase; Arginine; Castration; Clomiphene; Cyproterone; Estriol; Estrone; Glucuronates; Humans; Hypertrophy; Male; Prostate; Prostatic Diseases; Testis; Testosterone

Topics: Acid Phosphatase; Adenocarcinoma; Biopsy, Needle; Catheterization; Cystoscopy; Dilatation; Endoscopy; Humans; Male; Massage; Physical Examination; Prostate; Prostatectomy; Prostatic Diseases; Prostatic Hyperplasia; Prostatic Neoplasms; Rectum; Urethra; Urinary Bladder Neoplasms

Topics: Acid Phosphatase; Aged; Alkaline Phosphatase; Biopsy; Biopsy, Needle; Bone Marrow Examination; Castration; Cryosurgery; Humans; Male; Middle Aged; Neoplasm Metastasis; Palliative Care; Prostatectomy; Prostatic Diseases; Prostatic Hyperplasia; Prostatic Neoplasms; Prostatitis; Radiography, Thoracic; Radionuclide Imaging; Steroids

Topics: Acid Phosphatase; Alkaline Phosphatase; Amylases; Biliary Tract Diseases; Bone Diseases; Clinical Enzyme Tests; Creatine Kinase; Enzymes; Humans; Isoenzymes; Liver Diseases; Male; Muscular Diseases; Myocardial Infarction; Nervous System Diseases; Organ Specificity; Oxidoreductases; Pancreatic Diseases; Prostatic Diseases; Pulmonary Embolism; Transaminases

Topics: Acid Phosphatase; Biliary Tract Diseases; Blood Platelets; Bone and Bones; Breast Neoplasms; Erythrocytes; False Positive Reactions; Female; Formaldehyde; Humans; Hydrogen-Ion Concentration; Kidney; Kidney Diseases; Liver; Liver Diseases; Male; Neoplasms; Phenolphthaleins; Phosphates; Prostate; Prostatic Diseases; Prostatic Neoplasms; Tartrates

Topics: Acid Phosphatase; Humans; Infarction; Male; Prostatic Diseases

Topics: Acid Phosphatase; Blood Platelets; Breast Neoplasms; Buffers; Citrates; Cystic Fibrosis; Female; Heart Failure; Humans; Hydrogen-Ion Concentration; Kidney Failure, Chronic; Male; Phosphates; Prostate; Prostatic Diseases; Prostatic Neoplasms; Spectrophotometry; Stomach Neoplasms

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Histocytochemistry; Humans; Hyperplasia; Male; Microscopy, Electron; Prostate; Prostatic Diseases

Topics: Acid Phosphatase; Histocytochemistry; Humans; Hyperplasia; In Vitro Techniques; Male; Microscopy, Electron; Nucleotidases; Prostatic Diseases

Topics: Acid Phosphatase; Alkaline Phosphatase; Diagnosis, Differential; Humans; Male; Neoplasms; Physical Examination; Prostatic Diseases; Prostatic Hyperplasia; Prostatic Neoplasms

Topics: Acid Phosphatase; Alkaline Phosphatase; Diagnosis, Differential; Humans; Male; Neoplasms; Physical Examination; Prostatic Diseases; Prostatic Hyperplasia; Prostatic Neoplasms

Topics: Acid Phosphatase; Diagnosis, Differential; Humans; Male; Neoplasms; Physical Examination; Prostatic Diseases; Prostatic Hyperplasia; Prostatic Neoplasms

Topics: Acid Phosphatase; Blood Chemical Analysis; Diagnosis, Differential; Humans; Male; Mucoproteins; Neoplasms; Orosomucoid; Prostatectomy; Prostatic Diseases; Prostatic Hyperplasia; Prostatic Neoplasms; Tyrosine

Topics: Acid Phosphatase; Disease; Humans; Male; Phosphoric Monoester Hydrolases; Prostate; Prostatic Diseases; Urology

Topics: Acid Phosphatase; Disease; Humans; Male; Phosphoric Monoester Hydrolases; Prostate; Prostatic Diseases

Topics: Acid Phosphatase; Disease; Gaucher Disease; Humans; Lipidoses; Male; Phosphoric Monoester Hydrolases; Prostate; Prostatic Diseases; Prostatism

Topics: Acid Phosphatase; Body Fluids; Chronic Disease; Disease; Humans; Male; Peptide Hydrolases; Prostate; Prostatic Diseases; Prostatitis